Scholars@Duke
Harold Paul Erickson

Harold Paul Erickson

James B. Duke Distinguished Professor Emeritus of Cell Biology
Cell Biology
h.erickson@duke.edu
Duke Box 3709, Durham, NC 27710
x, Durham, NC 27710

Selected Publications

Recently Designed Multivalent Spike Binders Cannot Bind Multivalently─How Do They Achieve Enhanced Avidity to SARS-CoV-2?

Journal Article Biochemistry · January 17, 2023 The trimeric spike protein of SARS-CoV-2 has been targeted by antibody mimics that bind near or at the receptor-binding domain to neutralize the virus. Several independent studies have reported enhanced binding avidity for dimers and trimers, where binding ... Full text Open Access Link to item Cite

FtsZ at mid-cell is essential in Escherichia coli until the late stage of constriction.

Journal Article Microbiology (Reading) · June 2022 There has been recent debate as to the source of constriction force during cell division. FtsZ can generate a constriction force on tubular membranes in vitro, suggesting it may generate the constriction force in vivo. However, another study showed that mu ... Full text Open Access Link to item Cite

Progress and Challenges in the Biology of FNDC5 and Irisin.

Journal Article Endocr Rev · July 16, 2021 In 2002, a transmembrane protein-now known as FNDC5-was discovered and shown to be expressed in skeletal muscle, heart, and brain. It was virtually ignored for 10 years, until a study in 2012 proposed that, in response to exercise, the ectodomain of skelet ... Full text Open Access Link to item Cite

The Arabidopsis thaliana chloroplast division protein FtsZ1 counterbalances FtsZ2 filament stability in vitro.

Journal Article J Biol Chem · 2021 Bacterial cell and chloroplast division are driven by a contractile "Z ring" composed of the tubulin-like cytoskeletal GTPase FtsZ. Unlike bacterial Z rings, which consist of a single FtsZ, the chloroplast Z ring in plants is composed of two FtsZ proteins, ... Full text Open Access Link to item Cite

How Teichoic Acids Could Support a Periplasm in Gram-Positive Bacteria, and Let Cell Division Cheat Turgor Pressure.

Journal Article Front Microbiol · 2021 The cytoplasm of bacteria is maintained at a higher osmolality than the growth medium, which generates a turgor pressure. The cell membrane (CM) cannot support a large turgor, so there are two possibilities for transferring the pressure to the peptidoglyca ... Full text Open Access Link to item Cite

A Unified Model for Treadmilling and Nucleation of Single-Stranded FtsZ Protofilaments.

Journal Article Biophys J · August 18, 2020 Bacterial cell division is tightly coupled to the dynamic behavior of FtsZ, a tubulin homolog. Recent experimental work in vitro and in vivo has attributed FtsZ's assembly dynamics to treadmilling, in which subunits add to the bottom and dissociate from th ... Full text Open Access Link to item Cite

High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP.

Journal Article Acta Crystallogr F Struct Biol Commun · February 1, 2020 Bacterial cytokinesis is mediated by the Z-ring, which is formed by the prokaryotic tubulin homolog FtsZ. Recent data indicate that the Z-ring is composed of small patches of FtsZ protofilaments that travel around the bacterial cell by treadmilling. Treadm ... Full text Open Access Link to item Cite

L form bacteria growth in low-osmolality medium.

Journal Article Microbiology (Reading) · August 2019 L form bacteria do not have a cell wall and are thought to require medium of high osmolality for survival and growth. In this study we tested whether L forms can adapt to growth in lower osmolality medium. We first tested the Escherichia coli L form NC-7, ... Full text Open Access Link to item Cite

Determinants of Tenascin-C and HIV-1 envelope binding and neutralization.

Journal Article Mucosal Immunol · July 2019 Interactions between innate antiviral factors at mucosal surfaces and HIV-1 virions contribute to the natural inefficiency of HIV-1 transmission and are a platform to inform the development of vaccine and nonvaccine strategies to block mucosal HIV-1 transm ... Full text Link to item Cite

Microtubule Assembly from Single Flared Protofilaments-Forget the Cozy Corner?

Journal Article Biophys J · June 18, 2019 A paradigm shift for models of MT assembly is suggested by a recent cryo-electron microscopy study of microtubules (MTs). Previous assembly models have been based on the two-dimensional lattice of the MT wall, where incoming subunits can add with longitudi ... Full text Open Access Link to item Cite

The cell division protein MinD from Pseudomonas aeruginosa dominates the assembly of the MinC-MinD copolymers.

Journal Article J Biol Chem · May 18, 2018 Cell division of rod-shaped bacteria requires the Z ring, a ring of FtsZ filaments associated with the inner-membrane wall. The MinCDE proteins help localize the Z ring to the center of the Escherichia coli cell. MinC, which inhibits Z-ring assembly, is a ... Full text Open Access Link to item Cite

Turgor Pressure and Possible Constriction Mechanisms in Bacterial Division.

Journal Article Front Microbiol · 2018 Bacterial cytokinesis begins with the assembly of FtsZ into a Z ring at the center of the cell. The Z-ring constriction in Gram-negative bacteria may occur in an environment where the periplasm and the cytoplasm are isoosmotic, but in Gram-positive bacteri ... Full text Open Access Link to item Cite

Vaccine Induction of Heterologous Tier 2 HIV-1 Neutralizing Antibodies in Animal Models.

Journal Article Cell Rep · December 26, 2017 The events required for the induction of broad neutralizing antibodies (bnAbs) following HIV-1 envelope (Env) vaccination are unknown, and their induction in animal models as proof of concept would be critical. Here, we describe the induction of plasma ant ... Full text Link to item Cite

Fibronectin Conformation and Assembly: Analysis of Fibronectin Deletion Mutants and Fibronectin Glomerulopathy (GFND) Mutants.

Journal Article Biochemistry · August 29, 2017 To study fibronectin (FN) conformation and assembly, we generated several deletion mutants: FNΔI1-5, FNΔIII1-3, FNΔIII4-8, and FNΔIII11-14. A monomeric form, FNmono, which lacked the C-terminal dimerization region, was also created. FNtnA-D was generated b ... Full text Open Access Link to item Cite

How bacterial cell division might cheat turgor pressure - a unified mechanism of septal division in Gram-positive and Gram-negative bacteria.

Journal Article Bioessays · August 2017 An important question for bacterial cell division is how the invaginating septum can overcome the turgor force generated by the high osmolarity of the cytoplasm. I suggest that it may not need to. Several studies in Gram-negative bacteria have shown that t ... Full text Open Access Link to item Cite

ZipA and FtsA* stabilize FtsZ-GDP miniring structures.

Journal Article Sci Rep · June 16, 2017 The cytokinetic division ring of Escherichia coli comprises filaments of FtsZ tethered to the membrane by FtsA and ZipA. Previous results suggested that ZipA is a Z-ring stabilizer, since in vitro experiments it is shown that ZipA enhanced FtsZ assembly an ... Full text Open Access Link to item Cite

The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red Alga Galdieria sulphuraria Co-assemble into Dynamic Filaments.

Journal Article J Biol Chem · March 31, 2017 FtsZ is a homolog of eukaryotic tubulin and is present in almost all bacteria and many archaea, where it is the major cytoskeletal protein in the Z ring, required for cell division. Unlike some other cell organelles of prokaryotic origin, chloroplasts have ... Full text Open Access Link to item Cite

Protein unfolding under isometric tension-what force can integrins generate, and can it unfold FNIII domains?

Journal Article Curr Opin Struct Biol · February 2017 Extracellular matrix fibrils of fibronectin (FN) are highly elastic, and are typically stretched three to four times their relaxed length. The mechanism of stretching has been controversial, in particular whether it involves tension-induced unfolding of FN ... Full text Open Access Link to item Cite

The discovery of the prokaryotic cytoskeleton: 25th anniversary.

Journal Article Mol Biol Cell · February 1, 2017 The year 2017 marks the 25th anniversary of the discovery of homologues of tubulin and actin in prokaryotes. Before 1992, it was largely accepted that tubulin and actin were unique to eukaryotes. Then three laboratories independently discovered that FtsZ, ... Full text Open Access Link to item Cite

Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.

Journal Article J Biol Chem · January 20, 2017 Globular proteins are not permanently folded but spontaneously unfold and refold on time scales that can span orders of magnitude for different proteins. A longstanding debate in the protein-folding field is whether unfolding rates or folding rates correla ... Full text Open Access Link to item Cite

Probing for Binding Regions of the FtsZ Protein Surface through Site-Directed Insertions: Discovery of Fully Functional FtsZ-Fluorescent Proteins.

Journal Article J Bacteriol · January 1, 2017 UNLABELLED: FtsZ, a bacterial tubulin homologue, is a cytoskeletal protein that assembles into protofilaments that are one subunit thick. These protofilaments assemble further to form a "Z ring" at the center of prokaryotic cells. The Z ring generates a co ... Full text Open Access Link to item Cite

Whole genome re-sequencing to identify suppressor mutations of mutant and foreign Escherichia coli FtsZ.

Journal Article PLoS One · 2017 FtsZ is an essential protein for bacterial cell division, where it forms the cytoskeletal scaffold and may generate the constriction force. We have found previously that some mutant and foreign FtsZ that do not complement an ftsZ null can function for cell ... Full text Open Access Link to item Cite

FtsZ Constriction Force - Curved Protofilaments Bending Membranes.

Journal Article Subcell Biochem · 2017 FtsZ assembles in vitro into protofilaments (pfs) that are one subunit thick and ~50 subunits long. In vivo these pfs assemble further into the Z ring, which, along with accessory division proteins, constricts to divide the cell. We have reconstituted Z ri ... Full text Open Access Link to item Cite

FtsZ Protofilament Curvature Is the Opposite of Tubulin Rings.

Journal Article Biochemistry · July 26, 2016 FtsZ protofilaments (pfs) form the bacterial cytokinetic Z ring. Previous work suggested that a conformational change from straight to curved pfs generated the constriction force. In the simplest model, the C-terminal membrane tether is on the outside of t ... Full text Open Access Link to item Cite

How the kinetochore couples microtubule force and centromere stretch to move chromosomes.

Journal Article Nat Cell Biol · April 2016 The Ndc80 complex (Ndc80, Nuf2, Spc24 and Spc25) is a highly conserved kinetochore protein essential for end-on anchorage to spindle microtubule plus ends and for force generation coupled to plus-end polymerization and depolymerization. Spc24/Spc25 at one ... Full text Open Access Link to item Cite

The Presence and Anti-HIV-1 Function of Tenascin C in Breast Milk and Genital Fluids.

