Harold Paul Erickson
James B. Duke Distinguished Professor Emeritus
Current Research Interests
Cytoskeleton: A major research interest has been the cytoskeleton, in particular microtubules in eukaryotes, and the bacterial tubulin homolog FtsZ. Highlights of our research have been reconstituting FtsZ-rings in liposomes and the demonstration that FtsZ alone can generate a constriction force (Ozawa 2008, 2013); a computer model that explains both treadmilling and nucleation of FtsZ protofilaments based on GTP hydrolysis and the R to T conformational change (Corbin 2020); a perspective linking microtubule growth to the single protofilaments of FtsZ (Erickson 2019).
Irisin. We believe the irisin story is bunk. Irisin was proposed in 2012 as a novel myokine, secreted by muscle cells in response to exercise, it induces the transformation of white fat to brown fat. This inspired hopes of an exercise pill that might correct obesity and other metabolic disorders. We have argued that the original discovery was flawed in several respects (Erickson, Adipocyte, 2013), and that the 1,000+ published follow-up studies are based on flawed commercial antibodies (Albrecht et al, Sci Rep 2015). Our recent review (Maak et al, Endoc Rev 2021) expands these critiques, adds new ones, and suggests that gene knockouts will help resolve controversies.Sars-CoV-2: Several labs have developed antibody mimics that bind the spike protein, and then incorporated these into dimers and trimers that were designed to bind multivalently to the trimeric spike. We found that the linkers connecting the Nbs are too short to span the distance. We suggest an alternative mechanism for the modest (modest) enhanced avidity (Erickson and Corbin, 2022)
Principles of Protein-Protein Association, Erickson 2019: This ebook, published by IOP press and available to many institutions with a subscription, provides basic principles and discussion of seminal papers. It is suitable for a short course, or for individual learning.
Current Appointments & Affiliations
- James B. Duke Distinguished Professor Emeritus, Cell Biology, Basic Science Departments 2022
- Professor Emeritus of Cell Biology, Cell Biology, Basic Science Departments 2022
- Member of the Duke Cancer Institute, Duke Cancer Institute, Institutes and Centers 2013
Contact Information
- 412 Nanaline H Duke, Durham, NC 27708
- Duke Box 3709, Durham, NC 27710
-
h.erickson@duke.edu
-
Department of Cell Biology
-
Erickson CellBio page
- Background
-
Education, Training, & Certifications
- Ph.D., Johns Hopkins University 1968
-
Previous Appointments & Affiliations
- Professor of Biochemistry, Biochemistry, Basic Science Departments 2009 - 2022
- Professor of Cell Biology, Cell Biology, Basic Science Departments 1982 - 2022
- James B. Duke Distinguished Professor of Cell Biology, Cell Biology, Basic Science Departments 1996 - 2022
- Professor of Biomedical Engineering, Biomedical Engineering, Pratt School of Engineering 2017 - 2020
- Director, Graduate Studies, Cell Biology, Basic Science Departments 1990 - 2006
- Professor in Biomedical Engineering, Biomedical Engineering, Pratt School of Engineering 2004 - 2005
- Acting Chair, Department of Cell Biology, Cell Biology, Basic Science Departments 2000 - 2002
- Interim Chairman, Department of Cell Biology, Cell Biology, Basic Science Departments 1988 - 1989
- Recognition
-
In the News
-
AUG 14, 2015 Science -
MAR 17, 2015 MedPage Today -
MAR 11, 2015 The Scientist -
MAR 9, 2015
-
- Expertise
-
Subject Headings
- Acquired Immunodeficiency Syndrome
- Acrylamide
- Actin Cytoskeleton
- Actins
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Age Factors
- Alkaline Phosphatase
- Allosteric Regulation
- Alternative Splicing
- Amidohydrolases
- Amino Acid Motifs
- Amino Acid Sequence
- Amino Acid Substitution
- Anion Exchange Resins
- Annexin A2
- Antibodies
- Antibodies, Monoclonal
- Antigens, CD
- Antigens, CD18
- Antigens, CD29
- Antigens, Differentiation
- Antigens, Nuclear
- Antigens, Surface
- Aorta
- Archaea
- Archaeal Proteins
- Artificial Gene Fusion
- Aspartic Acid
- Astrocytes
- Astrocytoma
- Azotobacter vinelandii
- Bacillus anthracis
- Bacillus subtilis
- Bacillus thuringiensis
- Bacteria
- Bacterial Physiological Phenomena
- Bacterial Proteins
- Base Sequence
- Binding Sites
- Binding Sites, Antibody
- Binding, Competitive
- Biochemistry
- Biological Evolution
- Biophysical Phenomena
- Biophysics
- Biopolymers
- Blood Coagulation Factors
- Blood Platelets
- Blotting, Northern
- Blotting, Western
- Bone Marrow
- Bone Neoplasms
- Brain
- Brain Chemistry
- Brain Injuries
- Buffers
- CHO Cells
- Caenorhabditis elegans Proteins
- Calcium
- Calmodulin-Binding Proteins
- Calorimetry
- Carrier Proteins
- Catalytic Domain
- Cations
- Cations, Divalent
- Cattle
- Caulobacter crescentus
- Cell Adhesion
- Cell Adhesion Molecules
- Cell Adhesion Molecules, Neuronal
- Cell Cycle Proteins
- Cell Differentiation
- Cell Division
- Cell Line
- Cell Line, Transformed
- Cell Membrane
- Cell Movement
- Cell Separation
- Cell Survival
- Cell Transformation, Neoplastic
- Cells, Cultured
- Central Nervous System
- Centrifugation
- Centrifugation, Density Gradient
- Cereals
- Chelating Agents
- Chemical Fractionation
- Chemical Phenomena
- Chemical Precipitation
- Chemistry
- Chemistry, Physical
- Chemokine CX3CL1
- Chemokines, CX3C
- Chemokines, CXC
- Chick Embryo
- Chickens
- Child
- Chimera
- Chondrocytes
- Chondroitin Sulfate Proteoglycans
- Chondroitin Sulfates
- Chromaffin System
- Chromatography
- Chromatography, Affinity
- Chromatography, High Pressure Liquid
- Chromatography, Ion Exchange
- Chromatography, Liquid
- Chromosomal Proteins, Non-Histone
- Chromosome Deletion
- Chromosome Segregation
- Chromosomes
- Chromosomes, Bacterial
- Cloning, Molecular
- Colchicine
- Cold Temperature
- Collagen
- Computer Simulation
- Connective Tissue Diseases
- Cricetinae
- Cross-Linking Reagents
- Crystallization
- Crystallography
- Crystallography, X-Ray
- Culture Media
- Culture Media, Conditioned
- Culture Techniques
- Cycloheximide
- Cysteine
- Cytokines
- Cytokinesis
- Cytoplasm
- Cytoskeletal Proteins
- Cytoskeleton
- DEAE-Dextran
- DNA
- DNA Helicases
- DNA Ligases
- DNA Repair
- DNA Replication
- DNA, Bacterial
- DNA, Circular
- DNA, Complementary
- DNA-Binding Proteins
- Dactinomycin
- Detergents
- Dextrans
- Diffusion
- Dimerization
- Disulfides
- Dithiothreitol
- Dogs
- Dose-Response Relationship, Drug
- Down-Regulation
- Drosophila
- Drosophila Proteins
- Drosophila melanogaster
- Drug Interactions
- Drug Stability
- E-Selectin
- Edetic Acid
- Elasticity
- Electrophoresis, Gel, Two-Dimensional
- Electrophoresis, Polyacrylamide Gel
- Embryo Implantation
- Embryo, Mammalian
- Embryonic and Fetal Development
- Endopeptidases
- Endosomal Sorting Complexes Required for Transport
- Endothelial Cells
- Endothelium
- Endothelium, Vascular
- Energy Metabolism
- Entropy
- Enzyme Activation
- Epidermal Growth Factor
- Epidermis
- Epithelium
- Epitope Mapping
- Epitopes
- Erythrocytes
- Escherichia coli
- Escherichia coli Proteins
- Estrus
- Eukaryotic Cells
- Evolution, Molecular
- Exercise
- Exodeoxyribonucleases
- Exons
- Extracellular Matrix
- Extracellular Matrix Proteins
- Factor VIII
- Factor XIII
- Female
- Fetus
- Fibrinogen
- Fibroblasts
- Fibronectins
- Flow Cytometry
- Fluorescein
- Fluorescence
- Fluorescence Polarization
- Fluorescence Recovery After Photobleaching
- Fluorescence Resonance Energy Transfer
- Fluorescent Antibody Technique
- Fluorescent Dyes
- Focal Adhesions
- Fourier Analysis
- Fungal Proteins
- GTP Phosphohydrolases
- GTP-Binding Proteins
- Gene Deletion
- Gene Expression
- Gene Expression Regulation
- Gene Library
- Genes, Bacterial
- Genes, Insect
- Genes, Reporter
- Genes, src
- Genetic Variation
- Genetic Vectors
- Glutamine
- Glutaral
- Glycerol
- Glycoproteins
- Glycosaminoglycans
- Glycosides
- Glycosylation
- Gram-Negative Anaerobic Bacteria
- Gram-Negative Bacteria
- Green Fluorescent Proteins
- Growth Substances
- Guanine Nucleotides
- Guanosine Diphosphate
- Guanosine Triphosphate
- Guinea Pigs
- HEK293 Cells
- Half-Life
- HeLa Cells
- Heart Ventricles
- Helminth Proteins
- Hematopoietic Stem Cells
- Hemocyanin
- Heparin
- Heterozygote
- Hormones
- Humans
- Hydrogen Bonding
- Hydrogen-Ion Concentration
- Hydrolysis
- Image Processing, Computer-Assisted
- Immune Sera
- Immunoglobulin Constant Regions
- Immunoglobulins
- Immunohistochemistry
- Immunologic Techniques
- Immunoprecipitation
- Inhibitory Concentration 50
- Insect Proteins
- Integrin alpha Chains
- Integrin alphaVbeta3
- Integrins
- Intercellular Adhesion Molecule-1
- Ion Channels
- Isoenzymes
- K562 Cells
- Keratan Sulfate
- Kinesin
- Kinetics
- Laminin
- Lectins
- Lectins, C-Type
- Leukocyte L1 Antigen Complex
- Leukocytes
- Ligands
- Light
- Lipid Bilayers
- Liposomes
- Liver
- Luminescent Proteins
- Lung
- Lymphocyte Function-Associated Antigen-1
- Lymphocytes
- Macromolecular Substances
- Magnesium
- Magnetic Resonance Spectroscopy
- Mammary Glands, Animal
- Mass Spectrometry
- Mathematics
- Melanocytes
- Membrane Glycoproteins
- Membrane Potentials
- Membrane Proteins
- Membranes
- Mercaptoethanol
- Metaphase
- Methods
- Mice
- Mice, Inbred Strains
- Mice, Knockout
- Micromanipulation
- Microscopy, Atomic Force
- Microscopy, Electron
- Microscopy, Fluorescence
- Microscopy, Immunoelectron
- Microspheres
- Microtubule Proteins
- Microtubules
- Milk, Human
- Mitogens
- Models, Biological
- Models, Chemical
- Models, Genetic
- Models, Molecular
- Models, Structural
- Models, Theoretical
- Molecular Conformation
- Molecular Sequence Data
- Molecular Structure
- Molecular Weight
- Monte Carlo Method
- Morphogenesis
- Motion
- Mucins
- Multigene Family
- Multiprotein Complexes
- Muscle Proteins
- Muscle, Skeletal
- Muscles
- Muscular Dystrophy, Animal
- Mutagenesis
- Mutagenesis, Insertional
- Mutagenesis, Site-Directed
- Mutation
- Mycobacterium tuberculosis
- Myocardium
- Myosin-Light-Chain Kinase
- Myosins
- Negative Staining
- Neoplasm Proteins
- Neoplasms
- Nerve Growth Factors
- Nerve Tissue Proteins
- Nervous System Malformations
- Neural Cell Adhesion Molecules
- Neurons
- Neutrophils
- Nuclear Magnetic Resonance, Biomolecular
- Nuclear Proteins
- Nucleic Acid Conformation
- Octoxynol
- Oligonucleotide Probes
- Oligopeptides
- Organ Specificity
- Osmolar Concentration
- Oxygen
- P-Selectin
- Paclitaxel
- Palatine Tonsil
- Peptide Fragments
- Peptide Mapping
- Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
- Peptides
- Permeability
- Phenotype
- Phylogeny
- Physicochemical Phenomena
- Physicochemical Processes
- Phytochrome
- Plant Proteins
- Plasmids
- Plastics
- Platelet Aggregation
- Platelet Membrane Glycoproteins
- Platelet-Derived Growth Factor
- Pleurodeles
- Pliability
- Poly A
- Polyethylene Glycols
- Polymerase Chain Reaction
- Polymers
- Potassium
- Precipitin Tests
- Pregnancy
- Proline
- Promoter Regions, Genetic
- Protein Binding
- Protein Conformation
- Protein Denaturation
