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Ronald Venters

Ronald Venters

Adjunct Assistant Professor in the Department of Radiology
Radiology
venters@duke.edu
Box 3711 Med Ctr, Room B127 Levine Science Research Center, Durham, NC 27710
B127 Lev Sci Res Ctr, #08 Research Drive, Durham, NC 27708

Selected Publications

Structure-guided design and synthesis of C22- and C32-modified FK520 analogs with enhanced activity against human pathogenic fungi.

Journal Article Proc Natl Acad Sci U S A · January 7, 2025 Invasive fungal infections are a leading cause of death worldwide. Translating molecular insights into clinical benefits is challenging because fungal pathogens and their hosts share similar eukaryotic physiology. Consequently, current antifungal treatment ... Full text Link to item Cite

Backbone and sidechain 1H, 15N and 13C resonance assignments of the free and RNA-bound tandem zinc finger domain of the tristetraprolin family member from Selaginella moellendorffii.

Journal Article Biomol NMR Assign · April 2022 Members of the tristetraprolin (TTP) family of RNA binding proteins (RBPs) regulate the metabolism of a variety of mRNA targets. In mammals, these proteins modulate many physiological processes, including immune cell activation, hematopoiesis, and embryoni ... Full text Link to item Cite

Leveraging Fungal and Human Calcineurin-Inhibitor Structures, Biophysical Data, and Dynamics To Design Selective and Nonimmunosuppressive FK506 Analogs.

Journal Article mBio · December 21, 2021 Calcineurin is a critical enzyme in fungal pathogenesis and antifungal drug tolerance and, therefore, an attractive antifungal target. Current clinically accessible calcineurin inhibitors, such as FK506, are immunosuppressive to humans, so exploiting calci ... Full text Open Access Link to item Cite

FKBP12 dimerization mutations effect FK506 binding and differentially alter calcineurin inhibition in the human pathogen Aspergillus fumigatus.

Journal Article Biochem Biophys Res Commun · May 21, 2020 The 12-kDa FK506-binding protein (FKBP12) is the target of the commonly used immunosuppressive drug FK506. The FKBP12-FK506 complex binds to calcineurin and inhibits its activity, leading to immunosuppression and preventing organ transplant rejection. Our ... Full text Open Access Link to item Cite

Leveraging Fungal Calcineurin-Inhibitor Structures, Biophysics and Dynamics to Design Selective and Non-Immunosuppressive FK506 Analogs

Journal Article · 2020 Calcineurin is a critical enzyme in fungal pathogenesis and antifungal drug tolerance and, therefore, an attractive antifungal target. Current clinically-accessible calcineurin inhibitors, such as FK506, are immunosuppressive to humans, so exploiting calci ... Full text Open Access Cite

Harnessing calcineurin-FK506-FKBP12 crystal structures from invasive fungal pathogens to develop antifungal agents.

Journal Article Nat Commun · September 19, 2019 Calcineurin is important for fungal virulence and a potential antifungal target, but compounds targeting calcineurin, such as FK506, are immunosuppressive. Here we report the crystal structures of calcineurin catalytic (CnA) and regulatory (CnB) subunits c ... Full text Open Access Link to item Cite

15N, 13C and 1H resonance assignments of FKBP12 proteins from the pathogenic fungi Mucor circinelloides and Aspergillus fumigatus.

Journal Article Biomol NMR Assign · April 2019 Invasive fungal infections are a leading cause of death in immunocompromised patients and remain difficult to treat since fungal pathogens, like mammals, are eukaryotes and share many orthologous proteins. As a result, current antifungal drugs have limited ... Full text Open Access Link to item Cite

Structures of Pathogenic Fungal FKBP12s Reveal Possible Self-Catalysis Function.

Journal Article mBio · April 26, 2016 UNLABELLED: Invasive fungal infections remain difficult to treat and require novel targeting strategies. The 12-kDa FK506-binding protein (FKBP12) is a ubiquitously expressed peptidyl-prolyl isomerase with considerable homology between fungal pathogens and ... Full text Link to item Cite

Radial sampling for fast NMR: Concepts and practices over three decades.

Journal Article Prog Nucl Magn Reson Spectrosc · November 2010 Full text Link to item Cite

NMR assignment of the N-terminal repeat domain of Bacillus subtilis ClpC.

Journal Article Biomol NMR Assign · December 2007 The HSP100/AAA+ superfamily protein ClpC is a key regulator of cell development in Bacillus subtilis. We present here the backbone and side-chain assignments of the N-terminal repeat domain (residues 1-145) of ClpC from Bacillus subtilis. ... Full text Link to item Cite

Peptide binding proclivities of calcium loaded calbindin-D28k.

Journal Article FEBS Lett · October 2, 2007 Calbindin-D28k is known to function as a calcium-buffering protein in the cell. Moreover, recent evidence shows that it also plays a role as a sensor. Using circular dichroism and NMR, we show that calbindin-D28k undergoes significant conformational change ... Full text Link to item Cite

Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage.