Journal Article PLoS One · 2016 Tenascin-C (TNC) is a newly identified innate HIV-1-neutralizing protein present in breast milk, yet its presence and potential HIV-inhibitory function in other mucosal fluids is unknown. In this study, we identified TNC as a component of semen and cervica ... Full text Link to item Cite

FtsZ filament capping by MciZ, a developmental regulator of bacterial division.

Journal Article Proc Natl Acad Sci U S A · April 28, 2015 Cytoskeletal structures are dynamically remodeled with the aid of regulatory proteins. FtsZ (filamentation temperature-sensitive Z) is the bacterial homolog of tubulin that polymerizes into rings localized to cell-division sites, and the constriction of th ... Full text Open Access Link to item Cite

Irisin - a myth rather than an exercise-inducible myokine.

Journal Article Sci Rep · March 9, 2015 The myokine irisin is supposed to be cleaved from a transmembrane precursor, FNDC5 (fibronectin type III domain containing 5), and to mediate beneficial effects of exercise on human metabolism. However, evidence for irisin circulating in blood is largely b ... Full text Open Access Link to item Cite

Structural determinants of the interaction between the Haemophilus influenzae Hap autotransporter and fibronectin.

Journal Article Microbiology (Reading) · June 2014 Haemophilus influenzae is a Gram-negative cocco-bacillus that initiates infection by colonizing the upper respiratory tract. Hap is an H. influenzae serine protease autotransporter protein that mediates adherence, invasion and microcolony formation in assa ... Full text Link to item Cite

Gene product 0.4 increases bacteriophage T7 competitiveness by inhibiting host cell division.

Journal Article Proc Natl Acad Sci U S A · November 26, 2013 Bacteriophages take over host resources primarily via the activity of proteins expressed early in infection. One of these proteins, produced by the Escherichia coli phage T7, is gene product (Gp) 0.4. Here, we show that Gp0.4 is a direct inhibitor of the E ... Full text Open Access Link to item Cite

The structure of irisin reveals a novel intersubunit β-sheet fibronectin type III (FNIII) dimer: implications for receptor activation.

Journal Article J Biol Chem · November 22, 2013 Irisin was recently identified as a putative myokine that is induced by exercise. Studies suggest that it is produced by cleavage of the FNDC5 (fibronectin domain-containing protein 5) receptor; irisin corresponds to the extracellular receptor ectodomain. ... Full text Open Access Link to item Cite

Tenascin-C is an innate broad-spectrum, HIV-1-neutralizing protein in breast milk.

Journal Article Proc Natl Acad Sci U S A · November 5, 2013 Achieving an AIDS-free generation will require elimination of postnatal transmission of HIV-1 while maintaining the nutritional and immunologic benefits of breastfeeding for infants in developing regions. Maternal/infant antiretroviral prophylaxis can redu ... Full text Open Access Link to item Cite

Irisin and FNDC5 in retrospect: An exercise hormone or a transmembrane receptor?

Journal Article Adipocyte · October 1, 2013 FNDC5 (fibronectin domain-containing [protein] 5) was initially discovered and characterized by two groups in 2002. In 2011 FNDC5 burst into prominence as the parent of irisin, a small protein containing the fibronectin type III domain. Irisin was proposed ... Full text Open Access Link to item Cite

Rapid in vitro assembly of Caulobacter crescentus FtsZ protein at pH 6.5 and 7.2.

Journal Article J Biol Chem · August 16, 2013 FtsZ from most bacteria assembles rapidly in vitro, reaching a steady-state plateau in 5-10 s after addition of GTP. A recent study used a novel dynamic light-scattering technique to assay the assembly of FtsZ from Caulobacter crescentus (CcFtsZ) and repor ... Full text Open Access Link to item Cite

Liposome division by a simple bacterial division machinery.

Journal Article Proc Natl Acad Sci U S A · July 2, 2013 We previously reconstituted Z rings in tubular multilamellar liposomes with FtsZ-YFP-mts, where mts is a membrane-targeting amphiphilic helix. These reconstituted Z rings generated a constriction force but did not divide the thick-walled liposomes. Here we ... Full text Open Access Link to item Cite

The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide.

Journal Article Mol Microbiol · July 2013 The tubulin homologue FtsZ provides the cytoskeletal framework and constriction force for bacterial cell division. FtsZ has an 50-amino-acid (aa) linker between the protofilament-forming globular domain and the C-terminal (Ct) peptide that binds FtsA and Z ... Full text Open Access Link to item Cite

Bacterial actin homolog ParM: arguments for an apolar, antiparallel double helix.

Journal Article J Mol Biol · September 28, 2012 The bacterial actin homolog ParM has always been modeled as a polar filament, comprising two parallel helical strands, like actin itself. I present arguments here that ParM may be an apolar filament, in which the two helical strands are antiparallel. ... Full text Link to item Cite

Negative-stain electron microscopy of inside-out FtsZ rings reconstituted on artificial membrane tubules show ribbons of protofilaments.

Journal Article Biophys J · July 3, 2012 FtsZ, the primary cytoskeletal element of the Z ring, which constricts to divide bacteria, assembles into short, one-stranded filaments in vitro. These must be further assembled to make the Z ring in bacteria. Conventional electron microscopy (EM) has fail ... Full text Open Access Link to item Cite

SulA inhibits assembly of FtsZ by a simple sequestration mechanism.

Journal Article Biochemistry · April 10, 2012 We have investigated the inhibition by SulA of the assembly of Escherichia coli FtsZ. Using quantitative GTPase and fluorescence assays, we found that SulA inhibition resulted in an increase in the apparent critical concentration for FtsZ assembly. The inc ... Full text Open Access Link to item Cite

Fibronectin aggregation and assembly: the unfolding of the second fibronectin type III domain.

Journal Article J Biol Chem · November 11, 2011 The mechanism of fibronectin (FN) assembly and the self-association sites are still unclear and contradictory, although the N-terminal 70-kDa region ((I)1-9) is commonly accepted as one of the assembly sites. We previously found that (I)1-9 binds to superf ... Full text Open Access Link to item Cite

Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.

Journal Article J Biol Chem · July 29, 2011 Featured Publication Fibronectin (FN) is an extracellular matrix protein that is assembled into fibrils by cells during tissue morphogenesis and wound healing. FN matrix fibrils are highly elastic, but the mechanism of elasticity has been debated: it may be achieved by mechani ... Full text Open Access Link to item Cite

Inside-out Z rings--constriction with and without GTP hydrolysis.

Journal Article Mol Microbiol · July 2011 Featured Publication The bacterial tubulin homologue FtsZ forms a ring-like structure called the Z ring that drives cytokinesis. We showed previously that FtsZ-YFP-mts, which has a short amphipathic helix (mts) on its C terminus that inserts into the membrane, can assemble con ... Full text Open Access Link to item Cite

Conformational changes of FtsZ reported by tryptophan mutants.

Journal Article Biochemistry · May 31, 2011 Featured Publication E. coli FtsZ has no native tryptophan. We showed previously that the mutant FtsZ L68W gave a 2.5-fold increase in trp fluorescence when assembly was induced by GTP. L68 is probably buried in the protofilament interface upon assembly, causing the fluorescen ... Full text Open Access Link to item Cite

FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.

Journal Article Microbiol Mol Biol Rev · December 2010 Featured Publication FtsZ, a bacterial homolog of tubulin, is well established as forming the cytoskeletal framework for the cytokinetic ring. Recent work has shown that purified FtsZ, in the absence of any other division proteins, can assemble Z rings when incorporated inside ... Full text Open Access Link to item Cite

Cell division without FtsZ--a variety of redundant mechanisms.

Journal Article Mol Microbiol · October 2010 Featured Publication Full text Open Access Link to item Cite

Suprastructures and dynamic properties of Mycobacterium tuberculosis FtsZ.

Journal Article J Biol Chem · April 9, 2010 Featured Publication Tuberculosis causes the most death in humans by any bacterium. Drug targeting of bacterial cytoskeletal proteins requires detailed knowledge of the various filamentous suprastructures and dynamic properties. Here, we have investigated by high resolution el ... Full text Link to item Cite

Curved FtsZ protofilaments generate bending forces on liposome membranes.

Journal Article EMBO J · November 18, 2009 Featured Publication We have created FtsZ-YFP-mts where an amphipathic helix on the C-terminus tethers FtsZ to the membrane. When incorporated inside multi-lamellar tubular liposomes, FtsZ-YFP-mts can assemble Z rings that generate a constriction force. When added to the outsi ... Full text Open Access Link to item Cite

Structural determinants of autoproteolysis of the Haemophilus influenzae Hap autotransporter.

Journal Article Infect Immun · November 2009 Featured Publication Haemophilus influenzae is a gram-negative bacterium that initiates infection by colonizing the upper respiratory tract. The H. influenzae Hap autotransporter protein mediates adherence, invasion, and microcolony formation in assays with respiratory epithel ... Full text Link to item Cite

BtubA-BtubB heterodimer is an essential intermediate in protofilament assembly.

Journal Article PLoS One · September 29, 2009 Featured Publication BACKGROUND: BtubA and BtubB are two tubulin-like genes found in the bacterium Prosthecobacter. Our work and a previous crystal structure suggest that BtubB corresponds to alpha-tubulin and BtubA to beta-tubulin. A 1:1 mixture of the two proteins assembles ... Full text Link to item Cite

FtsZ filament dynamics at steady state: subunit exchange with and without nucleotide hydrolysis.

Journal Article Biochemistry · July 21, 2009 Featured Publication We have measured three aspects of FtsZ filament dynamics at steady state: rates of GTP hydrolysis, subunit exchange between protofilaments, and disassembly induced by dilution or excess GDP. All three reactions were slowed with an increase in the potassium ... Full text Link to item Cite

Modeling the physics of FtsZ assembly and force generation.

Journal Article Proc Natl Acad Sci U S A · June 9, 2009 Featured Publication The tubulin homolog FtsZ is the major cytoskeletal protein in bacterial cytokinesis. It can generate a constriction force on the bacterial membrane or inside tubular liposomes. Several models have recently been proposed for how this force might be generate ... Full text Link to item Cite

Transient opening of fibronectin type III (FNIII) domains: the interaction of the third FNIII domain of FN with anastellin.

Journal Article Biochemistry · May 19, 2009 Featured Publication We previously reported that the fibronectin (FN) type III domains of FN may unfold to interact with anastellin and form FN aggregates. In the present study, we have focused on the interaction between anastellin and the third FN type III domain (III3), whic ... Full text Link to item Cite

Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy.

Journal Article Biol Proced Online · May 15, 2009 Featured Publication An important part of characterizing any protein molecule is to determine its size and shape. Sedimentation and gel filtration are hydrodynamic techniques that can be used for this medium resolution structural analysis. This review collects a number of simp ... Full text Link to item Cite

FtsZ condensates: an in vitro electron microscopy study.