- Protein Engineering
- Protein Folding
- Protein Interaction Mapping
- Protein Isoforms
- Protein Kinases
- Protein Multimerization
- Protein Precursors
- Protein Sorting Signals
- Protein Stability
- Protein Structure, Quaternary
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Protein Subunits
- Protein Transport
- Proteins
- Proteoglycans
- Proto-Oncogene Proteins pp60(c-src)
- Pseudomonas aeruginosa
- R Factors
- RNA Splicing
- RNA, Messenger
- Rabbits
- Radioligand Assay
- Rats
- Rats, Sprague-Dawley
- Receptors
- Receptors, Cell Surface
- Receptors, Cholinergic
- Receptors, Fibronectin
- Receptors, Leukocyte-Adhesion
- Receptors, Somatotropin
- Receptors, Virus
- Receptors, Vitronectin
- Recombinant Fusion Proteins
- Recombinant Proteins
- Recombination, Genetic
- Repetitive Sequences, Amino Acid
- Repetitive Sequences, Nucleic Acid
- Resins, Synthetic
- Reticulin
- Rheology
- Rhinovirus
- Rhodamines
- Ristocetin
- Rubidium
- Ryanodine
- Ryanodine Receptor Calcium Release Channel
- Salts
- Sarcoplasmic Reticulum
- Scattering, Radiation
- Sea Urchins
- Selenomethionine
- Sensitivity and Specificity
- Sequence Alignment
- Sequence Analysis
- Sequence Analysis, DNA
- Sequence Homology
- Sequence Homology, Amino Acid
- Serine Endopeptidases
- Sertoli Cells
- Signal Transduction
- Silver Staining
- Skin
- Sodium
- Solubility
- Solutions
- Species Specificity
- Spectrometry, Fluorescence
- Spectrophotometry
- Spectrum Analysis
- Spinal Cord
- Static Electricity
- Structural Homology, Protein
- Structure-Activity Relationship
- Succinimides
- Sulfuric Acid Esters
- Surface Plasmon Resonance
- Surface Properties
- Swine
- Temperature
- Tenascin
- Tensile Strength
- Thermodynamics
- Thermolysin
- Time Factors
- Tissue Scaffolds
- Tongue
- Torsion, Mechanical
- Trans-Activators
- Transfection
- Transforming Growth Factor beta
- Transglutaminases
- Trypsin
- Tryptophan
- Tubulin
- Tumor Cells, Cultured
- Ultracentrifugation
- Unilamellar Liposomes
- Urea
- Uterus
- Versicans
- Vibrissae
- Video Recording
- Vinculin
- Viral Proteins
- Wound Healing
- X-Ray Diffraction
- X-ray crystallography
- Xenopus
- Xenopus Proteins
- Yeasts
- Zebrafish
- von Willebrand Factor
- Research
-
Selected Grants
- Organization and Function of Cellular Structure awarded by National Institutes of Health 1975 - 2020
- Differentiation Induced Changes in Centrosomes and Microtubule Organization awarded by National Institutes of Health 2014 - 2019
- Structure and Assembly Dynamics of FtsZ awarded by National Institutes of Health 2002 - 2019
- Fluoride and human health: Assessing novel biomarkers in detecting bone disorder awarded by National Institutes of Health 2015 - 2017
- Extracellular Matrix and Cell Attachment Proteins awarded by National Institutes of Health 2012 - 2017
- Assembly, Dynamics and Regulation of Chloroplast FtsZ awarded by Michigan State University 2011 - 2016
- Structural Biology and Biophysics Training Program awarded by National Institutes of Health 1994 - 2015
- A Genomic and Structural Study of FTsZ Constriction in Cell Divison awarded by National Institutes of Health 2010 - 2013
- A Fluorescence-Based Biosensor for Measurement of Cell Derived Forces awarded by National Institutes of Health 2009 - 2011
- Live cell widefield fluorescence microscope with activation and bleaching lasers awarded by National Institutes of Health 2010 - 2011
- Training in Biomolecular and Tissue Engineering awarded by National Institutes of Health 2003 - 2009
- Graduate training in Biologically Inspired Materials awarded by National Science Foundation 2002 - 2007
- Regulation of Germline Stem Cell Division in Drosophila awarded by National Institutes of Health 1996 - 2006
- Zeiss LSM510 META confocal-fluorescence spectroscopy awarded by National Institutes of Health 2003 - 2004
- Development and Construction of Single Molecule Spectrometers for Research and Student Training awarded by National Science Foundation 2001 - 2003
- Same awarded by National Institutes of Health 1981 - 2002
- Center for FEL Research in the Medical, Biological, and Materials Sciences awarded by Air Force Office of Scientific Research 2000 - 2001
- Multivalent Ligands To Enhance Cell Receptor Binding awarded by National Institutes of Health 1998 - 2000
- Structure And Assembly Of Cytoskeletal Filaments awarded by National Institutes of Health 1996 - 1999
- Structure & Assembly Of Cytoskeletal Filaments awarded by National Institutes of Health 1981 - 1999
- Tenascin Regulation Of Cell-Matrix Interactions In Skin awarded by National Institutes of Health 1996 - 1997
- Tenascin Regulation Of Cell Matrix Interactions In Skin awarded by National Institutes of Health 1995 - 1997
- Extracellular Matrix And Cell Attachment Proteins awarded by National Institutes of Health 1996 - 1997
- Structure And Assembly Of Cytoskeletal Filamients awarded by National Institutes of Health 1986 - 1989
- Electron Microscopy Of Plasma And Cell Surface Proteins awarded by National Institutes of Health 1986 - 1988
- Electron Microscopy Of Plasma And Cell Surface Protein awarded by National Institutes of Health 1986 - 1987
- 434uisition Of Philips Em 420 Microscope With Goniometer awarded by National Science Foundation 1984 - 1985
- Phailips Em420 Microscope With Goniometer & Cryo Stage awarded by National Institutes of Health 1984
- Publications & Artistic Works
-
Selected Publications
-
Academic Articles
-
Erickson, Harold P., and Lauren Corbin Goodman. “Recently Designed Multivalent Spike Binders Cannot Bind Multivalently─How Do They Achieve Enhanced Avidity to SARS-CoV-2?” Biochemistry 62, no. 2 (January 17, 2023): 163–68. https://doi.org/10.1021/acs.biochem.2c00291.Full Text Open Access Copy Link to Item
-
Corbin Goodman, Lauren C., and Harold P. Erickson. “FtsZ at mid-cell is essential in Escherichia coli until the late stage of constriction.” Microbiology (Reading) 168, no. 6 (June 2022). https://doi.org/10.1099/mic.0.001194.Full Text Open Access Copy Link to Item
-
Maak, Steffen, Frode Norheim, Christian A. Drevon, and Harold P. Erickson. “Progress and Challenges in the Biology of FNDC5 and Irisin.” Endocr Rev 42, no. 4 (July 16, 2021): 436–56. https://doi.org/10.1210/endrev/bnab003.Full Text Open Access Copy Link to Item
-
Erickson, Harold P. “How Teichoic Acids Could Support a Periplasm in Gram-Positive Bacteria, and Let Cell Division Cheat Turgor Pressure.” Front Microbiol 12 (2021): 664704. https://doi.org/10.3389/fmicb.2021.664704.Full Text Open Access Copy Link to Item
-
Porter, Katie J., Lingyan Cao, Yaodong Chen, Allan D. TerBush, Cheng Chen, Harold P. Erickson, and Katherine W. Osteryoung. “The Arabidopsis thaliana chloroplast division protein FtsZ1 counterbalances FtsZ2 filament stability in vitro.” J Biol Chem 296 (2021): 100627. https://doi.org/10.1016/j.jbc.2021.100627.Full Text Open Access Copy Link to Item
-
Corbin, Lauren C., and Harold P. Erickson. “A Unified Model for Treadmilling and Nucleation of Single-Stranded FtsZ Protofilaments.” Biophys J 119, no. 4 (August 18, 2020): 792–805. https://doi.org/10.1016/j.bpj.2020.05.041.Full Text Open Access Copy Link to Item
-
Schumacher, Maria A., Tomoo Ohashi, Lauren Corbin, and Harold P. Erickson. “High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP.” Acta Crystallogr F Struct Biol Commun 76, no. Pt 2 (February 1, 2020): 94–102. https://doi.org/10.1107/S2053230X20001132.Full Text Open Access Copy Link to Item
-
Osawa, Masaki, and Harold P. Erickson. “L form bacteria growth in low-osmolality medium.” Microbiology (Reading) 165, no. 8 (August 2019): 842–51. https://doi.org/10.1099/mic.0.000799.Full Text Open Access Copy Link to Item
-
Mangan, Riley J., Lisa Stamper, Tomoo Ohashi, Joshua A. Eudailey, Eden P. Go, Frederick H. Jaeger, Hannah L. Itell, et al. “Determinants of Tenascin-C and HIV-1 envelope binding and neutralization.” Mucosal Immunol 12, no. 4 (July 2019): 1004–12. https://doi.org/10.1038/s41385-019-0164-2.Full Text Link to Item
-
Erickson, Harold P. “Microtubule Assembly from Single Flared Protofilaments-Forget the Cozy Corner?” Biophys J 116, no. 12 (June 18, 2019): 2240–45. https://doi.org/10.1016/j.bpj.2019.05.005.Full Text Open Access Copy Link to Item
-
Huang, Haiyan, Ping Wang, Li Bian, Masaki Osawa, Harold P. Erickson, and Yaodong Chen. “The cell division protein MinD from Pseudomonas aeruginosa dominates the assembly of the MinC-MinD copolymers.” J Biol Chem 293, no. 20 (May 18, 2018): 7786–95. https://doi.org/10.1074/jbc.RA117.001513.Full Text Open Access Copy Link to Item
-
Osawa, Masaki, and Harold P. Erickson. “Turgor Pressure and Possible Constriction Mechanisms in Bacterial Division.” Front Microbiol 9 (2018): 111. https://doi.org/10.3389/fmicb.2018.00111.Full Text Open Access Copy Link to Item
-
Saunders, Kevin O., Laurent K. Verkoczy, Chuancang Jiang, Jinsong Zhang, Robert Parks, Haiyan Chen, Max Housman, et al. “Vaccine Induction of Heterologous Tier 2 HIV-1 Neutralizing Antibodies in Animal Models.” Cell Rep 21, no. 13 (December 26, 2017): 3681–90. https://doi.org/10.1016/j.celrep.2017.12.028.Full Text Link to Item
-
Ohashi, Tomoo, Christopher A. Lemmon, and Harold P. Erickson. “Fibronectin Conformation and Assembly: Analysis of Fibronectin Deletion Mutants and Fibronectin Glomerulopathy (GFND) Mutants.” Biochemistry 56, no. 34 (August 29, 2017): 4584–91. https://doi.org/10.1021/acs.biochem.7b00589.Full Text Open Access Copy Link to Item
-
Erickson, Harold P. “How bacterial cell division might cheat turgor pressure - a unified mechanism of septal division in Gram-positive and Gram-negative bacteria.” Bioessays 39, no. 8 (August 2017). https://doi.org/10.1002/bies.201700045.Full Text Open Access Copy Link to Item
-
Chen, Yaodong, Haiyan Huang, Masaki Osawa, and Harold P. Erickson. “ZipA and FtsA* stabilize FtsZ-GDP miniring structures.” Sci Rep 7, no. 1 (June 16, 2017): 3650. https://doi.org/10.1038/s41598-017-03983-4.Full Text Open Access Copy Link to Item
-
Chen, Yaodong, Katie Porter, Masaki Osawa, Anne Marie Augustus, Sara L. Milam, Chandra Joshi, Katherine W. Osteryoung, and Harold P. Erickson. “The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red Alga Galdieria sulphuraria Co-assemble into Dynamic Filaments.” J Biol Chem 292, no. 13 (March 31, 2017): 5207–15. https://doi.org/10.1074/jbc.M116.767715.Full Text Open Access Copy Link to Item
-
Erickson, Harold P. “Protein unfolding under isometric tension-what force can integrins generate, and can it unfold FNIII domains?” Curr Opin Struct Biol 42 (February 2017): 98–105. https://doi.org/10.1016/j.sbi.2016.12.002.Full Text Open Access Copy Link to Item
-
Erickson, Harold P. “The discovery of the prokaryotic cytoskeleton: 25th anniversary.” Mol Biol Cell 28, no. 3 (February 1, 2017): 357–58. https://doi.org/10.1091/mbc.E16-03-0183.Full Text Open Access Copy Link to Item
-
Shah, Riddhi, Tomoo Ohashi, Harold P. Erickson, and Terrence G. Oas. “Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.” J Biol Chem 292, no. 3 (January 20, 2017): 955–66. https://doi.org/10.1074/jbc.M116.760371.Full Text Open Access Copy Link to Item