Journal Article RNA · April 2007 Bacterial ribonuclease P (RNase P) is a ribonucleoprotein complex composed of one catalytic RNA (PRNA) and one protein subunit (P protein) that together catalyze the 5' maturation of precursor tRNA. High-resolution X-ray crystal structures of the individua ... Full text Link to item Cite

NMR structure of AbhN and comparison with AbrBN: FIRST insights into the DNA binding promiscuity and specificity of AbrB-like transition state regulator proteins.

Journal Article J Biol Chem · July 28, 2006 Understanding the molecular mechanisms of transition state regulator proteins is critical, since they play a pivotal role in the ability of bacteria to cope with changing environments. Although much effort has focused on their genetic characterization, lit ... Full text Link to item Cite

Structure, binding interface and hydrophobic transitions of Ca2+-loaded calbindin-D(28K).

Journal Article Nat Struct Mol Biol · July 2006 Calbindin-D(28K) is a Ca2+-binding protein, performing roles as both a calcium buffer and calcium sensor. The NMR solution structure of Ca2+-loaded calbindin-D(28K) reveals a single, globular fold consisting of six distinct EF-hand subdomains, which coordi ... Full text Link to item Cite

Filtered backprojection for the reconstruction of a high-resolution (4,2)D CH3-NH NOESY spectrum on a 29 kDa protein.

Journal Article J Am Chem Soc · August 24, 2005 Projection-reconstruction (PR) NMR enables rapid collection of multidimensional NMR data. NOESY represents a particularly difficult challenge for currently existing reconstruction algorithms, as it requires the quantitative reconstruction of an unknown num ... Full text Link to item Cite

(4,2)D Projection--reconstruction experiments for protein backbone assignment: application to human carbonic anhydrase II and calbindin D(28K).

Journal Article J Am Chem Soc · June 22, 2005 Projection-reconstruction NMR experiments have been shown to significantly reduce the acquisition time required to obtain protein backbone assignment data. To date, this concept has only been applied to smaller (15)N/(13)C-labeled proteins. Here, we show t ... Full text Link to item Cite

Generalized reconstruction of n-D NMR spectra from multiple projections: application to the 5-D HACACONH spectrum of protein G B1 domain.

Journal Article J Am Chem Soc · February 4, 2004 Reconstructing multidimensional NMR spectra from 2-D projections significantly reduces the time needed for data collection over conventional methodology. Here, we provide a generalization of the projection-reconstruction process to spectra of arbitrary dim ... Full text Link to item Cite

The effects of Ca(2+) binding on the conformation of calbindin D(28K): a nuclear magnetic resonance and microelectrospray mass spectrometry study.

Journal Article Anal Biochem · June 1, 2003 Calbindin D(28K) is a six-EF-hand calcium-binding protein found in the brain, peripheral nervous system, kidney, and intestine. There is a paucity of information on the effects of calcium binding on calbindin D(28K) structure. To further examine the mechan ... Full text Link to item Cite

Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.

Journal Article Biochem Biophys Res Commun · April 18, 2003 Calbindin D(28K) is an EF-hand containing protein that plays a vital role in neurological function. We now show that calcium-loaded calbindin D(28K) interacts with Ran-binding protein M, a protein known to play a role in microtubule function. Using NMR met ... Full text Link to item Cite

Current approaches for the study of large proteins by NMR

Journal Article Journal of Molecular Structure · January 9, 2002 An overview of current methods employed for characterizing larger (>25 kDa) proteins by NMR is presented. These techniques include: the attenuation of T2 relaxation effects by offsetting dipole-dipole and chemical shift anisotropy relaxation mec ... Full text Cite

Protein dynamic studies move to a new time slot.

Journal Article Nat Struct Biol · November 2001 Full text Link to item Cite

Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein.

Journal Article J Mol Biol · June 30, 2000 The global fold of maltose-binding protein in complex with the substrate beta-cyclodextrin was determined by solution NMR methods. The two-domain protein is comprised of a single polypeptide chain of 370 residues, with a molecular mass of 42 kDa. Distance ... Full text Link to item Cite

TROSY-based HNCO pulse sequences for the measurement of (1)HN-(15)N, (15)N-(13)CO, (1)HN-(13)CO, (13)CO-(13)C(α) and (1)HN-(13)C(α) dipolar couplings in (15)N, (13)C, (2)H-labeled proteins

Journal Article Journal of Biomolecular NMR · January 1, 1999 HNCO-based 3D pulse schemes are presented for measuring 1HN-15N,15N-13CO, 1HN-13CO,13CO-13C(α) and 1HN-13C(α) dipolar couplings in 15N, ... Full text Cite

NMR methods for analysis of CRALBP retinoid binding

Journal Article Techniques in Protein Chemistry · December 1, 1997 Full text Cite

Nmr and mutational analysis of retinoid-binding in the cellular retinaldehyde-binding protein (cralbp)

Journal Article Investigative Ophthalmology and Visual Science · December 1, 1997 Purpose. To identify amino acid residues in CRALBP associated with the retinoid binding pocket. CRALBP may play a regulatory role in the visual cycle regeneration of 11-o/s-retinaldehyde (11-c/s-Ral). Methods. Recombinant human CRALBP was labeled with "C-m ... Cite

Strategies for NMR assignment and global fold determinations using perdeuterated proteins

Journal Article Techniques in Protein Chemistry · December 1, 1997 Full text Cite

Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.