Journal Article Biopolymers · May 2009 Featured Publication In vivo cell division protein FtsZ from E. coli forms rings and spirals which have only been observed by low resolution light microscopy. We show that these suprastructures are likely formed by molecular crowding which is a predominant factor in prokaryoti ... Full text Link to item Cite

Revisiting the mystery of fibronectin multimers: the fibronectin matrix is composed of fibronectin dimers cross-linked by non-covalent bonds.

Journal Article Matrix Biol · April 2009 Featured Publication Fibronectin (FN) matrix fibrils have long been thought to be formed by disulfide-bonded FN multimers, although there is no direct evidence that they are covalently linked with each other. To understand the biochemical properties of these fibrils, we extrac ... Full text Link to item Cite

Display of cell surface sites for fibronectin assembly is modulated by cell adherence to (1)F3 and C-terminal modules of fibronectin.

Journal Article PLoS One · 2009 Featured Publication BACKGROUND: Fibronectin-null cells assemble soluble fibronectin shortly after adherence to a substrate coated with intact fibronectin but not when adherent to the cell-binding domain of fibronectin (modules (7)F3-(10)F3). Interactions of adherent cells wit ... Full text Open Access Link to item Cite

Chapter 1 - Tubular liposomes with variable permeability for reconstitution of FtsZ rings.

Journal Article Methods Enzymol · 2009 Featured Publication We have developed a system for producing tubular multilamellar liposomes that incorporate the protein FtsZ on the inside. We start with a mixture of spherical multilamellar liposomes with FtsZ initially on the outside. Shearing forces generated by applying ... Full text Open Access Link to item Cite

The coiled coils of cohesin are conserved in animals, but not in yeast.

Journal Article PLoS One · 2009 Featured Publication BACKGROUND: The SMC proteins are involved in DNA repair, chromosome condensation, and sister chromatid cohesion throughout Eukaryota. Long, anti-parallel coiled coils are a prominent feature of SMC proteins, and are thought to serve as spacer rods to provi ... Full text Link to item Cite

Reconstitution of contractile FtsZ rings in liposomes

Journal Article Chemtracts · June 1, 2008 FtsZ, a tubulin homolog, is the major protein involved in cell division in bacteria and archaea. FtsZ assembles along with a number of other proteins into the Z ring, which constricts to divide the cell. This investigation examined the nature of the FtsZ f ... Cite

Reconstitution of contractile FtsZ rings in liposomes.

Journal Article Science · May 9, 2008 FtsZ is a tubulin homolog and the major cytoskeletal protein in bacterial cell division. It assembles into the Z ring, which contains FtsZ and a dozen other division proteins, and constricts to divide the cell. We have constructed a membrane-targeted FtsZ ... Full text Link to item Cite

In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from Bacillus plasmids: evidence for a capping mechanism.

Journal Article J Biol Chem · March 28, 2008 Proteins with a weak sequence similarity to tubulin and FtsZ are expressed from large plasmids of Bacillus anthracis and Bacillus thuringiensis and are probably involved in plasmid segregation. Previously designated RepX and TubZ, we designate them here as ... Full text Link to item Cite

Synergistic actions of hematopoietic and mesenchymal stem/progenitor cells in vascularizing bioengineered tissues.

Journal Article PLoS One · 2008 Poor angiogenesis is a major road block for tissue repair. The regeneration of virtually all tissues is limited by angiogenesis, given the diffusion of nutrients, oxygen, and waste products is limited to a few hundred micrometers. We postulated that co-tra ... Full text Link to item Cite

Assembly dynamics of Mycobacterium tuberculosis FtsZ.

Journal Article J Biol Chem · September 21, 2007 We have investigated the assembly of FtsZ from Mycobacterium tuberculosis (MtbFtsZ). Electron microscopy confirmed the previous observation that MtbFtsZ assembled into long, two-stranded filaments at pH 6.5. However, we found that assembly at pH 7.2 or 7.7 ... Full text Link to item Cite

The RGD motif in fibronectin is essential for development but dispensable for fibril assembly.

Journal Article J Cell Biol · July 2, 2007 Featured Publication Fibronectin (FN) is secreted as a disulfide-bonded FN dimer. Each subunit contains three types of repeating modules: FN-I, FN-II, and FN-III. The interactions of alpha5beta1 or alphav integrins with the RGD motif of FN-III repeat 10 (FN-III10) are consider ... Full text Link to item Cite

Evolution of the cytoskeleton.

Journal Article Bioessays · July 2007 Featured Publication The eukaryotic cytoskeleton appears to have evolved from ancestral precursors related to prokaryotic FtsZ and MreB. FtsZ and MreB show 40-50% sequence identity across different bacterial and archaeal species. Here I suggest that this represents the limit o ... Full text Link to item Cite

An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins.

Journal Article Protein Sci · July 2007 Featured Publication We have experimentally studied the fluorescence resonance energy transfer (FRET) between green fluorescent protein (GFP) molecules by inserting folded or intrinsically unstructured proteins between CyPet and Ypet. We discovered that most of the enhanced FR ... Full text Link to item Cite

Designing an extracellular matrix protein with enhanced mechanical stability.

Journal Article Proc Natl Acad Sci U S A · June 5, 2007 The extracellular matrix proteins tenascin and fibronectin experience significant mechanical forces in vivo. Both contain a number of tandem repeating homologous fibronectin type III (fnIII) domains, and atomic force microscopy experiments have demonstrate ... Full text Link to item Cite

FtsZ from divergent foreign bacteria can function for cell division in Escherichia coli.

Journal Article J Bacteriol · October 2006 Featured Publication FtsZs from Mycoplasma pulmonis (MpuFtsZ) and Bacillus subtilis (BsFtsZ) are only 46% and 53% identical in amino acid sequence to FtsZ from Escherichia coli (EcFtsZ). In the present study we show that MpuFtsZ and BsFtsZ can function for cell division in E. ... Full text Link to item Cite

Sequence divergence of coiled coils--structural rods, myosin filament packing, and the extraordinary conservation of cohesins.

Journal Article J Struct Biol · May 2006 Featured Publication The amino acid sequences of the long, anti-parallel coiled coils of the cohesin subunits SMC1 and SMC3 are almost totally conserved in mammals. To understand this exceptional conservation more broadly, we analyzed amino acid sequence variation for several ... Full text Link to item Cite

Understanding the elasticity of fibronectin fibrils: unfolding strengths of FN-III and GFP domains measured by single molecule force spectroscopy.

Journal Article Matrix Biol · April 2006 While it is well established that fibronectin (FN) matrix fibrils are elastic, the mechanism of fibril elasticity during extension is still debated. To investigate the molecular origin of FN fibril elasticity, we used single molecule force spectroscopy (SM ... Full text Link to item Cite

Probing the domain structure of FtsZ by random truncation and insertion of GFP.

Journal Article Microbiology (Reading) · December 2005 Featured Publication Random transposon-mediated mutagenesis has been used to create truncations and insertions of green fluorescent protein (GFP), and Venus-yellow fluorescent protein (YFP), in Escherichia coli FtsZ. Sixteen unique insertions were obtained, and one of them, in ... Full text Link to item Cite

Domain unfolding plays a role in superfibronectin formation.

Journal Article J Biol Chem · November 25, 2005 Featured Publication Superfibronectin (sFN) is a fibronectin (FN) aggregate that is formed by mixing FN with anastellin, a fragment of the first type III domain of FN. However, the mechanism of this aggregation has not been clear. In this study, we found that anastellin co-pre ... Full text Link to item Cite

Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer.

Journal Article J Biol Chem · June 10, 2005 Featured Publication We have developed an assay for the assembly of FtsZ based on fluorescence resonance energy transfer (FRET). We mutated an innocuous surface residue to cysteine and labeled separate pools with fluorescein (donor) and tetramethylrhodamine (acceptor). When th ... Full text Link to item Cite

In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB.

Journal Article J Cell Biol · April 25, 2005 Featured Publication Arecent study identified genuine tubulin proteins, BtubA and BtubB, in the bacterial genus Prosthecobacter. We have expressed BtubA and BtubB in Escherichia coli and studied their in vitro assembly. BtubB by itself formed rings with an outer diameter of 35 ... Full text Link to item Cite

Mutants of FtsZ targeting the protofilament interface: effects on cell division and GTPase activity.

Journal Article J Bacteriol · April 2005 Featured Publication The bacterial cell division protein FtsZ assembles into straight protofilaments, one subunit thick, in which subunits appear to be connected by identical bonds or interfaces. These bonds involve the top surface of one subunit making extensive contact with ... Full text Link to item Cite

A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus.

Journal Article Biophys J · January 2005 Featured Publication FtsZ is the major cytoskeletal protein operating in bacterial cell division. FtsZ assembles into protofilaments in vitro, and there has been some controversy over whether the assembly is isodesmic or cooperative. Assembly has been assayed previously by sed ... Full text Link to item Cite

Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins.

Journal Article J Bacteriol · September 2004 Featured Publication FtsZ is the major cytoskeletal component of the bacterial cell division machinery. It forms a ring-shaped structure (the Z ring) that constricts as the bacterium divides. Previous in vivo experiments with green fluorescent protein-labeled FtsZ and fluoresc ... Full text Link to item Cite

Localization of a cryptic binding site for tenascin on fibronectin.

Journal Article J Biol Chem · July 2, 2004 Fibronectin and tenascin are large extracellular matrix proteins that interact with each other and with integrin receptors to regulate cell growth and movement. They are both modular proteins composed of independently folded domains (modules) that are arra ... Full text Link to item Cite

The disulfide bonding pattern in ficolin multimers.

Journal Article J Biol Chem · February 20, 2004 Featured Publication Ficolin is a plasma lectin, consisting of a short N-terminal multimerization domain, a middle collagen domain, and a C-terminal fibrinogen-like domain. The collagen domains assemble the subunits into trimers, and the N-terminal domain assembles four trimer ... Full text Link to item Cite

In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function.

Journal Article J Bacteriol · August 2003 Featured Publication We have characterized the in vivo phenotypes of 17 mutations of Escherichia coli ftsZ. In particular, we determined whether these mutations can complement a null ftsZ phenotype, and we demonstrated that two noncomplementing mutations show partial dominant- ... Full text Link to item Cite

Apparent cooperative assembly of the bacterial cell division protein FtsZ demonstrated by isothermal titration calorimetry.

Journal Article J Biol Chem · April 18, 2003 The assembly dynamics of FtsZ, a prokaryotic homolog of tubulin, are important for their role in bacterial cytokinesis. Here we used isothermal titration calorimetry (ITC) to measure the heat of FtsZ self-association under various conditions. The measureme ... Full text Link to item Cite

Macromolecular assemblages - Many structures to function

Journal Article Current Opinion in Structural Biology · April 1, 2003 Full text Cite

Force measurements of the alpha5beta1 integrin-fibronectin interaction.