-
Erickson, Harold P., and Masaki Osawa. “FtsZ Constriction Force - Curved Protofilaments Bending Membranes.” Subcell Biochem 84 (2017): 139–60. https://doi.org/10.1007/978-3-319-53047-5_5.Full Text Open Access Copy Link to Item
-
Gardner, Kiani AJ Arkus, Masaki Osawa, and Harold P. Erickson. “Whole genome re-sequencing to identify suppressor mutations of mutant and foreign Escherichia coli FtsZ.” Plos One 12, no. 4 (2017): e0176643. https://doi.org/10.1371/journal.pone.0176643.Full Text Open Access Copy Link to Item
-
Moore, Desmond A., Zakiya N. Whatley, Chandra P. Joshi, Masaki Osawa, and Harold P. Erickson. “Probing for Binding Regions of the FtsZ Protein Surface through Site-Directed Insertions: Discovery of Fully Functional FtsZ-Fluorescent Proteins.” J Bacteriol 199, no. 1 (January 1, 2017). https://doi.org/10.1128/JB.00553-16.Full Text Open Access Copy Link to Item
-
Housman, Max, Sara L. Milam, Desmond A. Moore, Masaki Osawa, and Harold P. Erickson. “FtsZ Protofilament Curvature Is the Opposite of Tubulin Rings.” Biochemistry 55, no. 29 (July 26, 2016): 4085–91. https://doi.org/10.1021/acs.biochem.6b00479.Full Text Open Access Copy Link to Item
-
Suzuki, Aussie, Benjamin L. Badger, Julian Haase, Tomoo Ohashi, Harold P. Erickson, Edward D. Salmon, and Kerry Bloom. “How the kinetochore couples microtubule force and centromere stretch to move chromosomes.” Nat Cell Biol 18, no. 4 (April 2016): 382–92. https://doi.org/10.1038/ncb3323.Full Text Open Access Copy Link to Item
-
Mansour, Robin G., Lisa Stamper, Frederick Jaeger, Erin McGuire, Genevieve Fouda, Joshua Amos, Kimberly Barbas, et al. “The Presence and Anti-HIV-1 Function of Tenascin C in Breast Milk and Genital Fluids.” Plos One 11, no. 5 (2016): e0155261. https://doi.org/10.1371/journal.pone.0155261.Full Text Link to Item
-
Bisson-Filho, Alexandre W., Karen F. Discola, Patrícia Castellen, Valdir Blasios, Alexandre Martins, Maurício L. Sforça, Wanius Garcia, et al. “FtsZ filament capping by MciZ, a developmental regulator of bacterial division.” Proc Natl Acad Sci U S A 112, no. 17 (April 28, 2015): E2130–38. https://doi.org/10.1073/pnas.1414242112.Full Text Open Access Copy Link to Item
-
Albrecht, Elke, Frode Norheim, Bernd Thiede, Torgeir Holen, Tomoo Ohashi, Lisa Schering, Sindre Lee, et al. “Irisin - a myth rather than an exercise-inducible myokine.” Sci Rep 5 (March 9, 2015): 8889. https://doi.org/10.1038/srep08889.Full Text Open Access Copy Link to Item
-
Spahich, Nicole A., Roma Kenjale, Jessica McCann, Guoyu Meng, Tomoo Ohashi, Harold P. Erickson, and Joseph W. St Geme. “Structural determinants of the interaction between the Haemophilus influenzae Hap autotransporter and fibronectin.” Microbiology (Reading) 160, no. Pt 6 (June 2014): 1182–90. https://doi.org/10.1099/mic.0.077784-0.Full Text Link to Item
-
Kiro, Ruth, Shahar Molshanski-Mor, Ido Yosef, Sara L. Milam, Harold P. Erickson, and Udi Qimron. “Gene product 0.4 increases bacteriophage T7 competitiveness by inhibiting host cell division.” Proc Natl Acad Sci U S A 110, no. 48 (November 26, 2013): 19549–54. https://doi.org/10.1073/pnas.1314096110.Full Text Open Access Copy Link to Item
-
Schumacher, Maria A., Nagababu Chinnam, Tomoo Ohashi, Riddhi Sanjay Shah, and Harold P. Erickson. “The structure of irisin reveals a novel intersubunit β-sheet fibronectin type III (FNIII) dimer: implications for receptor activation.” J Biol Chem 288, no. 47 (November 22, 2013): 33738–44. https://doi.org/10.1074/jbc.M113.516641.Full Text Open Access Copy Link to Item
-
Fouda, Genevieve G., Frederick H. Jaeger, Joshua D. Amos, Carrie Ho, Erika L. Kunz, Kara Anasti, Lisa W. Stamper, et al. “Tenascin-C is an innate broad-spectrum, HIV-1-neutralizing protein in breast milk.” Proc Natl Acad Sci U S A 110, no. 45 (November 5, 2013): 18220–25. https://doi.org/10.1073/pnas.1307336110.Full Text Open Access Copy Link to Item
-
Erickson, Harold P. “Irisin and FNDC5 in retrospect: An exercise hormone or a transmembrane receptor?” Adipocyte 2, no. 4 (October 1, 2013): 289–93. https://doi.org/10.4161/adip.26082.Full Text Open Access Copy Link to Item
-
Milam, Sara L., and Harold P. Erickson. “Rapid in vitro assembly of Caulobacter crescentus FtsZ protein at pH 6.5 and 7.2.” J Biol Chem 288, no. 33 (August 16, 2013): 23675–79. https://doi.org/10.1074/jbc.M113.491845.Full Text Open Access Copy Link to Item
-
Osawa, Masaki, and Harold P. Erickson. “Liposome division by a simple bacterial division machinery.” Proc Natl Acad Sci U S A 110, no. 27 (July 2, 2013): 11000–4. https://doi.org/10.1073/pnas.1222254110.Full Text Open Access Copy Link to Item
-
Gardner, Kiani AJ Arkus, Desmond A. Moore, and Harold P. Erickson. “The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide.” Mol Microbiol 89, no. 2 (July 2013): 264–75. https://doi.org/10.1111/mmi.12279.Full Text Open Access Copy Link to Item
-
Erickson, Harold P. “Bacterial actin homolog ParM: arguments for an apolar, antiparallel double helix.” J Mol Biol 422, no. 4 (September 28, 2012): 461–63. https://doi.org/10.1016/j.jmb.2012.05.019.Full Text Link to Item
-
Milam, Sara L., Masaki Osawa, and Harold P. Erickson. “Negative-stain electron microscopy of inside-out FtsZ rings reconstituted on artificial membrane tubules show ribbons of protofilaments.” Biophys J 103, no. 1 (July 3, 2012): 59–68. https://doi.org/10.1016/j.bpj.2012.05.035.Full Text Open Access Copy Link to Item
-
Chen, Yaodong, Sara L. Milam, and Harold P. Erickson. “SulA inhibits assembly of FtsZ by a simple sequestration mechanism.” Biochemistry 51, no. 14 (April 10, 2012): 3100–3109. https://doi.org/10.1021/bi201669d.Full Text Open Access Copy Link to Item
-
Erickson, Harold P. “Race disparity in grants: check the citations.” Science 334, no. 6058 (November 18, 2011): 899. https://doi.org/10.1126/science.334.6058.899-a.Full Text Open Access Copy Link to Item
-
Ohashi, Tomoo, and Harold P. Erickson. “Fibronectin aggregation and assembly: the unfolding of the second fibronectin type III domain.” J Biol Chem 286, no. 45 (November 11, 2011): 39188–99. https://doi.org/10.1074/jbc.M111.262337.Full Text Open Access Copy Link to Item
-
Lemmon, Christopher A., Tomoo Ohashi, and Harold P. Erickson. “Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.” J Biol Chem 286, no. 30 (July 29, 2011): 26375–82. https://doi.org/10.1074/jbc.M111.240028.Full Text Open Access Copy Link to Item
-
Osawa, Masaki, and Harold P. Erickson. “Inside-out Z rings--constriction with and without GTP hydrolysis.” Mol Microbiol 81, no. 2 (July 2011): 571–79. https://doi.org/10.1111/j.1365-2958.2011.07716.x.Full Text Open Access Copy Link to Item
-
Chen, Yaodong, and Harold P. Erickson. “Conformational changes of FtsZ reported by tryptophan mutants.” Biochemistry 50, no. 21 (May 31, 2011): 4675–84. https://doi.org/10.1021/bi200106d.Full Text Open Access Copy Link to Item
-
Erickson, Harold P., David E. Anderson, and Masaki Osawa. “FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.” Microbiol Mol Biol Rev 74, no. 4 (December 2010): 504–28. https://doi.org/10.1128/MMBR.00021-10.Full Text Open Access Copy Link to Item
-
Erickson, Harold P., and Masaki Osawa. “Cell division without FtsZ--a variety of redundant mechanisms.” Mol Microbiol 78, no. 2 (October 2010): 267–70. https://doi.org/10.1111/j.1365-2958.2010.07321.x.Full Text Open Access Copy Link to Item
-
Popp, David, Mitsusada Iwasa, Harold P. Erickson, Akihiro Narita, Yuichiro Maéda, and Robert C. Robinson. “Suprastructures and dynamic properties of Mycobacterium tuberculosis FtsZ.” J Biol Chem 285, no. 15 (April 9, 2010): 11281–89. https://doi.org/10.1074/jbc.M109.084079.Full Text Link to Item
-
Osawa, Masaki, David E. Anderson, and Harold P. Erickson. “Curved FtsZ protofilaments generate bending forces on liposome membranes.” Embo J 28, no. 22 (November 18, 2009): 3476–84. https://doi.org/10.1038/emboj.2009.277.Full Text Open Access Copy Link to Item
-
Kenjale, Roma, Guoyu Meng, Doran L. Fink, Twyla Juehne, Tomoo Ohashi, Harold P. Erickson, Gabriel Waksman, and Joseph W. St Geme. “Structural determinants of autoproteolysis of the Haemophilus influenzae Hap autotransporter.” Infect Immun 77, no. 11 (November 2009): 4704–13. https://doi.org/10.1128/IAI.00598-09.Full Text Link to Item
-
Sontag, Christopher A., Harvey Sage, and Harold P. Erickson. “BtubA-BtubB heterodimer is an essential intermediate in protofilament assembly.” Plos One 4, no. 9 (September 29, 2009): e7253. https://doi.org/10.1371/journal.pone.0007253.Full Text Link to Item
-
Chen, Yaodong, and Harold P. Erickson. “FtsZ filament dynamics at steady state: subunit exchange with and without nucleotide hydrolysis.” Biochemistry 48, no. 28 (July 21, 2009): 6664–73. https://doi.org/10.1021/bi8022653.Full Text Link to Item
-
Erickson, Harold P. “Modeling the physics of FtsZ assembly and force generation.” Proc Natl Acad Sci U S A 106, no. 23 (June 9, 2009): 9238–43. https://doi.org/10.1073/pnas.0902258106.Full Text Link to Item
-
Ohashi, Tomoo, Anne Marie Augustus, and Harold P. Erickson. “Transient opening of fibronectin type III (FNIII) domains: the interaction of the third FNIII domain of FN with anastellin.” Biochemistry 48, no. 19 (May 19, 2009): 4189–97. https://doi.org/10.1021/bi900001g.Full Text Link to Item
-
Erickson, Harold P. “Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy.” Biol Proced Online 11 (May 15, 2009): 32–51. https://doi.org/10.1007/s12575-009-9008-x.Full Text Link to Item
-
Popp, David, Mitsusada Iwasa, Akihiro Narita, Harold P. Erickson, and Yuichiro Maéda. “FtsZ condensates: an in vitro electron microscopy study.” Biopolymers 91, no. 5 (May 2009): 340–50. https://doi.org/10.1002/bip.21136.Full Text Link to Item
-
Ohashi, Tomoo, and Harold P. Erickson. “Revisiting the mystery of fibronectin multimers: the fibronectin matrix is composed of fibronectin dimers cross-linked by non-covalent bonds.” Matrix Biol 28, no. 3 (April 2009): 170–75. https://doi.org/10.1016/j.matbio.2009.03.002.Full Text Link to Item
-
White, Glenn E., and Harold P. Erickson. “The coiled coils of cohesin are conserved in animals, but not in yeast.” Plos One 4, no. 3 (2009): e4674. https://doi.org/10.1371/journal.pone.0004674.Full Text Link to Item
-
Xu, Jielin, Eunnyung Bae, Qinghong Zhang, Douglas S. Annis, Harold P. Erickson, and Deane F. Mosher. “Display of cell surface sites for fibronectin assembly is modulated by cell adherence to (1)F3 and C-terminal modules of fibronectin.” Plos One 4, no. 1 (2009): e4113. https://doi.org/10.1371/journal.pone.0004113.Full Text Open Access Copy Link to Item
-
Osawa, Masaki, and Harold P. Erickson. “Chapter 1 - Tubular liposomes with variable permeability for reconstitution of FtsZ rings.” Methods Enzymol 464 (2009): 3–17. https://doi.org/10.1016/S0076-6879(09)64001-5.Full Text Open Access Copy Link to Item
-
Osawa, M., D. A. Anderson, and H. P. Erickson. “Reconstitution of contractile FtsZ rings in liposomes.” Chemtracts 21, no. 6 (June 1, 2008): 222–23.