Journal Article Biophys J · February 2003 The interaction of the alpha(5)beta(1) integrin and its ligand, fibronectin (FN), plays a crucial role in the adhesion of cells to the extracellular matrix. An important intrinsic property of the alpha(5)beta(1)/FN interaction is the dynamic response of th ... Full text Link to item Cite

Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain.

Journal Article J Bacteriol · August 2002 The cell division protein ZipA has an N-terminal transmembrane domain and a C-terminal globular domain that binds FtsZ. Between them are a charged domain and a P/Q domain rich in proline and glutamine that has been proposed to be an unfolded polypeptide. H ... Full text Link to item Cite

Tenascin-C expression and distribution in cultured human chondrocytes and chondrosarcoma cells.

Journal Article J Orthop Res · July 2002 Tenascin-C (TNC) is an oligomeric glycoprotein of the extracellular matrix with several distinct isoforms variably expressed during embryogenesis, tumorogenesis, angiogenesis and wound healing. In the normal human adult, TNC is found in large concentration ... Full text Link to item Cite

Trimers of the fibronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation.

Journal Article J Cell Sci · June 15, 2002 Previous studies have shown that small beads coated with FN7-10, a four-domain cell adhesion fragment of fibronectin, bind to cell surfaces and translocate rearward. Here we investigate whether soluble constructs containing two to five FN7-10 units might b ... Full text Link to item Cite

Trimers of the fivronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation

Journal Article Journal of Cell Science · June 15, 2002 Previous studies have shown that small beads coated with FN7-10, a four-domain cell adhesion fragment of fibronectin, bind to cell surfaces and translocate rearward. Here we investigate whether soluble constructs containing two to five FN7-10 units might b ... Full text Cite

The role of the specificity-determining loop of the integrin beta subunit I-like domain in autonomous expression, association with the alpha subunit, and ligand binding.

Journal Article Biochemistry · April 2, 2002 Integrin beta subunits contain a highly conserved I-like domain that is known to be important for ligand binding. Unlike integrin I domains, the I-like domain requires integrin alpha and beta subunit association for optimal folding. Pactolus is a novel gen ... Full text Link to item Cite

Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants.

Journal Article J Cell Sci · March 15, 2002 Featured Publication We have prepared 3T3 cells doubly labeled to visualize simultaneously the extracellular fibronectin (FN) matrix and intracellular actin cytoskeleton in living cell cultures. We used FN-yellow fluorescent protein (FN-yfp) for the FN matrix, and the actin-bi ... Full text Link to item Cite

Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching.

Journal Article Proc Natl Acad Sci U S A · March 5, 2002 Featured Publication FtsZ, the major cytoskeletal component of the bacterial cell-division machine, assembles into a ring (the Z-ring) that contracts at septation. FtsZ is a bacterial homolog of tubulin, with similar tertiary structure, GTP hydrolysis, and in vitro assembly. W ... Full text Link to item Cite

Condensin and cohesin display different arm conformations with characteristic hinge angles.

Journal Article J Cell Biol · February 4, 2002 Structural maintenance of chromosomes (SMC) proteins play central roles in higher-order chromosome dynamics from bacteria to humans. In eukaryotes, two different SMC protein complexes, condensin and cohesin, regulate chromosome condensation and sister chro ... Full text Link to item Cite

Stretching fibronectin.

Journal Article J Muscle Res Cell Motil · 2002 Featured Publication Fibronectin (FN) matrix fibrils assembled in cell culture have been observed to stretch in response to cell movements, and when broken relax to 1/3 to 1/4 of their rest length. Two molecular mechanisms have been proposed, for the elasticity. One proposes t ... Full text Link to item Cite

Disulfide-mediated dimerization of L1 Ig domains.

Journal Article J Neurosci Res · November 1, 2001 The neural cell adhesion molecule L1 contains immunoglobulin-like (Ig) domains in its extracellular region that mediate homophilic binding, neurite outgrowth and other activities relevant to CNS development. To correlate conformations of these domains to b ... Full text Link to item Cite

Structure of the Rad50 x Mre11 DNA repair complex from Saccharomyces cerevisiae by electron microscopy.

Journal Article J Biol Chem · October 5, 2001 The RAD50 gene of Saccharomyces cerevisiae is one of several genes required for recombinational repair of double-strand DNA breaks during vegetative growth and for initiation of meiotic recombination. Rad50 forms a complex with two other proteins, Mre11 an ... Full text Link to item Cite

Multiple conformations of PEVK proteins detected by single-molecule techniques.

Journal Article Proc Natl Acad Sci U S A · September 11, 2001 An important component of muscle elasticity is the PEVK region of titin, so named because of the preponderance of these amino acids. However, the PEVK region, similar to other elastomeric proteins, is thought to form a random coil and therefore its structu ... Full text Link to item Cite

Cytoskeleton. Evolution in bacteria.

Journal Article Nature · September 6, 2001 Full text Link to item Cite

Cytoskeleton. Evolution in bacteria.

Journal Article Nature · September 2001 Cite

Ultrastructure and function of dimeric, soluble intercellular adhesion molecule-1 (ICAM-1).

Journal Article J Biol Chem · August 3, 2001 Previous studies have demonstrated dimerization of intercellular adhesion molecule-1 (ICAM-1) on the cell surface and suggested a role for immunoglobulin superfamily domain 5 and/or the transmembrane domain in mediating such dimerization. Crystallization s ... Full text Link to item Cite

XMAP215 is a long thin molecule that does not increase microtubule stiffness.

Journal Article J Cell Sci · August 2001 XMAP215 is a microtubule associated protein that speeds microtubule plus end growth by seven- to tenfold and protects these ends from destabilization by the Kin I kinesin, XKCM1. To understand the mechanisms responsible for these activities, it is necessar ... Full text Link to item Cite

Bimodal activation of SMC ATPase by intra- and inter-molecular interactions.

Journal Article EMBO J · June 15, 2001 Structural maintenance of chromosomes (SMC) proteins play fundamental roles in higher-order chromosome dynamics from bacteria to humans. It has been proposed that the Bacillus subtilis SMC (BsSMC) homodimer is composed of two anti-parallel coiled-coil arms ... Full text Link to item Cite

Tenascin-C splice variant adhesive/anti-adhesive effects on chondrosarcoma cell attachment to fibronectin.

Journal Article Cell Struct Funct · June 2001 Tenascin-C is an oligomeric glycoprotein of the extracellular matrix that has been found to have both adhesive and anti-adhesive properties for cells. Recent elucidation of the two major TNC splice variants (320 kDa and 220 kDa) has shed light on the possi ... Full text Link to item Cite

Cell adhesion molecule L1 in folded (horseshoe) and extended conformations.

Journal Article Mol Biol Cell · June 2001 We have investigated the structure of the cell adhesion molecule L1 by electron microscopy. We were particularly interested in the conformation of the four N-terminal immunoglobulin domains, because x-ray diffraction showed that these domains are bent into ... Full text Link to item Cite

Site-specific mutations of FtsZ - Effects on GTPase and in vitro assembly

Journal Article BMC Microbiology · May 24, 2001 Background: FtsZ, the major cytoskeletal protein in bacterial cytokinesis, assembles in vitro into protofilaments, which can further associate into sheets, bundles or tubes. We have constructed 16 site-directed mutants of E. coli ftsZ, and tested them for ... Full text Cite

C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1.

Journal Article Nat Struct Biol · May 2001 Integrins are adhesion molecules that convey signals both to and from the cytoplasm across the plasma membrane. In resting cells, integrins in a low affinity state can be activated by 'inside-out signaling', in which signals affecting integrin heterodimer ... Full text Link to item Cite

Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?

Journal Article J Biol Chem · April 13, 2001 FtsZ is a bacterial homolog of tubulin that is essential for prokaryotic cytokinesis. In vitro, GTP induces FtsZ to assemble into straight, 5-nm-wide polymers. Here we show that the polymerization of these FtsZ filaments most closely resembles noncooperati ... Full text Link to item Cite

Plasma fibronectin supports neuronal survival and reduces brain injury following transient focal cerebral ischemia but is not essential for skin-wound healing and hemostasis.

Journal Article Nat Med · March 2001 Fibronectin performs essential roles in embryonic development and is prominently expressed during tissue repair. Two forms of fibronectin have been identified: plasma fibronectin (pFn), which is expressed by hepatocytes and secreted in soluble form into pl ... Full text Link to item Cite

The FtsZ protofilament and attachment of ZipA--structural constraints on the FtsZ power stroke.

Journal Article Curr Opin Cell Biol · February 2001 Bacterial cell division protein FtsZ forms protofilaments in vitro that can shift from a straight to a curved conformation. The inside of the curved protofilaments, which corresponds to the carboxyl terminus, should face the center of the cell as curvature ... Full text Link to item Cite

Site-specific mutations of FtsZ--effects on GTPase and in vitro assembly.

Journal Article BMC Microbiol · 2001 BACKGROUND: FtsZ, the major cytoskeletal protein in bacterial cytokinesis, assembles in vitro into protofilaments, which can further associate into sheets, bundles or tubes. We have constructed 16 site-directed mutants of E. coli ftsZ, and tested them for ... Full text Link to item Cite

The clinical significance of tenascin-C splice variant expression in chondrosarcoma.

Journal Article Oncology · 2001 OBJECTIVES: Tenascin-C (TNC) is an oligomeric glycoprotein of the extracellular matrix that is prominently expressed in malignant tumors. The purpose of this study was: (1) to determine the in vitro TNC splicing pattern in cultured human chondrocytes and c ... Full text Link to item Cite

XMAP215 is a long thin molecule that does not increase microtubule stiffness

Journal Article Journal of Cell Science · January 1, 2001 XMAP215 is a microtubule associated protein that speeds microtubule plus end growth by seven- to tenfold and protects these ends from destabilization by the Kin I kinesin, XKCM1. To understand the mechanisms responsible for these activities, it is necessar ... Full text Cite

Drosophila stretchin-MLCK is a novel member of the Titin/Myosin light chain kinase family.

Journal Article J Mol Biol · July 21, 2000 Members of the titin/myosin light chain kinase family play an essential role in the organization of the actin/myosin cytoskeleton, especially in sarcomere assembly and function. In Drosophila melanogaster, projectin is so far the only member of this family ... Full text Link to item Cite

Identification of amino acid sequences in fibrinogen gamma -chain and tenascin C C-terminal domains critical for binding to integrin alpha vbeta 3.