-
Osawa, Masaki, David E. Anderson, and Harold P. Erickson. “Reconstitution of contractile FtsZ rings in liposomes.” Science 320, no. 5877 (May 9, 2008): 792–94. https://doi.org/10.1126/science.1154520.Full Text Link to Item
-
Chen, Yaodong, and Harold P. Erickson. “In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from Bacillus plasmids: evidence for a capping mechanism.” J Biol Chem 283, no. 13 (March 28, 2008): 8102–9. https://doi.org/10.1074/jbc.M709163200.Full Text Link to Item
-
Moioli, Eduardo K., Paul A. Clark, Mo Chen, James E. Dennis, Helaman P. Erickson, Stanton L. Gerson, and Jeremy J. Mao. “Synergistic actions of hematopoietic and mesenchymal stem/progenitor cells in vascularizing bioengineered tissues.” Plos One 3, no. 12 (2008): e3922. https://doi.org/10.1371/journal.pone.0003922.Full Text Link to Item
-
Chen, Yaodong, David E. Anderson, Malini Rajagopalan, and Harold P. Erickson. “Assembly dynamics of Mycobacterium tuberculosis FtsZ.” J Biol Chem 282, no. 38 (September 21, 2007): 27736–43. https://doi.org/10.1074/jbc.M703788200.Full Text Link to Item
-
Takahashi, Seiichiro, Michael Leiss, Markus Moser, Tomoo Ohashi, Tomoe Kitao, Dominik Heckmann, Alexander Pfeifer, et al. “The RGD motif in fibronectin is essential for development but dispensable for fibril assembly.” J Cell Biol 178, no. 1 (July 2, 2007): 167–78. https://doi.org/10.1083/jcb.200703021.Full Text Link to Item
-
Ohashi, Tomoo, Stephane D. Galiacy, Gina Briscoe, and Harold P. Erickson. “An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins.” Protein Sci 16, no. 7 (July 2007): 1429–38. https://doi.org/10.1110/ps.072845607.Full Text Link to Item
-
Erickson, Harold P. “Evolution of the cytoskeleton.” Bioessays 29, no. 7 (July 2007): 668–77. https://doi.org/10.1002/bies.20601.Full Text Link to Item
-
Ng, Sean P., Kate S. Billings, Tomoo Ohashi, Mark D. Allen, Robert B. Best, Lucy G. Randles, Harold P. Erickson, and Jane Clarke. “Designing an extracellular matrix protein with enhanced mechanical stability.” Proc Natl Acad Sci U S A 104, no. 23 (June 5, 2007): 9633–37. https://doi.org/10.1073/pnas.0609901104.Full Text Link to Item
-
Osawa, Masaki, and Harold P. Erickson. “FtsZ from divergent foreign bacteria can function for cell division in Escherichia coli.” J Bacteriol 188, no. 20 (October 2006): 7132–40. https://doi.org/10.1128/JB.00647-06.Full Text Link to Item
-
White, Glenn E., and Harold P. Erickson. “Sequence divergence of coiled coils--structural rods, myosin filament packing, and the extraordinary conservation of cohesins.” J Struct Biol 154, no. 2 (May 2006): 111–21. https://doi.org/10.1016/j.jsb.2006.01.001.Full Text Link to Item
-
Abu-Lail, Nehal I., Tomoo Ohashi, Robert L. Clark, Harold P. Erickson, and Stefan Zauscher. “Understanding the elasticity of fibronectin fibrils: unfolding strengths of FN-III and GFP domains measured by single molecule force spectroscopy.” Matrix Biol 25, no. 3 (April 2006): 175–84. https://doi.org/10.1016/j.matbio.2005.10.007.Full Text Link to Item
-
Osawa, Masaki, and Harold P. Erickson. “Probing the domain structure of FtsZ by random truncation and insertion of GFP.” Microbiology (Reading) 151, no. Pt 12 (December 2005): 4033–43. https://doi.org/10.1099/mic.0.28219-0.Full Text Link to Item
-
Ohashi, Tomoo, and Harold P. Erickson. “Domain unfolding plays a role in superfibronectin formation.” J Biol Chem 280, no. 47 (November 25, 2005): 39143–51. https://doi.org/10.1074/jbc.M509082200.Full Text Link to Item
-
Chen, Yaodong, and Harold P. Erickson. “Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer.” J Biol Chem 280, no. 23 (June 10, 2005): 22549–54. https://doi.org/10.1074/jbc.M500895200.Full Text Link to Item
-
Sontag, Christopher A., James T. Staley, and Harold P. Erickson. “In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB.” J Cell Biol 169, no. 2 (April 25, 2005): 233–38. https://doi.org/10.1083/jcb.200410027.Full Text Link to Item
-
Redick, Sambra D., Jesse Stricker, Gina Briscoe, and Harold P. Erickson. “Mutants of FtsZ targeting the protofilament interface: effects on cell division and GTPase activity.” J Bacteriol 187, no. 8 (April 2005): 2727–36. https://doi.org/10.1128/JB.187.8.2727-2736.2005.Full Text Link to Item
-
Chen, Yaodong, Keith Bjornson, Sambra D. Redick, and Harold P. Erickson. “A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus.” Biophys J 88, no. 1 (January 2005): 505–14. https://doi.org/10.1529/biophysj.104.044149.Full Text Link to Item
-
Anderson, David E., Frederico J. Gueiros-Filho, and Harold P. Erickson. “Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins.” J Bacteriol 186, no. 17 (September 2004): 5775–81. https://doi.org/10.1128/JB.186.17.5775-5781.2004.Full Text Link to Item
-
Ingham, Kenneth C., Shelesa A. Brew, and Harold P. Erickson. “Localization of a cryptic binding site for tenascin on fibronectin.” J Biol Chem 279, no. 27 (July 2, 2004): 28132–35. https://doi.org/10.1074/jbc.M312785200.Full Text Link to Item
-
Ohashi, Tomoo, and Harold P. Erickson. “The disulfide bonding pattern in ficolin multimers.” J Biol Chem 279, no. 8 (February 20, 2004): 6534–39. https://doi.org/10.1074/jbc.M310555200.Full Text Link to Item
-
Stricker, Jesse, and Harold P. Erickson. “In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function.” J Bacteriol 185, no. 16 (August 2003): 4796–4805. https://doi.org/10.1128/JB.185.16.4796-4805.2003.Full Text Link to Item
-
Caplan, Michael R., and Harold P. Erickson. “Apparent cooperative assembly of the bacterial cell division protein FtsZ demonstrated by isothermal titration calorimetry.” J Biol Chem 278, no. 16 (April 18, 2003): 13784–88. https://doi.org/10.1074/jbc.M300860200.Full Text Link to Item
-
Doudna Cate, J. H., and H. P. Erickson. “Macromolecular assemblages - Many structures to function.” Current Opinion in Structural Biology 13, no. 2 (April 1, 2003): 203–5. https://doi.org/10.1016/S0959-440X(03)00043-5.Full Text
-
Li, Feiya, Sambra D. Redick, Harold P. Erickson, and Vincent T. Moy. “Force measurements of the alpha5beta1 integrin-fibronectin interaction.” Biophys J 84, no. 2 Pt 1 (February 2003): 1252–62. https://doi.org/10.1016/S0006-3495(03)74940-6.Full Text Link to Item
-
Ohashi, Tomoo, Cynthia A. Hale, Piet A. J. de Boer, and Harold P. Erickson. “Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain.” J Bacteriol 184, no. 15 (August 2002): 4313–15. https://doi.org/10.1128/JB.184.15.4313-4315.2002.Full Text Link to Item
-
Ghert, Michelle A., Wen-ning Qi, Harold P. Erickson, Joel A. Block, and Sean P. Scully. “Tenascin-C expression and distribution in cultured human chondrocytes and chondrosarcoma cells.” J Orthop Res 20, no. 4 (July 2002): 834–41. https://doi.org/10.1016/S0736-0266(01)00172-3.Full Text Link to Item
-
Coussen, F., D. Choquet, M. P. Sheetz, and H. P. Erickson. “Trimers of the fivronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation.” Journal of Cell Science 115, no. 12 (June 15, 2002): 2581–90.
-
Coussen, Françoise, Daniel Choquet, Michael P. Sheetz, and Harold P. Erickson. “Trimers of the fibronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation.” J Cell Sci 115, no. Pt 12 (June 15, 2002): 2581–90. https://doi.org/10.1242/jcs.115.12.2581.Full Text Link to Item
-
Takagi, Junichi, Daniel P. DeBottis, Harold P. Erickson, and Timothy A. Springer. “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.” Biochemistry 41, no. 13 (April 2, 2002): 4339–47. https://doi.org/10.1021/bi016047u.Full Text Link to Item
-
Ohashi, Tomoo, Daniel P. Kiehart, and Harold P. Erickson. “Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants.” J Cell Sci 115, no. Pt 6 (March 15, 2002): 1221–29. https://doi.org/10.1242/jcs.115.6.1221.Full Text Link to Item
-
Stricker, Jesse, Paul Maddox, E. D. Salmon, and Harold P. Erickson. “Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching.” Proc Natl Acad Sci U S A 99, no. 5 (March 5, 2002): 3171–75. https://doi.org/10.1073/pnas.052595099.Full Text Link to Item
-
Anderson, David E., Ana Losada, Harold P. Erickson, and Tatsuya Hirano. “Condensin and cohesin display different arm conformations with characteristic hinge angles.” J Cell Biol 156, no. 3 (February 4, 2002): 419–24. https://doi.org/10.1083/jcb.200111002.Full Text Link to Item
-
Erickson, Harold P. “Stretching fibronectin.” J Muscle Res Cell Motil 23, no. 5–6 (2002): 575–80. https://doi.org/10.1023/a:1023427026818.Full Text Link to Item
-
Haspel, J., G. Schürmann, J. Jacob, H. P. Erickson, and M. Grumet. “Disulfide-mediated dimerization of L1 Ig domains.” J Neurosci Res 66, no. 3 (November 1, 2001): 347–55. https://doi.org/10.1002/jnr.1227.Full Text Link to Item
-
Anderson, D. E., K. M. Trujillo, P. Sung, and H. P. Erickson. “Structure of the Rad50 x Mre11 DNA repair complex from Saccharomyces cerevisiae by electron microscopy.” J Biol Chem 276, no. 40 (October 5, 2001): 37027–33. https://doi.org/10.1074/jbc.M106179200.Full Text Link to Item
-
Cassimeris, L., D. Gard, P. T. Tran, and H. P. Erickson. “XMAP215 is a long thin molecule that does not increase microtubule stiffness.” Journal of Cell Science 114, no. 16 (September 17, 2001): 3025–33.
-
Li, H., A. F. Oberhauser, S. D. Redick, M. Carrion-Vazquez, H. P. Erickson, and J. M. Fernandez. “Multiple conformations of PEVK proteins detected by single-molecule techniques.” Proc Natl Acad Sci U S A 98, no. 19 (September 11, 2001): 10682–86. https://doi.org/10.1073/pnas.191189098.Full Text Link to Item
-
Erickson, H. P. “Cytoskeleton. Evolution in bacteria.” Nature 413, no. 6851 (September 6, 2001): 30. https://doi.org/10.1038/35092655.Full Text Link to Item
-
Erickson, H. P. “Cytoskeleton. Evolution in bacteria.” Nature 413, no. 6851 (September 2001): 30.
-
Jun, C. D., C. V. Carman, S. D. Redick, M. Shimaoka, H. P. Erickson, and T. A. Springer. “Ultrastructure and function of dimeric, soluble intercellular adhesion molecule-1 (ICAM-1).” J Biol Chem 276, no. 31 (August 3, 2001): 29019–27. https://doi.org/10.1074/jbc.M103394200.Full Text Link to Item
-
Cassimeris, L., D. Gard, P. T. Tran, and H. P. Erickson. “XMAP215 is a long thin molecule that does not increase microtubule stiffness.” J Cell Sci 114, no. Pt 16 (August 2001): 3025–33. https://doi.org/10.1242/jcs.114.16.3025.Full Text Link to Item
-
Hirano, M., D. E. Anderson, H. P. Erickson, and T. Hirano. “Bimodal activation of SMC ATPase by intra- and inter-molecular interactions.” Embo J 20, no. 12 (June 15, 2001): 3238–50. https://doi.org/10.1093/emboj/20.12.3238.Full Text Link to Item
-
Ghert, M. A., W. N. Qi, H. P. Erickson, J. A. Block, and S. P. Scully. “Tenascin-C splice variant adhesive/anti-adhesive effects on chondrosarcoma cell attachment to fibronectin.” Cell Struct Funct 26, no. 3 (June 2001): 179–87. https://doi.org/10.1247/csf.26.179.Full Text Link to Item
-
Schürmann, G., J. Haspel, M. Grumet, and H. P. Erickson. “Cell adhesion molecule L1 in folded (horseshoe) and extended conformations.” Mol Biol Cell 12, no. 6 (June 2001): 1765–73. https://doi.org/10.1091/mbc.12.6.1765.Full Text Link to Item
-
Lu, C., J. Stricker, and H. P. Erickson. “Site-specific mutations of FtsZ - Effects on GTPase and in vitro assembly.” Bmc Microbiology 1 (May 24, 2001): 1–12. https://doi.org/10.1186/1471-2180-1-1.Full Text
-
Takagi, J., H. P. Erickson, and T. A. Springer. “C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1.” Nat Struct Biol 8, no. 5 (May 2001): 412–16. https://doi.org/10.1038/87569.Full Text Link to Item
-
Romberg, L., M. Simon, and H. P. Erickson. “Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?” J Biol Chem 276, no. 15 (April 13, 2001): 11743–53. https://doi.org/10.1074/jbc.M009033200.Full Text Link to Item
-
Sakai, T., K. J. Johnson, M. Murozono, K. Sakai, M. A. Magnuson, T. Wieloch, T. Cronberg, A. Isshiki, H. P. Erickson, and R. Fässler. “Plasma fibronectin supports neuronal survival and reduces brain injury following transient focal cerebral ischemia but is not essential for skin-wound healing and hemostasis.” Nat Med 7, no. 3 (March 2001): 324–30. https://doi.org/10.1038/85471.Full Text Link to Item
-
Erickson, H. P. “The FtsZ protofilament and attachment of ZipA--structural constraints on the FtsZ power stroke.” Curr Opin Cell Biol 13, no. 1 (February 2001): 55–60. https://doi.org/10.1016/s0955-0674(00)00174-5.Full Text Link to Item
-
Ghert, M. A., S. T. Jung, W. Qi, J. M. Harrelson, H. P. Erickson, J. A. Block, and S. P. Scully. “The clinical significance of tenascin-C splice variant expression in chondrosarcoma.” Oncology 61, no. 4 (2001): 306–14. https://doi.org/10.1159/000055338.Full Text Link to Item
-
Lu, C., J. Stricker, and H. P. Erickson. “Site-specific mutations of FtsZ--effects on GTPase and in vitro assembly.” Bmc Microbiol 1 (2001): 7. https://doi.org/10.1186/1471-2180-1-7.Full Text Link to Item
-
Champagne, M. B., K. A. Edwards, H. P. Erickson, and D. P. Kiehart. “Drosophila stretchin-MLCK is a novel member of the Titin/Myosin light chain kinase family.” J Mol Biol 300, no. 4 (July 21, 2000): 759–77. https://doi.org/10.1006/jmbi.2000.3802.Full Text Link to Item
-
Yokoyama, K., H. P. Erickson, Y. Ikeda, and Y. Takada. “Identification of amino acid sequences in fibrinogen gamma -chain and tenascin C C-terminal domains critical for binding to integrin alpha vbeta 3.” J Biol Chem 275, no. 22 (June 2, 2000): 16891–98. https://doi.org/10.1074/jbc.M000610200.Full Text Link to Item
-
Erickson, H. P. “Gamma-tubulin nucleation: template or protofilament?” Nat Cell Biol 2, no. 6 (June 2000): E93–96. https://doi.org/10.1038/35014084.Full Text Link to Item
-
Redick, S. D., D. L. Settles, G. Briscoe, and H. P. Erickson. “Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis.” J Cell Biol 149, no. 2 (April 17, 2000): 521–27. https://doi.org/10.1083/jcb.149.2.521.Full Text Link to Item
-
Erickson, H. P. “Dynamin and FtsZ. Missing links in mitochondrial and bacterial division.” J Cell Biol 148, no. 6 (March 20, 2000): 1103–5. https://doi.org/10.1083/jcb.148.6.1103.Full Text Link to Item
-
Fong, A. M., H. P. Erickson, J. P. Zachariah, S. Poon, N. J. Schamberg, T. Imai, and D. D. Patel. “Ultrastructure and function of the fractalkine mucin domain in CX(3)C chemokine domain presentation.” J Biol Chem 275, no. 6 (February 11, 2000): 3781–86. https://doi.org/10.1074/jbc.275.6.3781.Full Text Link to Item
-
Lu, C., M. Reedy, and H. P. Erickson. “Straight and curved conformations of FtsZ are regulated by GTP hydrolysis.” J Bacteriol 182, no. 1 (January 2000): 164–70. https://doi.org/10.1128/JB.182.1.164-170.2000.Full Text Link to Item
-
Lu, C., and H. P. Erickson. “The straight and curved conformation of FtsZ protofilaments-evidence for rapid exchange of GTP into the curved protofilament.” Cell Struct Funct 24, no. 5 (October 1999): 285–90. https://doi.org/10.1247/csf.24.285.Full Text Link to Item
-
Johnson, K. J., H. Sage, G. Briscoe, and H. P. Erickson. “The compact conformation of fibronectin is determined by intramolecular ionic interactions.” J Biol Chem 274, no. 22 (May 28, 1999): 15473–79. https://doi.org/10.1074/jbc.274.22.15473.Full Text Link to Item
-
Ohashi, T., D. P. Kiehart, and H. P. Erickson. “Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein.” Proc Natl Acad Sci U S A 96, no. 5 (March 2, 1999): 2153–58. https://doi.org/10.1073/pnas.96.5.2153.Full Text Link to Item
-
Fuller, S. D., and H. P. Erickson. “Macramolecular assemblages. Editorial overview.” Current Opinion in Structural Biology 9, no. 2 (January 1, 1999): 213–14. https://doi.org/10.1016/S0959-440X(99)80030-X.Full Text
-
Ohashi, T., and H. P. Erickson. “Oligomeric structure and tissue distribution of ficolins from mouse, pig and human.” Arch Biochem Biophys 360, no. 2 (December 15, 1998): 223–32. https://doi.org/10.1006/abbi.1998.0957.Full Text Link to Item
-
Kumar, J., H. P. Erickson, and M. P. Sheetz. “Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin.” J Biol Chem 273, no. 48 (November 27, 1998): 31738–43. https://doi.org/10.1074/jbc.273.48.31738.Full Text Link to Item
-
Melby, T. E., C. N. Ciampaglio, G. Briscoe, and H. P. Erickson. “The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge.” J Cell Biol 142, no. 6 (September 21, 1998): 1595–1604. https://doi.org/10.1083/jcb.142.6.1595.Full Text Link to Item
-
Oberhauser, A. F., P. E. Marszalek, H. P. Erickson, and J. M. Fernandez. “The molecular elasticity of the extracellular matrix protein tenascin.” Nature 393, no. 6681 (May 14, 1998): 181–85. https://doi.org/10.1038/30270.Full Text Link to Item
-
Denda, S., U. Müller, K. L. Crossin, H. P. Erickson, and L. F. Reichardt. “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.” Biochemistry 37, no. 16 (April 21, 1998): 5464–74. https://doi.org/10.1021/bi9727489.Full Text Link to Item
-
Erickson, H. P. “Atomic structures of tubulin and FtsZ.” Trends Cell Biol 8, no. 4 (April 1998): 133–37. https://doi.org/10.1016/s0962-8924(98)01237-9.Full Text Link to Item
-
Seiffert, M., S. C. Beck, F. Schermutzki, C. A. Müller, H. P. Erickson, and G. Klein. “Mitogenic and adhesive effects of tenascin-C on human hematopoietic cells are mediated by various functional domains.” Matrix Biol 17, no. 1 (April 1998): 47–63. https://doi.org/10.1016/s0945-053x(98)90124-x.Full Text Link to Item
-
Akke, M., J. Liu, J. Cavanagh, H. P. Erickson, and A. G. Palmer. “Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain.” Nat Struct Biol 5, no. 1 (January 1998): 55–59. https://doi.org/10.1038/nsb0198-55.Full Text Link to Item
-
Lu, C., J. Stricker, and H. P. Erickson. “FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima--quantitation, GTP hydrolysis, and assembly.” Cell Motil Cytoskeleton 40, no. 1 (1998): 71–86. https://doi.org/10.1002/(SICI)1097-0169(1998)40:1<71::AID-CM7>3.0.CO;2-I.Full Text Link to Item
-
Lu, C., and H. P. Erickson. “Purification and assembly of FtsZ.” Methods Enzymol 298 (1998): 305–13. https://doi.org/10.1016/s0076-6879(98)98027-2.Full Text Link to Item
-
Lu, C., and H. P. Erickson. “Expression in Escherichia coli of the thermostable DNA polymerase from Pyrococcus furiosus.” Protein Expr Purif 11, no. 2 (November 1997): 179–84. https://doi.org/10.1006/prep.1997.0775.Full Text Link to Item
-
Siever, D. A., and H. P. Erickson. “Extracellular annexin II.” Int J Biochem Cell Biol 29, no. 11 (November 1997): 1219–23. https://doi.org/10.1016/s1357-2725(97)00057-5.Full Text Link to Item
-
Mehta, P., K. D. Patel, T. M. Laue, H. P. Erickson, and R. P. McEver. “Soluble monomeric P-selectin containing only the lectin and epidermal growth factor domains binds to P-selectin glycoprotein ligand-1 on leukocytes.” Blood 90, no. 6 (September 15, 1997): 2381–89.Link to Item
-
Erickson, H. P. “A tenascin knockout with a phenotype.” Nat Genet 17, no. 1 (September 1997): 5–7. https://doi.org/10.1038/ng0997-5.Full Text Link to Item
-