Journal Article J Biol Chem · June 2, 2000 Integrin alpha(v)beta(3) recognizes fibrinogen gamma and alpha(E) chain C-terminal domains (gammaC and alpha(E)C) but does not require the gammaC dodecapeptide sequence HHLGGAKQAGDV(400-411) for binding to gammaC. We have localized the alpha(v)beta(3) bind ... Full text Link to item Cite

Gamma-tubulin nucleation: template or protofilament?

Journal Article Nat Cell Biol · June 2000 Featured Publication Gamma-tubulin is known to nucleate microtubule assembly from alpha/beta-tubulin, but the molecular mechanism by which this process occurs is the subject of some controversy. Four recent papers have provided new structural and biochemical constraints on the ... Full text Link to item Cite

Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis.

Journal Article J Cell Biol · April 17, 2000 Featured Publication Fibronectin's RGD-mediated binding to the alpha5beta1 integrin is dramatically enhanced by a synergy site within fibronectin III domain 9 (FN9). Guided by the crystal structure of the cell-binding domain, we selected amino acids in FN9 that project in the ... Full text Link to item Cite

Ultrastructure and function of the fractalkine mucin domain in CX(3)C chemokine domain presentation.

Journal Article J Biol Chem · February 11, 2000 Fractalkine (FKN), a CX(3)C chemokine/mucin hybrid molecule on endothelium, functions as an adhesion molecule to capture and induce firm adhesion of a subset of leukocytes in a selectin- and integrin-independent manner. We hypothesized that the FKN mucin d ... Full text Link to item Cite

Straight and curved conformations of FtsZ are regulated by GTP hydrolysis.

Journal Article J Bacteriol · January 2000 FtsZ assembles in vitro into protofilaments that can adopt two conformations-the straight conformation, which can assemble further into two-dimensional protofilament sheets, and the curved conformation, which forms minirings about 23 nm in diameter. Here, ... Full text Link to item Cite

The straight and curved conformation of FtsZ protofilaments-evidence for rapid exchange of GTP into the curved protofilament.

Journal Article Cell Struct Funct · October 1999 Bacterial cell division protein FtsZ assembles into protofilaments, which can adopt a straight or curved conformation, similar to its eukaryotic homolog, tubulin. The straight protofilaments can assemble into sheets with a lattice similar to the microtubul ... Full text Link to item Cite

The compact conformation of fibronectin is determined by intramolecular ionic interactions.

Journal Article J Biol Chem · May 28, 1999 Fibronectin exists in a compact or extended conformation, depending upon environmental pH and salt concentration. Using recombinant fragments expressed in bacteria and baculovirus, we determined the domains responsible for producing fibronectin's compact c ... Full text Link to item Cite

Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein.

Journal Article Proc Natl Acad Sci U S A · March 2, 1999 Featured Publication Fibronectin (FN) forms the primitive fibrillar matrix in both embryos and healing wounds. To study the matrix in living cell cultures, we have constructed a cell line that secretes FN molecules chimeric with green fluorescent protein. These FN-green fluore ... Full text Link to item Cite

Macramolecular assemblages. Editorial overview

Journal Article Current Opinion in Structural Biology · January 1, 1999 Full text Cite

Oligomeric structure and tissue distribution of ficolins from mouse, pig and human.

Journal Article Arch Biochem Biophys · December 15, 1998 Featured Publication Mouse plasma ficolin was purified by GlcNAc affinity and anion-exchange chromatography. Gel-filtration chromatography and gradient sedimentation indicated that mouse plasma ficolin is a 12-mer of approximately 35 kDa subunits, and electron microscopy showe ... Full text Link to item Cite

Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin.

Journal Article J Biol Chem · November 27, 1998 Kinectin, an integral membrane protein (160 kDa), was identified as a kinesin-binding protein. Analysis of the predicted amino acid sequence of kinectin cDNA indicated an alpha-helical coiled-coil structure from amino acid 320 to 1310. A 120-kDa kinectin h ... Full text Link to item Cite

The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge.

Journal Article J Cell Biol · September 21, 1998 Featured Publication Structural maintenance of chromosomes (SMC) proteins function in chromosome condensation and several other aspects of DNA processing. They are large proteins characterized by an NH2-terminal nucleotide triphosphate (NTP)-binding domain, two long segments o ... Full text Link to item Cite

The molecular elasticity of the extracellular matrix protein tenascin.

Journal Article Nature · May 14, 1998 Extracellular matrix proteins are thought to provide a rigid mechanical anchor that supports and guides migrating and rolling cells. Here we examine the mechanical properties of the extracellular matrix protein tenascin by using atomic-force-microscopy tec ... Full text Link to item Cite

Utilization of a soluble integrin-alkaline phosphatase chimera to characterize integrin alpha 8 beta 1 receptor interactions with tenascin: murine alpha 8 beta 1 binds to the RGD site in tenascin-C fragments, but not to native tenascin-C.

Journal Article Biochemistry · April 21, 1998 The integrin alpha 8 beta 1 has been reported to bind to fibronectin, vitronectin, and tenascin-C in cell adhesion or neurite outgrowth assays. Here, we describe cDNA cloning of the murine alpha 8 subunit, purification of a recombinant soluble heterodimer ... Full text Link to item Cite

Mitogenic and adhesive effects of tenascin-C on human hematopoietic cells are mediated by various functional domains.

Journal Article Matrix Biol · April 1998 In the adult organism, the extracellular matrix molecule tenascin-C is prominently expressed in the bone marrow. Bone marrow mononuclear cells can adhere to plastic-immobilized tenascin-C, and in the present study we have used bacterial expression proteins ... Full text Link to item Cite

Atomic structures of tubulin and FtsZ.

Journal Article Trends Cell Biol · April 1998 The recently published atomic structures of tubulin and FtsZ are a research milestone. The N-terminal GTP-binding domains of tubulin and FtsZ are virtually identical in structure, as expected from the substantial sequence identity. Sequence identity is abs ... Full text Link to item Cite

Purification and assembly of FtsZ.

Journal Article Methods Enzymol · 1998 Full text Link to item Cite

Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain.

Journal Article Nat Struct Biol · January 1998 A novel off-resonance rotating-frame 15N NMR spin relaxation experiment is used to characterize conformational fluctuations with correlation times between 32 and 175 microseconds in the third fibronectin type III domain of human tenascin-C. Conformational ... Full text Link to item Cite

FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima--quantitation, GTP hydrolysis, and assembly.

Journal Article Cell Motil Cytoskeleton · 1998 We have cloned the ftsZ genes from Thermotoga maritima and Azotobacter vinelandii and expressed the proteins (TmFtsZ and AzFtsZ) in Escherichia coli. We compared these proteins to E. coli FtsZ (EcFtsZ), and found that several remarkable features of their G ... Full text Link to item Cite

Expression in Escherichia coli of the thermostable DNA polymerase from Pyrococcus furiosus.

Journal Article Protein Expr Purif · November 1997 Pfu, the DNA polymerase from Pyrococcus furiosus, has the lowest error rate of any known polymerase in polymerase chain reaction (PCR) amplification. Previously the protein has been purified from P. furiosus bacterial cultures, and a recombinant form has b ... Full text Link to item Cite

Extracellular annexin II.

Journal Article Int J Biochem Cell Biol · November 1997 Annexin II belongs to a family of calcium-dependent, phospholipid binding proteins. Annexin II was first identified as an intracellular protein and attributed intracellular functions. Although it lacks a signal peptide and its mechanism of secretion is unk ... Full text Link to item Cite

Soluble monomeric P-selectin containing only the lectin and epidermal growth factor domains binds to P-selectin glycoprotein ligand-1 on leukocytes.

Journal Article Blood · September 15, 1997 Under shear stress, leukocytes use P-selectin glycoprotein ligand-1 (PSGL-1) to tether to and roll on P-selectin expressed on activated platelets or endothelial cells. P-selectin has an NH2-terminal lectin domain, an epidermal growth factor (EGF)-like moti ... Link to item Cite

A tenascin knockout with a phenotype.

Journal Article Nat Genet · September 1997 Full text Link to item Cite

FtsZ, a tubulin homologue in prokaryote cell division.

Journal Article Trends Cell Biol · September 1997 Sequence alignments convincingly demonstrate that FtsZ is a prokaryotic homologue of eukaryotic tubulins. FtsZ appears to be universal in eubacteria and archaebacteria and has also been identified in chloroplasts. Like tubulin, it appears to have a cytoske ... Full text Link to item Cite

Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin.

Journal Article Structure · July 15, 1997 BACKGROUND: Fibronectin type III domains are found as autonomously-folded domains in a large variety of multidomain proteins, including extracellular matrix proteins. A subset of these domains employ an Arg-Gly-Asp (RGD) tripeptide motif to mediate contact ... Full text Link to item Cite

Glycosaminoglycans modulate fibronectin matrix assembly and are essential for matrix incorporation of tenascin-C.

Journal Article J Cell Sci · June 1997 We have investigated the role of glycosaminoglycans in fibronectin matrix assembly and the incorporation of tenascin-C into matrix fibrils. Chinese hamster ovary cell mutants with a total block in heparan and chondroitin sulfate production failed to assemb ... Full text Link to item Cite

Two oligomeric forms of plasma ficolin have differential lectin activity.

Journal Article J Biol Chem · May 30, 1997 Ficolins are plasma proteins with binding activity for carbohydrates, elastin, and corticosteroids. The ficolin polypeptide has a collagen-like domain that presumably brings three subunits together in a triple helical rod, a C-terminal fibrinogen-like doma ... Full text Link to item Cite

Tenascin supports lymphocyte rolling.

Journal Article J Cell Biol · May 5, 1997 Tenascin is a large extracellular matrix molecule expressed at specific sites in the adult, including immune system tissues such as the bone marrow, thymus, spleen, and T cell areas of lymph nodes. Tenascin has been reported to have both adhesive and anti- ... Full text Link to item Cite

How Calicum Causes Microtubule Depolymerization

Journal Article Cell Motility and the Cytoskeleton · 1997 Full text Link to item Cite

Tenascin-C knockout mouse has no detectable tenascin-C protein.

Journal Article J Neurosci Res · January 1, 1997 A recent study by Mitrovic and Schachner (J Neurosci Res 42:710-717, 1995) reported the detection of a small amount of truncated tensacin-C (TN-C) in the nervous system of the TN-C knockout mice created by Saga et al. (Genes Dev 6:1821-1831, 1992). The aut ... Link to item Cite

How calcium causes microtubule depolymerization.

Journal Article Cell Motil Cytoskeleton · 1997 Featured Publication The effects of calcium (Ca) were assessed using video-enhanced differential interference contrast light microscopy on individual microtubules in vitro. Phosphocellulose-purified (PC) and microtubule associated protein (MAP)-containing preparations of porci ... Full text Link to item Cite

Structural analysis of a human glial variant laminin.