Erickson, H. P. “FtsZ, a tubulin homologue in prokaryote cell division.” Trends Cell Biol 7, no. 9 (September 1997): 362–67. https://doi.org/10.1016/S0962-8924(97)01108-2.Full Text Link to Item
-
Carr, P. A., H. P. Erickson, and A. G. Palmer. “Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin.” Structure 5, no. 7 (July 15, 1997): 949–59. https://doi.org/10.1016/S0969-2126(97)00248-7.Full Text Link to Item
-
Chung, C. Y., and H. P. Erickson. “Glycosaminoglycans modulate fibronectin matrix assembly and are essential for matrix incorporation of tenascin-C.” J Cell Sci 110 ( Pt 12) (June 1997): 1413–19. https://doi.org/10.1242/jcs.110.12.1413.Full Text Link to Item
-
Ohashi, T., and H. P. Erickson. “Two oligomeric forms of plasma ficolin have differential lectin activity.” J Biol Chem 272, no. 22 (May 30, 1997): 14220–26. https://doi.org/10.1074/jbc.272.22.14220.Full Text Link to Item
-
Erickson, H. P. “Stretching single protein molecules: titin is a weird spring.” Science 276, no. 5315 (May 16, 1997): 1090–92. https://doi.org/10.1126/science.276.5315.1090.Full Text Link to Item
-
Clark, R. A., H. P. Erickson, and T. A. Springer. “Tenascin supports lymphocyte rolling.” J Cell Biol 137, no. 3 (May 5, 1997): 755–65. https://doi.org/10.1083/jcb.137.3.755.Full Text Link to Item
-
O’Brien, E. T., E. D. Salmon, and H. P. Erickson. “How Calicum Causes Microtubule Depolymerization.” Cell Motility and the Cytoskeleton 36, no. 2 (1997): 125. https://doi.org/10.1002/(SICI)1097-0169(1997)36:23.0.CO;2-8.Full Text Link to Item
-
O’Brien, E. T., E. D. Salmon, and H. P. Erickson. “How calcium causes microtubule depolymerization.” Cell Motil Cytoskeleton 36, no. 2 (1997): 125–35. https://doi.org/10.1002/(SICI)1097-0169(1997)36:2<125::AID-CM3>3.0.CO;2-8.Full Text Link to Item
-
Settles, D. L., M. Kusakabe, D. A. Steindler, H. Fillmore, and H. P. Erickson. “Tenascin-C knockout mouse has no detectable tenascin-C protein.” J Neurosci Res 47, no. 1 (January 1, 1997): 109–17.Link to Item
-
Erickson, H. P., and D. Stoffler. “Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to alpha/beta and gamma tubulin.” J Cell Biol 135, no. 1 (October 1996): 5–8. https://doi.org/10.1083/jcb.135.1.5.Full Text Link to Item
-
LeMosy, E. K., V. A. Lightner, and H. P. Erickson. “Structural analysis of a human glial variant laminin.” Exp Cell Res 227, no. 1 (August 25, 1996): 80–88. https://doi.org/10.1006/excr.1996.0252.Full Text Link to Item
-
Chung, C. Y., J. E. Murphy-Ullrich, and H. P. Erickson. “Mitogenesis, cell migration, and loss of focal adhesions induced by tenascin-C interacting with its cell surface receptor, annexin II.” Mol Biol Cell 7, no. 6 (June 1996): 883–92. https://doi.org/10.1091/mbc.7.6.883.Full Text Link to Item
-
Li, F., H. P. Erickson, J. A. James, K. L. Moore, R. D. Cummings, and R. P. McEver. “Visualization of P-selectin glycoprotein ligand-1 as a highly extended molecule and mapping of protein epitopes for monoclonal antibodies.” J Biol Chem 271, no. 11 (March 15, 1996): 6342–48. https://doi.org/10.1074/jbc.271.11.6342.Full Text Link to Item
-
Savarese, J. J., H. Erickson, and S. P. Scully. “Articular chondrocyte tenascin-C production and assembly into de novo extracellular matrix.” J Orthop Res 14, no. 2 (March 1996): 273–81. https://doi.org/10.1002/jor.1100140216.Full Text Link to Item
-
Settles, D. L., R. A. Cihak, and H. P. Erickson. “Tenascin-C expression in dystrophin-related muscular dystrophy.” Muscle Nerve 19, no. 2 (February 1996): 147–54. https://doi.org/10.1002/(SICI)1097-4598(199602)19:2<147::AID-MUS4>3.0.CO;2-E.Full Text Link to Item
-
Leahy, D. J., I. Aukhil, and H. P. Erickson. “2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region.” Cell 84, no. 1 (January 12, 1996): 155–64. https://doi.org/10.1016/s0092-8674(00)81002-8.Full Text Link to Item
-
Erickson, H. P., D. W. Taylor, K. A. Taylor, and D. Bramhill. “Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers.” Proc Natl Acad Sci U S A 93, no. 1 (January 9, 1996): 519–23. https://doi.org/10.1073/pnas.93.1.519.Full Text Link to Item
-
Chung, C. Y., L. Zardi, and H. P. Erickson. “Binding of tenascin-C to soluble fibronectin and matrix fibrils.” J Biol Chem 270, no. 48 (December 1, 1995): 29012–17. https://doi.org/10.1074/jbc.270.48.29012.Full Text Link to Item
-
Burns, C. G., D. A. Larochelle, H. Erickson, M. Reedy, and A. De Lozanne. “Single-headed myosin II acts as a dominant negative mutation in Dictyostelium.” Proc Natl Acad Sci U S A 92, no. 18 (August 29, 1995): 8244–48. https://doi.org/10.1073/pnas.92.18.8244.Full Text Link to Item
-
Qiao, T., B. K. Maddox, and H. P. Erickson. “A novel alternative splice domain in zebrafish tenascin-C.” Gene 156, no. 2 (April 24, 1995): 307–8. https://doi.org/10.1016/0378-1119(95)00039-9.Full Text Link to Item
-
Steindler, D. A., D. Settles, H. P. Erickson, E. D. Laywell, A. Yoshiki, A. Faissner, and M. Kusakabe. “Tenascin knockout mice: barrels, boundary molecules, and glial scars.” J Neurosci 15, no. 3 Pt 1 (March 1995): 1971–83. https://doi.org/10.1523/JNEUROSCI.15-03-01971.1995.Full Text Link to Item
-
Erickson, H. P. “FtsZ, a prokaryotic homolog of tubulin?” Cell 80, no. 3 (February 10, 1995): 367–70. https://doi.org/10.1016/0092-8674(95)90486-7.Full Text Link to Item
-
Jones, P. L., N. Boudreau, C. A. Myers, H. P. Erickson, and M. J. Bissell. “Tenascin-C inhibits extracellular matrix-dependent gene expression in mammary epithelial cells. Localization of active regions using recombinant tenascin fragments.” J Cell Sci 108 ( Pt 2) (February 1995): 519–27. https://doi.org/10.1242/jcs.108.2.519.Full Text Link to Item
-
Erickson, H. P. “Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin.” Proc Natl Acad Sci U S A 91, no. 21 (October 11, 1994): 10114–18. https://doi.org/10.1073/pnas.91.21.10114.Full Text Link to Item
-
Sadhu, C., B. Lipsky, H. P. Erickson, J. Hayflick, K. O. Dick, W. M. Gallatin, and D. E. Staunton. “LFA-1 binding site in ICAM-3 contains a conserved motif and non-contiguous amino acids.” Cell Adhes Commun 2, no. 5 (October 1994): 429–40. https://doi.org/10.3109/15419069409004453.Full Text Link to Item
-
Chung, C. Y., and H. P. Erickson. “Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C.” J Cell Biol 126, no. 2 (July 1994): 539–48. https://doi.org/10.1083/jcb.126.2.539.Full Text Link to Item
-
Leahy, D. J., H. P. Erickson, I. Aukhil, P. Joshi, and W. A. Hendrickson. “Crystallization of a fragment of human fibronectin: introduction of methionine by site-directed mutagenesis to allow phasing via selenomethionine.” Proteins 19, no. 1 (May 1994): 48–54. https://doi.org/10.1002/prot.340190107.Full Text Link to Item
-
Julian, J., R. Chiquet-Ehrismann, H. P. Erickson, and D. D. Carson. “Tenascin is induced at implantation sites in the mouse uterus and interferes with epithelial cell adhesion.” Development 120, no. 3 (March 1994): 661–71. https://doi.org/10.1242/dev.120.3.661.Full Text Link to Item
-
Rettig, W. J., H. P. Erickson, A. P. Albino, and P. Garin-Chesa. “Induction of human tenascin (neuronectin) by growth factors and cytokines: cell type-specific signals and signalling pathways.” J Cell Sci 107 ( Pt 2) (February 1994): 487–97.Link to Item
-
Young, S. L., L. Y. Chang, and H. P. Erickson. “Tenascin-C in rat lung: distribution, ontogeny and role in branching morphogenesis.” Dev Biol 161, no. 2 (February 1994): 615–25. https://doi.org/10.1006/dbio.1994.1057.Full Text Link to Item
-
Erickson, H. P. “Evolution of the tenascin family--implications for function of the C-terminal fibrinogen-like domain.” Perspect Dev Neurobiol 2, no. 1 (1994): 9–19. https://doi.org/10.1080/0907676x.1994.9961218.Full Text Link to Item
-
Perides, G., H. P. Erickson, F. Rahemtulla, and A. Bignami. “Colocalization of tenascin with versican, a hyaluronate-binding chondroitin sulfate proteoglycan.” Anat Embryol (Berl) 188, no. 5 (November 1993): 467–79. https://doi.org/10.1007/BF00190141.Full Text Link to Item
-
Erickson, H. P. “Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions.” Curr Opin Cell Biol 5, no. 5 (October 1993): 869–76. https://doi.org/10.1016/0955-0674(93)90037-q.Full Text Link to Item
-
Joshi, P., C. Y. Chung, I. Aukhil, and H. P. Erickson. “Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin.” J Cell Sci 106 ( Pt 1) (September 1993): 389–400. https://doi.org/10.1242/jcs.106.1.389.Full Text Link to Item
-
Ushiyama, S., T. M. Laue, K. L. Moore, H. P. Erickson, and R. P. McEver. “Structural and functional characterization of monomeric soluble P-selectin and comparison with membrane P-selectin.” J Biol Chem 268, no. 20 (July 15, 1993): 15229–37.Link to Item
-
Chandra, R., E. D. Salmon, H. P. Erickson, A. Lockhart, and S. A. Endow. “Structural and functional domains of the Drosophila ncd microtubule motor protein.” J Biol Chem 268, no. 12 (April 25, 1993): 9005–13.Link to Item
-
Erickson, H. P. “Gene knockouts of c-src, transforming growth factor beta 1, and tenascin suggest superfluous, nonfunctional expression of proteins.” J Cell Biol 120, no. 5 (March 1993): 1079–81. https://doi.org/10.1083/jcb.120.5.1079.Full Text Link to Item
-
Aukhil, I., P. Joshi, Y. Yan, and H. P. Erickson. “Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins.” J Biol Chem 268, no. 4 (February 5, 1993): 2542–53.Link to Item
-
Erickson, H., and K. Holmes. “Editorial overview.” Current Opinion in Structural Biology 3, no. 2 (January 1, 1993): 165–66. https://doi.org/10.1016/S0959-440X(05)80147-2.Full Text
-
Erickson, H., and K. Holmes. “Macromolecular assemblages.” Current Opinion in Structural Biology 3, no. 2 (1993): 165–66.
-
Goodsell, D. S., and P. Erickson Harold. “Machinery of life.” Nature 365, no. 6444 (1993): 306.
-
Vollmer, G., V. A. Lightner, C. A. Carter, G. P. Siegal, H. P. Erickson, R. Knuppen, and D. G. Kaufman. “Localization of tenascin in uterine sarcomas and partially transformed endometrial stromal cells.” Pathobiology 61, no. 2 (1993): 67–76. https://doi.org/10.1159/000163763.Full Text Link to Item
-
Schaefer, E. M., H. P. Erickson, M. Federwisch, A. Wollmer, and L. Ellis. “Structural organization of the human insulin receptor ectodomain.” J Biol Chem 267, no. 32 (November 15, 1992): 23393–402.Link to Item
-
Leahy, D. J., W. A. Hendrickson, I. Aukhil, and H. P. Erickson. “Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein.” Science 258, no. 5084 (November 6, 1992): 987–91. https://doi.org/10.1126/science.1279805.Full Text Link to Item
-
LeMosy, E. K., H. P. Erickson, W. F. Beyer, J. T. Radek, J. M. Jeong, S. N. Murthy, and L. Lorand. “Visualization of purified fibronectin-transglutaminase complexes.” J Biol Chem 267, no. 11 (April 15, 1992): 7880–85.Link to Item
-
Northrup, S. H., and H. P. Erickson. “Kinetics of protein-protein association explained by Brownian dynamics computer simulation.” Proc Natl Acad Sci U S A 89, no. 8 (April 15, 1992): 3338–42. https://doi.org/10.1073/pnas.89.8.3338.Full Text Link to Item
-
Erickson, H. P., and E. T. O’Brien. “Microtubule dynamic instability and GTP hydrolysis.” Annu Rev Biophys Biomol Struct 21 (1992): 145–66. https://doi.org/10.1146/annurev.bb.21.060192.001045.Full Text Link to Item
-
Murphy-Ullrich, J. E., V. A. Lightner, I. Aukhil, Y. Z. Yan, H. P. Erickson, and M. Höök. “Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin.” J Cell Biol 115, no. 4 (November 1991): 1127–36. https://doi.org/10.1083/jcb.115.4.1127.Full Text Link to Item
-
Voter, W. A., E. T. O’Brien, and H. P. Erickson. “Dilution-induced disassembly of microtubules: relation to dynamic instability and the GTP cap.” Cell Motil Cytoskeleton 18, no. 1 (1991): 55–62. https://doi.org/10.1002/cm.970180106.Full Text Link to Item
-
O’Brien, E. T., E. D. Salmon, R. A. Walker, and H. P. Erickson. “Effects of magnesium on the dynamic instability of individual microtubules.” Biochemistry 29, no. 28 (July 17, 1990): 6648–56. https://doi.org/10.1021/bi00480a014.Full Text Link to Item
-
Neely, M. D., H. P. Erickson, and K. Boekelheide. “HMW-2, the Sertoli cell cytoplasmic dynein from rat testis, is a dimer composed of nearly identical subunits.” J Biol Chem 265, no. 15 (May 25, 1990): 8691–98.Link to Item
-
Aukhil, I., C. C. Slemp, V. A. Lightner, K. Nishimura, G. Briscoe, and H. P. Erickson. “Purification of hexabrachion (tenascin) from cell culture conditioned medium, and separation from a cell adhesion factor.” Matrix 10, no. 2 (May 1990): 98–111. https://doi.org/10.1016/s0934-8832(11)80176-9.Full Text Link to Item
-
Staunton, D. E., M. L. Dustin, H. P. Erickson, and T. A. Springer. “The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus.” Cell 61, no. 2 (April 20, 1990): 243–54. https://doi.org/10.1016/0092-8674(90)90805-o.Full Text Link to Item
-
Lightner, V. A., and H. P. Erickson. “Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion.” J Cell Sci 95 ( Pt 2) (February 1990): 263–77. https://doi.org/10.1242/jcs.95.2.263.Full Text Link to Item
-
Lightner, V. A., C. A. Slemp, and H. P. Erickson. “Localization and quantitation of hexabrachion (tenascin) in skin, embryonic brain, tumors, and plasma.” Ann N Y Acad Sci 580 (1990): 260–75. https://doi.org/10.1111/j.1749-6632.1990.tb17935.x.Full Text Link to Item
-
Lotz, M. M., C. A. Burdsal, H. P. Erickson, and D. R. McClay. “Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response.” J Cell Biol 109, no. 4 Pt 1 (October 1989): 1795–1805. https://doi.org/10.1083/jcb.109.4.1795.Full Text Link to Item
-
Lotz, M. M., C. A. Burdsal, H. P. Erickson, and D. R. McClay. “Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response.” The Journal of Cell Biology 109, no. 4 Pt 1 (October 1989): 1795–1805. https://doi.org/10.1083/jcb.109.4.1795.Full Text
-
Taylor, H. C., V. A. Lightner, W. F. Beyer, D. McCaslin, G. Briscoe, and H. P. Erickson. “Biochemical and structural studies of tenascin/hexabrachion proteins.” J Cell Biochem 41, no. 2 (October 1989): 71–90. https://doi.org/10.1002/jcb.240410204.Full Text Link to Item
-
Lightner, V. A., F. Gumkowski, D. D. Bigner, and H. P. Erickson. “Tenascin/hexabrachion in human skin: biochemical identification and localization by light and electron microscopy.” J Cell Biol 108, no. 6 (June 1989): 2483–93. https://doi.org/10.1083/jcb.108.6.2483.Full Text Link to Item
-
O’Keefe, E. J., H. P. Erickson, and V. Bennett. “Desmoplakin I and desmoplakin II. Purification and characterization.” J Biol Chem 264, no. 14 (May 15, 1989): 8310–18.Link to Item
-
Erickson, H. P. “Co-operativity in protein-protein association. The structure and stability of the actin filament.” J Mol Biol 206, no. 3 (April 5, 1989): 465–74. https://doi.org/10.1016/0022-2836(89)90494-4.Full Text Link to Item
-
Jones, A. M., and H. P. Erickson. “Domain structure of phytochrome from Avena sativa visualized by electron microscopy.” Photochem Photobiol 49, no. 4 (April 1989): 479–83. https://doi.org/10.1111/j.1751-1097.1989.tb09198.x.Full Text Link to Item
-
Kirshner, N., J. J. Corcoran, and H. P. Erickson. “Synthesis of alpha 2-macroglobulin by bovine adrenal cortical cell cultures.” Am J Physiol 256, no. 4 Pt 1 (April 1989): C779–85. https://doi.org/10.1152/ajpcell.1989.256.4.C779.Full Text Link to Item
-
O’Brien, E. T., and H. P. Erickson. “Assembly of pure tubulin in the absence of free GTP: effect of magnesium, glycerol, ATP, and the nonhydrolyzable GTP analogues.” Biochemistry 28, no. 3 (February 7, 1989): 1413–22. https://doi.org/10.1021/bi00429a070.Full Text Link to Item
-
Becker, J. W., H. P. Erickson, S. Hoffman, B. A. Cunningham, and G. M. Edelman. “Topology of cell adhesion molecules.” Proc Natl Acad Sci U S A 86, no. 3 (February 1989): 1088–92. https://doi.org/10.1073/pnas.86.3.1088.Full Text Link to Item
-
Anderson, K., F. A. Lai, Q. Y. Liu, E. Rousseau, H. P. Erickson, and G. Meissner. “Structural and functional characterization of the purified cardiac ryanodine receptor-Ca2+ release channel complex.” J Biol Chem 264, no. 2 (January 15, 1989): 1329–35.Link to Item
-
Carrell, N. A., H. P. Erickson, and J. McDonagh. “Electron microscopy and hydrodynamic properties of factor XIII subunits.” J Biol Chem 264, no. 1 (January 5, 1989): 551–56.Link to Item
-
Erickson, H. P., and M. A. Bourdon. “Tenascin: an extracellular matrix protein prominent in specialized embryonic tissues and tumors.” Annu Rev Cell Biol 5 (1989): 71–92. https://doi.org/10.1146/annurev.cb.05.110189.000443.Full Text Link to Item
-
Kirshner, N., J. J. Corcoran, and H. P. Erickson. “Synthesis of α2-macroglobulin by bovine adrenal cortical cell cultures.” American Journal of Physiology Cell Physiology 256, no. 4 (January 1, 1989).
-
Alliegro, M. C., C. A. Ettensohn, C. A. Burdsal, H. P. Erickson, and D. R. McClay. “Echinonectin: a new embryonic substrate adhesion protein.” J Cell Biol 107, no. 6 Pt 1 (December 1988): 2319–27. https://doi.org/10.1083/jcb.107.6.2319.Full Text Link to Item
-
Walker, R. A., E. T. O’Brien, N. K. Pryer, M. F. Soboeiro, W. A. Voter, H. P. Erickson, and E. D. Salmon. “Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies.” J Cell Biol 107, no. 4 (October 1988): 1437–48. https://doi.org/10.1083/jcb.107.4.1437.Full Text Link to Item
-
Mukherjee, S., H. Erickson, and D. Bastia. “Detection of DNA looping due to simultaneous interaction of a DNA-binding protein with two spatially separated binding sites on DNA.” Proc Natl Acad Sci U S A 85, no. 17 (September 1988): 6287–91. https://doi.org/10.1073/pnas.85.17.6287.Full Text Link to Item
-
Mukherjee, S., H. Erickson, and D. Bastia. “Enhancer-origin interaction in plasmid R6K involves a DNA loop mediated by initiator protein.” Cell 52, no. 3 (February 12, 1988): 375–83. https://doi.org/10.1016/s0092-8674(88)80030-8.Full Text Link to Item
-
Lai, F. A., H. P. Erickson, E. Rousseau, Q. Y. Liu, and G. Meissner. “Purification and reconstitution of the calcium release channel from skeletal muscle.” Nature 331, no. 6154 (January 28, 1988): 315–19. https://doi.org/10.1038/331315a0.Full Text Link to Item
-
Alliegro, M. C., C. A. Ettensohn, C. A. Burdsal, H. P. Erickson, and D. R. McClay. “Echinonectin: A new embryonic substrate adhesion protein.” Journal of Cell Biology 107, no. 6 I (January 1, 1988): 2319–27. https://doi.org/10.1083/jcb.107.6.2319.Full Text
-
Erickson, H. P., and V. A. Lightner. “Hexabrachion Protein (Tenascin, Cytotactin, Brachionectin) in Connective Tissues, Embryonic Brain, and Tumors.” Advances in Molecular and Cell Biology 2, no. C (January 1, 1988): 55–90. https://doi.org/10.1016/S1569-2558(08)60430-0.Full Text
-
Erickson, H. P., and H. C. Taylor. “Hexabrachion proteins in embryonic chicken tissues and human tumors.” J Cell Biol 105, no. 3 (September 1987): 1387–94. https://doi.org/10.1083/jcb.105.3.1387.Full Text Link to Item
-
O’Brien, E. T., W. A. Voter, and H. P. Erickson. “GTP hydrolysis during microtubule assembly.” Biochemistry 26, no. 13 (June 30, 1987): 4148–56. https://doi.org/10.1021/bi00387a061.Full Text Link to Item
-
Lai, F. A., H. Erickson, B. A. Block, and G. Meissner. “Evidence for a junctional feet-ryanodine receptor complex from sarcoplasmic reticulum.” Biochem Biophys Res Commun 143, no. 2 (March 13, 1987): 704–9. https://doi.org/10.1016/0006-291x(87)91411-2.Full Text Link to Item
-
Voter, W. A., C. Lucaveche, A. E. Blaurock, and H. P. Erickson. “Lateral packing of protofibrils in fibrin fibers and fibrinogen polymers.” Biopolymers 25, no. 12 (December 1986): 2359–73. https://doi.org/10.1002/bip.360251213.Full Text Link to Item
-
Voter, W. A., C. Lucaveche, and H. P. Erickson. “Concentration of protein in fibrin fibers and fibrinogen polymers determined by refractive index matching.” Biopolymers 25, no. 12 (December 1986): 2375–84. https://doi.org/10.1002/bip.360251214.Full Text Link to Item
-
Fretto, L. J., W. E. Fowler, D. R. McCaslin, H. P. Erickson, and P. A. McKee. “Substructure of human von Willebrand factor. Proteolysis by V8 and characterization of two functional domains.” J Biol Chem 261, no. 33 (November 25, 1986): 15679–89.Link to Item
-
Erickson, H. P. “Nucleosome structure.” Science 233, no. 4771 (September 26, 1986): 1429–31. https://doi.org/10.1126/science.3749888.Full Text Link to Item
-
Erickson, H. P., and W. A. Voter. “Nucleation of microtubule assembly. Experimental kinetics, computer fitting of models, and observations on tubulin rings.” Ann N Y Acad Sci 466 (1986): 552–65. https://doi.org/10.1111/j.1749-6632.1986.tb38432.x.Full Text Link to Item
-
Fowler, W. E., L. J. Fretto, K. K. Hamilton, H. P. Erickson, and P. A. McKee. “Substructure of human von Willebrand factor.” J Clin Invest 76, no. 4 (October 1985): 1491–1500. https://doi.org/10.1172/JCI112129.Full Text Link to Item
-
Milam, L. M., and H. P. Erickson. “A structural comparison of tryptic fragments of three types of intermediate filaments.” J Ultrastruct Res 90, no. 3 (March 1985): 251–60. https://doi.org/10.1016/s0022-5320(85)80003-4.Full Text Link to Item
-