Journal Article Exp Cell Res · August 25, 1996 Astrocytes secrete laminin-like molecules in culture and may represent a major source of laminin in the developing central nervous system, yet these laminins have not been extensively characterized. We previously reported the presence of an astrocyte-deriv ... Full text Link to item Cite

Mitogenesis, cell migration, and loss of focal adhesions induced by tenascin-C interacting with its cell surface receptor, annexin II.

Journal Article Mol Biol Cell · June 1996 In a previous study we demonstrated that the alternatively spliced region of tenascin-C, TNfnA-D, bound with high affinity to a cell surface receptor, annexin II. In the present study we demonstrate three changes in cellular activity that are produced by a ... Full text Link to item Cite

Visualization of P-selectin glycoprotein ligand-1 as a highly extended molecule and mapping of protein epitopes for monoclonal antibodies.

Journal Article J Biol Chem · March 15, 1996 P-selectin glycoprotein ligand-1 (PSGL-1), a sialomucin on human leukocytes, mediates rolling of leukocytes on P-selectin expressed by activated platelets or endothelial cells under shear forces. PSGL-1 requires both tyrosine sulfate and O-linked glycans t ... Full text Link to item Cite

Articular chondrocyte tenascin-C production and assembly into de novo extracellular matrix.

Journal Article J Orthop Res · March 1996 Tenascin-C is an oligomeric glycoprotein of the extracellular matrix that is expressed in a variety of processes including development, tissue remodeling, wound healing, cell adhesion/antiadhesion, and cell/matrix interactions. Tenascin has recently been a ... Full text Link to item Cite

Tenascin-C expression in dystrophin-related muscular dystrophy.

Journal Article Muscle Nerve · February 1996 The mdx mouse has a mutated dystrophin gene and is used as a model for the study of Duchenne muscular dystrophy (DMD). We investigated whether regenerating mdx skeletal muscle contains the extracellular matrix protein tenascin-C (TN-C), which is expressed ... Full text Link to item Cite

2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region.

Journal Article Cell · January 12, 1996 Featured Publication We have determined the 2.0 A crystal structure of a fragment of human fibronectin encompassing the seventh through the RGD-containing tenth type III repeats (FN7-10). The structure reveals an extended rod-like molecule with a long axis of approximately 140 ... Full text Link to item Cite

Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers.

Journal Article Proc Natl Acad Sci U S A · January 9, 1996 Featured Publication The bacterial cell division protein FtsZ is a homolog of tubulin, but it has not been determined whether FtsZ polymers are structurally related to the microtubule lattice. In the present study, we have obtained high-resolution electron micrographs of two F ... Full text Link to item Cite

Binding of tenascin-C to soluble fibronectin and matrix fibrils.

Journal Article J Biol Chem · December 1, 1995 The small splice variant of tenascin-C (TN) has eight fibronectin type III (FN3) domains. The major large splice variant has three (in chicken) or seven (in human) additional FN3 domains inserted between domains five and six. Chiquet-Ehrismann et al. (Chiq ... Full text Link to item Cite

Single-headed myosin II acts as a dominant negative mutation in Dictyostelium.

Journal Article Proc Natl Acad Sci U S A · August 29, 1995 Conventional myosin II is an essential protein for cytokinesis, capping of cell surface receptors, and development of Dictyostelium cells. Myosin II also plays an important role in the polarization and movement of cells. All conventional myosins are double ... Full text Link to item Cite

A novel alternative splice domain in zebrafish tenascin-C.

Journal Article Gene · April 24, 1995 We have identified and sequenced clones from a zebrafish library that correspond to tenascin-C (TN-C). The 2036-bp sequence covers the C-terminal segment of the protein. Comparison of this sequence to TN-C from other vertebrates indicates that our sequence ... Full text Link to item Cite

Tenascin knockout mice: barrels, boundary molecules, and glial scars.

Journal Article J Neurosci · March 1995 In light of a previous report suggesting that the brains of tenascin-deficient animals are grossly normal, we have studied the somatosensory cortical barrel field and injured cerebral cortex in postnatal homozygous tenascin knockout, heterozygote, and norm ... Full text Link to item Cite

FtsZ, a prokaryotic homolog of tubulin?

Journal Article Cell · February 10, 1995 Full text Link to item Cite

Tenascin-C inhibits extracellular matrix-dependent gene expression in mammary epithelial cells. Localization of active regions using recombinant tenascin fragments.

Journal Article J Cell Sci · February 1995 The physiological role of tenascin in vivo has remained obscure. Although tenascin is regulated in a stage and tissue-dependent manner, knock-out mice appear normal. When tenascin expression was examined in the normal adult mouse mammary gland, little or n ... Full text Link to item Cite

Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin.

Journal Article Proc Natl Acad Sci U S A · October 11, 1994 Featured Publication The elastic protein titin comprises a tandem array of fibronectin type III and immunoglobulin domains, which are structurally similar 7-strand beta-sandwiches. A proposed mechanism for stretching titin, by sequential denaturation of individual fibronectin ... Full text Link to item Cite

LFA-1 binding site in ICAM-3 contains a conserved motif and non-contiguous amino acids.

Journal Article Cell Adhes Commun · October 1994 The intercellular adhesion molecule-3 (ICAM-3) is a counter receptor for the integrin LFA-1 that supports cell-cell adhesion dependent functions. ICAM-3 is a member of the immunoglobulin superfamily possessing five immunoglobulin-like domains. Here, we cha ... Full text Link to item Cite

Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C.

Journal Article J Cell Biol · July 1994 We have investigated the binding of soluble tenascin-C (TN-C) to several cell lines using a radioligand binding assay. Specific binding was demonstrated to U-251MG human glioma cells and to a line of bovine aortic endothelial cells, but hamster fibroblasts ... Full text Link to item Cite

Crystallization of a fragment of human fibronectin: introduction of methionine by site-directed mutagenesis to allow phasing via selenomethionine.

Journal Article Proteins · May 1994 Crystals of a fragment of human fibronectin encompassing the 7th through the RGD-containing 10th type III repeats (FN7-10) have been produced with protein expressed in E. coli. The crystals are monoclinic with one molecule in the asymmetric unit and diffra ... Full text Link to item Cite

Tenascin is induced at implantation sites in the mouse uterus and interferes with epithelial cell adhesion.

Journal Article Development · March 1994 Expression of tenascin, an extracellular matrix protein associated with morphogenetic events and altered states of cellular adhesion, was examined in mouse uterus during the peri-implantation period. A uniform low level expression of tenascin was detected ... Full text Link to item Cite

Tenascin-C in rat lung: distribution, ontogeny and role in branching morphogenesis.

Journal Article Dev Biol · February 1994 Extracellular matrix is important to organogenesis and may function by modifying cellular adhesion, motility, proliferation, and differentiation. Tenascin-C (TN-C) is a matrix molecule reported to bind some cell lines and to inhibit adhesion of some cell t ... Full text Link to item Cite

Induction of human tenascin (neuronectin) by growth factors and cytokines: cell type-specific signals and signalling pathways.

Journal Article J Cell Sci · February 1994 The extracellular matrix protein tenascin (TN) is expressed with precise temporo-spatial patterns during embryonic and fetal development and is induced in healing wounds, inflammatory lesions and solid tumors. These tissue patterns suggest that TN synthesi ... Link to item Cite

Evolution of the tenascin family--implications for function of the C-terminal fibrinogen-like domain.

Journal Article Perspect Dev Neurobiol · 1994 The three members of the tenascin (TN) family, TN-C, TN-R, and TN-X, are apparently conserved in all vertebrates and therefore must have functions that contribute to survival. One specific domain of tenascins, the fibrinogen-like terminal knob, can be argu ... Full text Link to item Cite

Colocalization of tenascin with versican, a hyaluronate-binding chondroitin sulfate proteoglycan.

Journal Article Anat Embryol (Berl) · November 1993 Rabbit antisera against tenascin, a large extracellular matrix protein, in conjunction with monoclonal antibodies of mouse origin against versican, a large hyaluronate-binding proteoglycan, were used to make a comparative study of the distribution of the t ... Full text Link to item Cite

Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions.

Journal Article Curr Opin Cell Biol · October 1993 "Mice develop normally without tenascin", was a shock to biologists studying the extracellular matrix. Could tenascin be a useless protein? This seems most improbable, as it is conserved in every vertebrate species. Moreover, two new proteins have been dis ... Full text Link to item Cite

Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin.

Journal Article J Cell Sci · September 1993 We have found that endothelial cells adhere much more strongly than fibroblasts to domains of tenascin and fibronectin. Endothelial cells adhered weakly, without spreading, to bacterial expression proteins corresponding to the tenth fibronectin type III (F ... Full text Link to item Cite

Structural and functional characterization of monomeric soluble P-selectin and comparison with membrane P-selectin.

Journal Article J Biol Chem · July 15, 1993 P-selectin is an adhesion receptor for leukocytes on thrombin-activated platelets and endothelial cells. It contains a NH2-terminal carbohydrate-recognition domain, an epidermal growth factor motif, nine consensus repeats, a transmembrane domain, and a cyt ... Link to item Cite

Structural and functional domains of the Drosophila ncd microtubule motor protein.

Journal Article J Biol Chem · April 25, 1993 Nonclaret disjunctional (ncd) is a kinesin-related microtubule motor protein that is required for proper chromosome distribution in Drosophila. Despite its sequence similarity to kinesin heavy chain, ncd translocates with the opposite polarity as kinesin, ... Link to item Cite

Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins.

Journal Article J Biol Chem · February 5, 1993 We have produced a set of bacterial expression proteins corresponding to 10 segments of tenascin and two of fibronectin and tested them for heparin binding and cell adhesion. We used polymerase chain reaction cloning to terminate the segments precisely at ... Link to item Cite

Editorial overview

Journal Article Current Opinion in Structural Biology · January 1, 1993 Full text Cite

Machinery of life

Journal Article Nature · 1993 Cite

Localization of tenascin in uterine sarcomas and partially transformed endometrial stromal cells.

Journal Article Pathobiology · 1993 Normal mesenchymal cells within developing embryonic organs and transformed stromal cells in organs undergoing spontaneous carcinogenesis have the capacity for normal or altered expression of the extracellular matrix glycoprotein tenascin (Tn). Mesenchymal ... Full text Link to item Cite

Macromolecular assemblages

Journal Article Current Opinion in Structural Biology · 1993 Cite

Structural organization of the human insulin receptor ectodomain.

Journal Article J Biol Chem · November 15, 1992 To provide an experimental system amenable to a detailed biochemical and structural investigation of the extracellular (ligand binding) domain of the insulin receptor, we developed a mammalian heterologous cell expression system from which tens of milligra ... Link to item Cite

Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein.