Carrell, N. A., L. A. Fitzgerald, B. Steiner, H. P. Erickson, and D. R. Phillips. “Structure of human platelet membrane glycoproteins IIb and IIIa as determined by electron microscopy.” J Biol Chem 260, no. 3 (February 10, 1985): 1743–49.Link to Item
-
Milam, L., and H. P. Erickson. “Structural characteristics of the desmin protofilament.” J Ultrastruct Res 89, no. 2 (November 1984): 179–86. https://doi.org/10.1016/s0022-5320(84)80013-1.Full Text Link to Item
-
Erickson, H. P., and J. L. Inglesias. “A six-armed oligomer isolated from cell surface fibronectin preparations.” Nature 311, no. 5983 (September 20, 1984): 267–69. https://doi.org/10.1038/311267a0.Full Text Link to Item
-
Voter, W. A., and H. P. Erickson. “The kinetics of microtubule assembly. Evidence for a two-stage nucleation mechanism.” J Biol Chem 259, no. 16 (August 25, 1984): 10430–38.Link to Item
-
Erickson, H. P., and N. A. Carrell. “Fibronectin in extended and compact conformations. Electron microscopy and sedimentation analysis.” J Biol Chem 258, no. 23 (December 10, 1983): 14539–44.Link to Item
-
Erickson, H. P., and W. E. Fowler. “Electron microscopy of fibrinogen, its plasmic fragments and small polymers.” Ann N Y Acad Sci 408 (June 27, 1983): 146–63. https://doi.org/10.1111/j.1749-6632.1983.tb23242.x.Full Text Link to Item
-
Brown, H. R., and H. P. Erickson. “Assembly of proteolytically cleaved tubulin.” Arch Biochem Biophys 220, no. 1 (January 1983): 46–51. https://doi.org/10.1016/0003-9861(83)90385-5.Full Text Link to Item
-
Ohmori, K., L. J. Fretto, R. L. Harrison, M. E. P. Switzer, H. P. Erickson, and P. A. McKee. “Electron microscopy of human factor VIII/von willebrand glycoprotein: Effect of reducing reagents on structure and function.” Journal of Cell Biology 95, no. 2 (November 1, 1982): 632–40. https://doi.org/10.1083/jcb.95.2.632.Full Text
-
Ohmori, K., L. J. Fretto, R. L. Harrison, M. E. Switzer, H. P. Erickson, and P. A. McKee. “Electron microscopy of human factor VIII/Von Willebrand glycoprotein: effect of reducing reagents on structure and function.” J Cell Biol 95, no. 2 Pt 1 (November 1982): 632–40. https://doi.org/10.1083/jcb.95.2.632.Full Text Link to Item
-
Milam, L., and H. P. Erickson. “Visualization of a 21-nm axial periodicity in shadowed keratin filaments and neurofilaments.” J Cell Biol 94, no. 3 (September 1982): 592–96. https://doi.org/10.1083/jcb.94.3.592.Full Text Link to Item
-
Voter, W. A., and H. P. Erickson. “Electron microscopy of MAP 2 (microtubule-associated protein 2).” J Ultrastruct Res 80, no. 3 (September 1982): 374–82. https://doi.org/10.1016/s0022-5320(82)80051-8.Full Text Link to Item
-
Erickson, H. P., N. Carrell, and J. McDonagh. “Fibronectin molecule visualized in electron microscopy: a long, thin, flexible strand.” J Cell Biol 91, no. 3 Pt 1 (December 1981): 673–78. https://doi.org/10.1083/jcb.91.3.673.Full Text Link to Item
-
Hesterberg, L. K., J. C. Lee, and H. P. Erickson. “Structural properties of an active form of rabbit muscle phosphofructokinase.” J Biol Chem 256, no. 18 (September 25, 1981): 9724–30.Link to Item
-
Fowler, W. E., R. R. Hantgan, J. Hermans, and H. P. Erickson. “Structure of the fibrin protofibril.” Proc Natl Acad Sci U S A 78, no. 8 (August 1981): 4872–76. https://doi.org/10.1073/pnas.78.8.4872.Full Text Link to Item
-
Erickson, H. P., and D. Pantaloni. “The role of subunit entropy in cooperative assembly. Nucleation of microtubules and other two-dimensional polymers.” Biophys J 34, no. 2 (May 1981): 293–309. https://doi.org/10.1016/S0006-3495(81)84850-3.Full Text Link to Item
-
Fowler, W. E., H. P. Erickson, R. R. Hantgan, J. McDonagh, and J. Hermans. “Cross-linked fibrinogen dimers demonstrate a feature of the molecular packing in fibrin fibers.” Science 211, no. 4479 (January 16, 1981): 287–89. https://doi.org/10.1126/science.6108612.Full Text Link to Item
-
Hantgan, R., W. Fowler, H. Erickson, and J. Hermans. “Fibrin assembly: a comparison of electron microscopic and light scattering results.” Thromb Haemost 44, no. 3 (December 19, 1980): 119–24.Link to Item
-
Fowler, W. E., L. J. Fretto, H. P. Erickson, and P. A. McKee. “Electron microsocpy of plasmic fragments of human fibrinogen as related to trinodular structure of the intact molecule.” J Clin Invest 66, no. 1 (July 1980): 50–56. https://doi.org/10.1172/JCI109834.Full Text Link to Item
-
Erickson, H. P. “Thermodynamic and kinetic aspects of assembly.” Prog Clin Biol Res 40 (1980): 327–30.Link to Item
-
Hantgan, R., J. Hermans, W. Fowler, and H. Erickson. “Fibrin formation as a biological assembly process.” Biophysical Journal 32, no. 1 (January 1, 1980): 438–40. https://doi.org/10.1016/S0006-3495(80)84973-3.Full Text
-
Fowler, W. E., and H. P. Erickson. “Trinodular structure of fibrinogen. Confirmation by both shadowing and negative stain electron microscopy.” J Mol Biol 134, no. 2 (October 25, 1979): 241–49. https://doi.org/10.1016/0022-2836(79)90034-2.Full Text Link to Item
-
Voter, W. A., and H. P. Erickson. “Tubulin rings: curved filaments with limited flexibility and two modes of association.” J Supramol Struct 10, no. 4 (1979): 419–31. https://doi.org/10.1002/jss.400100405.Full Text Link to Item
-
Erickson, H. P., W. A. Voter, and K. Leonard. “Image reconstruction in electron microscopy: enhancement of periodic structure by optical filtering.” Methods Enzymol 49 (1978): 39–63. https://doi.org/10.1016/s0076-6879(78)49006-8.Full Text Link to Item
-
David-Pfeuty, T., H. P. Erickson, and D. Pantaloni. “Guanosinetriphosphatase activity of tubulin associated with microtubule assembly.” Proc Natl Acad Sci U S A 74, no. 12 (December 1977): 5372–76. https://doi.org/10.1073/pnas.74.12.5372.Full Text Link to Item
-
Erickson, H. P., and W. A. Voter. “Polycation-induced assembly of purified tubulin.” Proc Natl Acad Sci U S A 73, no. 8 (August 1976): 2813–17. https://doi.org/10.1073/pnas.73.8.2813.Full Text Link to Item
-
Erickson, H. P. “The structure and assembly of microtubules.” Ann N Y Acad Sci 253 (June 30, 1975): 60–77. https://doi.org/10.1111/j.1749-6632.1975.tb19193.x.Full Text Link to Item
-
Erickson, H. P. “Negatively stained vinblastine aggregates.” Ann N Y Acad Sci 253 (June 30, 1975): 51–52. https://doi.org/10.1111/j.1749-6632.1975.tb19191.x.Full Text Link to Item
-
Erickson, H. P. “Microtubule surface lattice and subunit structure and observations on reassembly.” J Cell Biol 60, no. 1 (January 1974): 153–67. https://doi.org/10.1083/jcb.60.1.153.Full Text Link to Item
-
Erickson, H. P. “Assembly of microtubules from preformed, ring-shaped protofilaments and 6-S tubulin.” J Supramol Struct 2, no. 2–4 (1974): 393–411. https://doi.org/10.1002/jss.400020228.Full Text Link to Item
-
Bartl, P., H. Erickson, and M. Beer. “Electron microscopic study of base sequence in nucleic acids VI. Guanine sites in yeast alanine transfer RNA.” Micron (1969) 1, no. 4 (January 1, 1970): 374–92. https://doi.org/10.1016/0047-7206(70)90053-1.Full Text
-
Erickson, H., and M. Beer. “Electron microscopic study of the base sequence in nucleic acids. VI. Preparation of ribonucleic acid with marked gauanosine monophosphate nucleotides.” Biochemistry 6, no. 9 (September 1967): 2694–2701. https://doi.org/10.1021/bi00861a008.Full Text Link to Item
-
Blattner, F. R., and H. P. Erickson. “Rapid nucleotide separation by chromatography on cation-exchange columns.” Analytical Biochemistry 18, no. 2 (January 1, 1967): 220–27. https://doi.org/10.1016/0003-2697(67)90004-8.Full Text
-
-
Book Sections
-
Erickson, Harold P. “Fibronectin, the FNIII domain, and artificial antibodies.” In Principles of Protein–Protein Association. IOP Publishing, 2019. https://doi.org/10.1088/2053-2563/ab19bach10.Full Text
-
Erickson, Harold P. “Cooperativity in protein–protein association and efficiency of bonds.” In Principles of Protein–Protein Association. IOP Publishing, 2019. https://doi.org/10.1088/2053-2563/ab19bach7.Full Text
-
Erickson, Harold P. “The nature of the protein–protein bond, à la Chothia and Janin.” In Principles of Protein–Protein Association. IOP Publishing, 2019. https://doi.org/10.1088/2053-2563/ab19bach3.Full Text
-
Erickson, Harold P. “Basic thermodynamics of reversible association.” In Principles of Protein–Protein Association. IOP Publishing, 2019. https://doi.org/10.1088/2053-2563/ab19bach2.Full Text
-
Erickson, Harold P. “Kinetics of protein–protein association and dissociation.” In Principles of Protein–Protein Association. IOP Publishing, 2019. https://doi.org/10.1088/2053-2563/ab19bach8.Full Text
-
Erickson, Harold P. “Size and shape of protein molecules at the nm level determined by sedimentation, gel filtration and electron microscopy.” In Principles of Protein–Protein Association. IOP Publishing, 2019. https://doi.org/10.1088/2053-2563/ab19bach1.Full Text
-
Erickson, Harold P. “Techniques for measuring protein–protein association—use and misuse of ELISA.” In Principles of Protein–Protein Association. IOP Publishing, 2019. https://doi.org/10.1088/2053-2563/ab19bach9.Full Text
-
Erickson, Harold P. “Association of intrinsically disordered proteins—flexible binding partners.” In Principles of Protein–Protein Association. IOP Publishing, 2019. https://doi.org/10.1088/2053-2563/ab19bach11.Full Text
-
Erickson, Harold P. “The structure of an antibody bound to its protein ligand—lock and key versus induced fit and conformational selection.” In Principles of Protein–Protein Association. IOP Publishing, 2019. https://doi.org/10.1088/2053-2563/ab19bach4.Full Text Open Access Copy
-
Erickson, Harold P. “The complex of growth hormone with its receptor—one protein interface binds two partners.” In Principles of Protein–Protein Association. IOP Publishing, 2019. https://doi.org/10.1088/2053-2563/ab19bach5.Full Text
-
Erickson, Harold P. “Principles of Protein-Protein Association Preface.” In PRINCIPLES OF PROTEIN-PROTEIN ASSOCIATION, VIII–VIII, 2019.Link to Item
-
Erickson, Harold P. “The hot spot in protein–protein interfaces.” In Principles of Protein–Protein Association. IOP Publishing, 2019. https://doi.org/10.1088/2053-2563/ab19bach6.Full Text
-
-
Conference Papers
-
Anderson, David E., and Harold P. Erickson. “Improved Specimen Preparations for Electron Microscopy of FtsZ Protofilaments.” In Biophysical Journal, 96:519a-519a. Elsevier BV, 2009. https://doi.org/10.1016/j.bpj.2008.12.2675.Full Text
-
-
Datasets
-
Erickson, Harold. “Faculty Opinions recommendation of Impact of reconstituted cytosol on protein stability.,” January 16, 2014. https://doi.org/10.3410/f.718173174.793489436.Data Access
-
-
Preprints
-
Goodman, Lauren Corbin, and Harold Erickson. “FtsZ is essential until the late stage of constriction.” BioRxiv, 2022. https://doi.org/10.1101/2022.03.01.482533.Full Text Open Access Copy
-
Corbin, L., and H. P. Erickson. “Modelling FtsZ nucleation, hydrolysis and treadmilling activity with Monte Carlo methods.” BioRxiv, 2020. https://doi.org/10.1101/2020.02.25.965095.Full Text
-
-
- Teaching & Mentoring
-
Recent Courses
Some information on this profile has been compiled automatically from Duke databases and external sources. (Our About page explains how this works.) If you see a problem with the information, please write to Scholars@Duke and let us know. We will reply promptly.