Journal Article Science · November 6, 1992 Featured Publication Fibronectin type III domains are found in many different proteins including cell surface receptors and cell adhesion molecules. The crystal structure of one such domain from the extracellular matrix protein tenascin was determined. The structure was solved ... Full text Link to item Cite

Kinetics of protein-protein association explained by Brownian dynamics computer simulation.

Journal Article Proc Natl Acad Sci U S A · April 15, 1992 Featured Publication Protein-protein bond formations, such as antibody-antigen complexation or aggregation of protein monomers into dimers and larger aggregates, occur with bimolecular rate constants on the order of 10(6) M-1.s-1, which is only 3 orders of magnitude slower tha ... Full text Link to item Cite

Visualization of purified fibronectin-transglutaminase complexes.

Journal Article J Biol Chem · April 15, 1992 It has been reported previously (Turner, P.M., and Lorand, L. (1989) Biochemistry 28, 628-635) that human erythrocyte transglutaminase forms a noncovalent complex with human plasma fibronectin near its collagen-binding domain. In the present study, we show ... Link to item Cite

Microtubule dynamic instability and GTP hydrolysis.

Journal Article Annu Rev Biophys Biomol Struct · 1992 Full text Link to item Cite

Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin.

Journal Article J Cell Biol · November 1991 Tenascin, together with thrombospondin and SPARC, form a family of matrix proteins that, when added to bovine aortic endothelial cells, caused a dose-dependent reduction in the number of focal adhesion-positive cells to approximately 50% of albumin-treated ... Full text Link to item Cite

Dilution-induced disassembly of microtubules: relation to dynamic instability and the GTP cap.

Journal Article Cell Motil Cytoskeleton · 1991 Microtubules were assembled from purified tubulin in the buffer originally used to study dynamic instability (100 mM PIPES, 2 mM EGTA, 1 mM magnesium, 0.2 mM GTP) and then diluted in the same buffer to study the rate of disassembly. Following a 15-fold dil ... Full text Link to item Cite

Effects of magnesium on the dynamic instability of individual microtubules.

Journal Article Biochemistry · July 17, 1990 We investigated the effect of magnesium ion (Mg) on the parameters of dynamic instability of individual porcine brain microtubules. Rates of elongation and rapid shortening were measured by using video-enhanced DIC light microscopy and evaluated by using c ... Full text Link to item Cite

HMW-2, the Sertoli cell cytoplasmic dynein from rat testis, is a dimer composed of nearly identical subunits.

Journal Article J Biol Chem · May 25, 1990 The ultrastructure and biochemical characteristics of HMW-2, the Sertoli cell cytoplasmic dynein isolated from rat testes, were analyzed. Electron microscopic studies revealed a two-headed two-stem structure with dimensions very similar to other dyneins. W ... Link to item Cite

Purification of hexabrachion (tenascin) from cell culture conditioned medium, and separation from a cell adhesion factor.

Journal Article Matrix · May 1990 We describe a protocol for purifying hexabrachion from conditioned medium of cell cultures, using gel filtration chromatography on Sephacryl 500, followed by anion-exchange chromatography on a Mono Q column, followed optionally by a second gel filtration o ... Full text Link to item Cite

The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus.

Journal Article Cell · April 20, 1990 Intercellular adhesion molecule 1 (ICAM-1, CD54) binds to the integrin LFA-1 (CD11a/CD18), promoting cell adhesion in immune and inflammatory reactions. ICAM-1 is also subverted as a receptor by the major group of rhinoviruses. Electron micrographs show th ... Full text Link to item Cite

Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion.

Journal Article J Cell Sci · February 1990 Hexabrachion is a large glycoprotein of the extracellular matrix (ECM) that is prominent in embryogenesis, wound healing and tumorigenesis. Because of the role of extracellular matrix proteins in the regulation of cell differentiation and migration, the in ... Full text Link to item Cite

Biochemical and structural studies of tenascin/hexabrachion proteins.

Journal Article J Cell Biochem · October 1989 Tenascin is a large, disulfide-bonded glycoprotein of the extracellular matrix. The predominant form of tenascin observed by electron microscopy is a six-armed oligomer, termed a hexabrachion. We have determined the molecular mass of the native human hexab ... Full text Link to item Cite

Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response.

Journal Article J Cell Biol · October 1989 Cell-substratum adhesion strengths have been quantified using fibroblasts and glioma cells binding to two extracellular matrix proteins, fibronectin and tenascin. A centrifugal force-based adhesion assay was used for the adhesive strength measurements, and ... Full text Link to item Cite

Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response.

Journal Article The Journal of cell biology · October 1989 Cell-substratum adhesion strengths have been quantified using fibroblasts and glioma cells binding to two extracellular matrix proteins, fibronectin and tenascin. A centrifugal force-based adhesion assay was used for the adhesive strength measurements, and ... Full text Cite

Tenascin/hexabrachion in human skin: biochemical identification and localization by light and electron microscopy.

Journal Article J Cell Biol · June 1989 Tenascin/hexabrachion is a large glycoprotein of the extracellular matrix. Previous reports have demonstrated that tenascin is associated with epithelial-mesenchymal interfaces during embryogenesis and is prominent in the matrix of many tumors. However, th ... Full text Link to item Cite

Desmoplakin I and desmoplakin II. Purification and characterization.

Journal Article J Biol Chem · May 15, 1989 Desmoplakins I and II (DP1 and DP2), major cytoskeletal structural proteins concentrated in desmosomes, have been purified in milligram quantities from keratomed pig tongue epithelium. DP1 and DP2 extracted from purified desmosomes in 4 M urea were chromat ... Link to item Cite

Co-operativity in protein-protein association. The structure and stability of the actin filament.

Journal Article J Mol Biol · April 5, 1989 Featured Publication Co-operative association, in which a protein subunit is held simultaneously by two bonds, is enormously more favorable than association forming either bond alone. A theoretical framework for calculating the effect of co-operativity is developed here, which ... Full text Link to item Cite

Synthesis of alpha 2-macroglobulin by bovine adrenal cortical cell cultures.

Journal Article Am J Physiol · April 1989 Primary cultures of bovine adrenal medullary cells synthesize and secrete a high-molecular-weight protein into the culture medium. The protein was purified from the serum-free medium of cultured cells and was identified as alpha 2-macroglobulin by gel elec ... Full text Link to item Cite

Domain structure of phytochrome from Avena sativa visualized by electron microscopy.

Journal Article Photochem Photobiol · April 1989 Highly purified phytochrome from Avena sativa was visualized by electron microscopy after negative staining with uranyl acetate and after rotary shadowing with platinum. The particle shape was variable in both types of specimens, but tripartite structures ... Full text Link to item Cite

Assembly of pure tubulin in the absence of free GTP: effect of magnesium, glycerol, ATP, and the nonhydrolyzable GTP analogues.

Journal Article Biochemistry · February 7, 1989 We describe in vitro microtubule assembly that exhibits, in bulk solution, behavior consistent with the GTP cap model of dynamic instability. Microtubules assembled from pure tubulin in the absence of free nucleotides could undergo one cycle of assembly, b ... Full text Link to item Cite

Topology of cell adhesion molecules.

Journal Article Proc Natl Acad Sci U S A · February 1989 The neural cell adhesion molecule (N-CAM) exists in two major forms [ld (large cytoplasmic domain) peptide and sd (small cytoplasmic domain) peptide] that contain transmembrane segments and different cytoplasmic domains and in a third form [ssd (small surf ... Full text Link to item Cite

Structural and functional characterization of the purified cardiac ryanodine receptor-Ca2+ release channel complex.

Journal Article J Biol Chem · January 15, 1989 Using density gradient centrifugation and [3H]ryanodine as a specific marker, the ryanodine receptor-Ca2+ release channel complex from Chaps-solubilized canine cardiac sarcoplasmic reticulum (SR) has been purified in the form of an approximately 30 S compl ... Link to item Cite

Electron microscopy and hydrodynamic properties of factor XIII subunits.

Journal Article J Biol Chem · January 5, 1989 Factor XIII is a transglutaminase important in blood coagulation and fibrinolysis. Its function is to catalyze peptide bond formation between the gamma-carboxamide group of glutamines in one protein and the epsilon-amino group of lysine in another. There a ... Link to item Cite

Synthesis of α2-macroglobulin by bovine adrenal cortical cell cultures

Journal Article American Journal of Physiology - Cell Physiology · January 1, 1989 Primary cultures of bovine adrenal medullary cells synthesize and secrete a high-molecular-weight protein into the culture medium. The protein was purified from the serum-free medium of cultured cells and was identified as α2-macroglobulin by gel electroph ... Cite

Echinonectin: a new embryonic substrate adhesion protein.

Journal Article J Cell Biol · December 1988 An extracellular matrix molecule has been purified from sea urchin (Lytechinus variegatus) embryos. Based on its functional properties and on its origin, this glycoprotein has been given the name "echinonectin." Echinonectin is a 230-kD dimer with a unique ... Full text Link to item Cite

Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies.

Journal Article J Cell Biol · October 1988 Featured Publication We have developed video microscopy methods to visualize the assembly and disassembly of individual microtubules at 33-ms intervals. Porcine brain tubulin, free of microtubule-associated proteins, was assembled onto axoneme fragments at 37 degrees C, and th ... Full text Link to item Cite

Detection of DNA looping due to simultaneous interaction of a DNA-binding protein with two spatially separated binding sites on DNA.

Journal Article Proc Natl Acad Sci U S A · September 1988 We describe different and relatively rapid biochemical techniques to detect protein-mediated DNA looping. These techniques, based on enhancement of DNA knotting and that of ligase-catalyzed cyclization, were used to show that the replication initiator prot ... Full text Link to item Cite

Enhancer-origin interaction in plasmid R6K involves a DNA loop mediated by initiator protein.

Journal Article Cell · February 12, 1988 Initiation of DNA replication from ori beta of plasmid R6K requires the presence of the ori gamma sequence in cis. We demonstrate that binding of initiator protein to the seven strong, tandem binding sites in gamma increases binding of the protein at the v ... Full text Link to item Cite

Purification and reconstitution of the calcium release channel from skeletal muscle.

Journal Article Nature · January 28, 1988 The calcium release channel from rabbit muscle sarcoplasmic reticulum (SR) has been purified and reconstituted as a functional unit in lipid bilayers. Electron microscopy reveals the four-leaf clover structure previously described for the 'feet' that span ... Full text Link to item Cite

Echinonectin: A new embryonic substrate adhesion protein

Journal Article Journal of Cell Biology · January 1, 1988 An extracellular matrix molecule has been purified from sea urchin (Lytechinus variegatus) embryos. Based on its functional properties and on its origin, this glycoprotein has been given the name 'echinonectin'. Echinonectin is a 230-kD dimer with a unique ... Full text Cite

Hexabrachion Protein (Tenascin, Cytotactin, Brachionectin) in Connective Tissues, Embryonic Brain, and Tumors

Journal Article Advances in Molecular and Cell Biology · January 1, 1988 The hexabrachion is a large oligomeric glycoprotein of the extracellular matrix (ECM). It is synthesized at very specific times and locations during embryonic development, it is absent or restricted in most adult tissues, and it is prominently expressed in ... Full text Cite

Hexabrachion proteins in embryonic chicken tissues and human tumors.

Journal Article J Cell Biol · September 1987 Cell cultures of chicken embryo and human fibroblasts produce a large extracellular matrix molecule with a six-armed structure that we called a hexabrachion (Erickson, H. P., and J. L. Iglesias, 1984, Nature (Lond.), 311:267-269. In the present work we hav ... Full text Link to item Cite

GTP hydrolysis during microtubule assembly.

Journal Article Biochemistry · June 30, 1987 The GTP cap model of dynamic instability [Mitchison, T., & Kirschner, M.W. (1984) Nature (London) 312, 237] postulates that a GTP cap at the end of most microtubules stabilizes the polymer and allows continuing assembly of GTP-tubulin subunits while microt ... Full text Link to item Cite

Evidence for a junctional feet-ryanodine receptor complex from sarcoplasmic reticulum.

Journal Article Biochem Biophys Res Commun · March 13, 1987 Heavy sarcoplasmic reticulum vesicles, labelled with the Ca2+ release channel probe [3H]ryanodine, were solubilized in detergent, then centrifuged through sucrose gradients. A single peak of ryanodine binding activity was observed with an apparent sediment ... Full text Link to item Cite

Substructure of human von Willebrand factor. Proteolysis by V8 and characterization of two functional domains.

Journal Article J Biol Chem · November 25, 1986 The effects of Staphylococcus aureus V8 protease (V8) on the multimeric structure of human von Willebrand factor (vWF) were studied to test and expand our model for the substructure of vWF. Electron microscopy of V8 digests of vWF revealed that the multime ... Link to item Cite

Nucleosome structure.

Journal Article Science · September 26, 1986 Full text Link to item Cite

Substructure of human von Willebrand factor.

Journal Article J Clin Invest · October 1985 Using electron microscopy, we have visualized the substructure of human von Willebrand factor (vWf) purified by two different approaches. vWf multimers, which appear as flexible strands varying in length up to 2 micron, consist of dimeric units (protomers) ... Full text Link to item Cite

A structural comparison of tryptic fragments of three types of intermediate filaments.

Journal Article J Ultrastruct Res · March 1985 We have compared tryptic fragments of three types of intermediate filaments, emphasizing structural characteristics as seen in the electron microscope. Variable, long alpha-helical rod fragments were found to be similar for keratin, neurofilaments and desm ... Full text Link to item Cite

Structure of human platelet membrane glycoproteins IIb and IIIa as determined by electron microscopy.

Journal Article J Biol Chem · February 10, 1985 The glycoprotein (GP) IIb-IIIa complex was isolated from human platelet membranes and examined for glycoprotein stoichiometry and morphology. To determine the ratio of glycoproteins in the complex, the isolated glycoproteins were solubilized with sodium do ... Link to item Cite

Structural characteristics of the desmin protofilament.

Journal Article J Ultrastruct Res · November 1984 Biochemical investigations of intermediate filaments in soluble or partially assembled forms are often difficult to perform due to the unusual insolubility of most types of intermediate filaments. However, desmin is soluble in 10 mM Tris. The structure of ... Full text Link to item Cite

A six-armed oligomer isolated from cell surface fibronectin preparations.

Journal Article Nature · September 20, 1984 Featured Publication Fibronectins are adhesive glycoproteins thought to mediate the attachment of cells to various substrates. Plasma fibronectin (PFN) is a dimer comprising subunits of molecular weight 220,000, connected by one or two disulphide bonds. Electron microscopy sho ... Full text Link to item Cite

The kinetics of microtubule assembly. Evidence for a two-stage nucleation mechanism.

Journal Article J Biol Chem · August 25, 1984 Featured Publication A model describing the nucleation and assembly of purified tubulin has been developed. The novel feature of this model is a two stage nucleation process to allow the explicit inclusion of the two-dimensional nature of the early stages of microtubule assemb ... Link to item Cite

Fibronectin in extended and compact conformations. Electron microscopy and sedimentation analysis.

Journal Article J Biol Chem · December 10, 1983 We have studied the ionic strength-dependent change in conformation of fibronectin, half-molecules of fibronectin produced by reduction and carboxyamidomethylation, and proteolytic fragments. In zone sedimentation through glycerol gradients, intact fibrone ... Link to item Cite

Assembly of proteolytically cleaved tubulin.

Journal Article Arch Biochem Biophys · January 1983 Conditions have been found for limited proteolysis of purified tubulin, in which 70-90% of the molecules are cleaved at one or two sites. Thermolysin and chymotrypsin cleave the alpha and beta subunits, respectively, at single sites. Trypsin cleaves the al ... Full text Link to item Cite

Electron microscopy of human factor VIII/Von Willebrand glycoprotein: effect of reducing reagents on structure and function.

Journal Article J Cell Biol · November 1982 The structure of native and progressively reduced human factor VIII/von Willebrand factor (FVIII/vWF) was examined by electron microscopy and SDS gel electrophoresis and then correlated with its biological activities. Highly resolved electron micrographs o ... Full text Link to item Cite

Electron microscopy of human factor VIII/von willebrand glycoprotein: Effect of reducing reagents on structure and function

Journal Article Journal of Cell Biology · November 1, 1982 The structure of native and progressively reduced human factor Vlll/von Willebrand factor (FVlll/vWF) was examined by electron microscopy and SDS gel electrophoresis and then correlated with its biological activities. Highly resolved electron micrographs o ... Full text Cite

Visualization of a 21-nm axial periodicity in shadowed keratin filaments and neurofilaments.

Journal Article J Cell Biol · September 1982 Unidirectional and rotary shadowing techniques have been applied in studying the surface structure of two types of intermediate filaments. Keratin filaments and neurofilaments demonstrate a approximately 21-nm axial periodicity which probably indicates the ... Full text Link to item Cite

Fibronectin molecule visualized in electron microscopy: a long, thin, flexible strand.

Journal Article J Cell Biol · December 1981 We have determined the structure of plasma fibronectin by electron microscopy of shadowed specimens. the 440,000 molecular weight, dimeric molecule appears to be a long, thin, highly flexible strand. The contour length of the most extended molecules is 160 ... Full text Link to item Cite

Structural properties of an active form of rabbit muscle phosphofructokinase.

Journal Article J Biol Chem · September 25, 1981 The quaternary structure of an active form of rabbit muscle phosphofructokinase was studied by sedimentation and electron microscopy. Active enzyme centrifugation studies at pH 7.0 and 23 +/- 1 degrees C showed that phosphofructokinase sediments as a singl ... Link to item Cite

Structure of the fibrin protofibril.

Journal Article Proc Natl Acad Sci U S A · August 1981 We identified the two-stranded fibrin protofibril and studied its structure in electron micrographs of negatively stained specimens. Based on these images and on considerations of symmetry, we constructed a model of the protofibril in which the two strands ... Full text Link to item Cite

The role of subunit entropy in cooperative assembly. Nucleation of microtubules and other two-dimensional polymers.

Journal Article Biophys J · May 1981 The self-assembly and nucleation of two-dimensional polymers is described by a theory based on a model of rigid subunits and bonds and simple principles of thermodynamics. The key point in the theory is to separate as an explicit parameter the free energy, ... Full text Link to item Cite

Fibrin assembly: a comparison of electron microscopic and light scattering results.

Journal Article Thromb Haemost · December 19, 1980 To test the validity of a proposed two step fibrin assembly mechanism and directly visualize the molecular species present at various stages of fibrin formation, we have carried out an electron microscopic investigation. Assembly conditions duplicated thos ... Link to item Cite

Electron microsocpy of plasmic fragments of human fibrinogen as related to trinodular structure of the intact molecule.

Journal Article J Clin Invest · July 1980 We have examined rotary shadowed, purified plasmic fragments of human fibrinogen with the electron microscope and have determined the relation of these fragments to the intact fibrinogen molecule. Both intact fibrinogen and its earliest cleavage product, f ... Full text Link to item Cite

Fibrin formation as a biological assembly process

Journal Article Biophysical Journal · January 1, 1980 Full text Cite

Thermodynamic and kinetic aspects of assembly.

Journal Article Prog Clin Biol Res · 1980 Link to item Cite

Tubulin rings: curved filaments with limited flexibility and two modes of association.

Journal Article J Supramol Struct · 1979 Tubulin rings have been previously identified as composed of linear polymers of tubulin subunits, equivalent to a protofilament in the microtubule wall but in a curved rather than a straight conformation. We have examined and measured a number of different ... Full text Link to item Cite

Guanosinetriphosphatase activity of tubulin associated with microtubule assembly.

Journal Article Proc Natl Acad Sci U S A · December 1977 Tubulin, purified by cycles of assembly followed by phosphocellulose chromatography, exhibits a characteristic GTPase activity that is polymerization dependent and can be attributed to the tubulin itself. This activity has been observed, in a standard reas ... Full text Link to item Cite

Polycation-induced assembly of purified tubulin.

Journal Article Proc Natl Acad Sci U S A · August 1976 Several different polycations have been found that can substitute for the microtubule-associated proteins, or tau factor, in facilitating assembly of tubulin that has been purified by ion exchange chromatography. In low concentrations of the polycation die ... Full text Link to item Cite

The structure and assembly of microtubules.

Journal Article Ann N Y Acad Sci · June 30, 1975 Full text Link to item Cite

Negatively stained vinblastine aggregates.

Journal Article Ann N Y Acad Sci · June 30, 1975 Full text Link to item Cite

Microtubule surface lattice and subunit structure and observations on reassembly.

Journal Article J Cell Biol · January 1974 Featured Publication Neuronal microtubules have been reassembled from brain tissue homogenates and purified. In reassembly from purified preparations, one of the first structures formed was a flat sheet, consisting of up to 13 longitudinal filaments, which was identified as an ... Full text Link to item Cite

Electron microscopic study of base sequence in nucleic acids VI. Guanine sites in yeast alanine transfer RNA

Journal Article Micron (1969) · January 1, 1970 Yeast alanine t-RNA was reacted with 2-diazo-p-benzene-disulphonic acid, which is known to attach with high specificity to the guanosine monophosphate nucleotides. The guanine marked RNA molecules were extended on thin carbon film, stained with uranyl acet ... Full text Cite

Rapid nucleotide separation by chromatography on cation-exchange columns

Journal Article Analytical Biochemistry · January 1, 1967 Full text Cite