Journal Article J Mol Biol · December 20, 1996 Perdeuteration of all non-exchangeable proton sites can significantly increase the size of proteins and protein complexes for which NMR resonance assignments and structural studies are possible. Backbone 1H, 15N, 13CO, 13C alpha and 13C beta chemical shift ... Full text Link to item Cite

Assignment of aliphatic side-chain 1HN/15N resonances in perdeuterated proteins.

Journal Article J Biomol NMR · January 1996 The perdeuteration of aliphatic sites in large proteins has been shown to greatly facilitate the process of sequential backbone and side-chain 13C assignments and has also been utilized in obtaining long-range NOE distance restraints for structure calculat ... Full text Link to item Cite

High-level 2H/13C/15N labeling of proteins for NMR studies.

Journal Article J Biomol NMR · June 1995 The protein human carbonic anhydrase II (HCA II) has been isotopically labeled with 2H, 13C and 15N for high-resolution NMR assignment studies and pulse sequence development. To increase the sensitivity of several key 1H/13C/15N triple-resonance correlatio ... Full text Link to item Cite

NMR-STUDIES OF H-2/C-13/N-15-LABELED HCA-II

Conference JOURNAL OF CELLULAR BIOCHEMISTRY · April 2, 1995 Link to item Cite

Assignment of Side-Chain 13C Resonances in Perdeuterated Proteins

Journal Article Journal of the American Chemical Society · January 1, 1995 Full text Cite

Heteronuclear gradient-enhanced NMR for the study of 20–30kDa proteins: Application to human carbonic anhydrase II

Journal Article Techniques in Protein Chemistry · January 1, 1995 Human carbonic anhydrase (HCA) is ubiquitous in living systems with seven different mammalian isozymes (CAI to CAVII), and HCAII is one of the largest monomeric proteins currently, being studied by NMR, making it a good system on which to demonstrate the a ... Full text Cite

Use of 1HN- 1HN NOEs to Determine Protein Global Folds in Perdeuterated Proteins

Journal Article Journal of the American Chemical Society · January 1, 1995 Full text Cite

HETERONUCLEAR EDITED STUDIES OF THE ESCHERICHIA-COLI METHIONINE REPRESSOR SYSTEM

Conference JOURNAL OF CELLULAR BIOCHEMISTRY · February 8, 1993 Link to item Cite

A refocused and optimized HNCA: increased sensitivity and resolution in large macromolecules.

Journal Article J Biomol NMR · March 1992 A 3D optimized, refocused HNCA experiment is described. It is demonstrated to yield a dramatic increase in sensitivity when applied to [13C, 15N]-labeled human carbonic anhydrase II, a 29-kDa protein. The reasons for the gain in sensitivity are discussed, ... Full text Link to item Cite

Uniform 13C isotope labeling of proteins with sodium acetate for NMR studies: application to human carbonic anhydrase II.

Journal Article Biochemistry · May 7, 1991 Uniform double labeling of proteins for NMR studies can be prohibitively expensive, even with an efficient expression and purification scheme, due largely to the high cost of [13C6, 99%]glucose. We demonstrate here that uniformly (greater than 95%) 13C and ... Full text Link to item Cite

Use of gel filtration in the preparation of biological fluids for magnetic resonance spectroscopy.

Journal Article Magn Reson Med · March 1990 Analysis of biological fluids by proton magnetic resonance spectroscopy is often complicated by dynamic range problems created from the large water resonance. Gel filtration chromatography is found to be a simple and nondestructive method for exchanging D2 ... Full text Link to item Cite

57Fe Hyperfine Coupling Tensors of the FeMo Cluster in Azotobacter vinelandii MoFe Protein: Determination by Polycrystalline ENDOR Spectroscopy

Journal Article Journal of the American Chemical Society · March 1, 1988 37Fe ENDOR spectra obtained from frozen-solution samples of Azotobacter vinelandii molybdenum—iron protein (Avl) have been interpreted through use of a method we have devised for analyzing and simulating the ENDOR spectra of a randomly oriented ... Full text Cite

ENDOR of the Resting State of Nitrogenase Molybdenum-Iron Proteins from Azotobacter vinelandii, Klebsiella pneumoniae, and Clostridium pasteurianum: 1H, 57Fe, 95Mo, and 33S Studies

Journal Article Journal of the American Chemical Society · January 1, 1986 Electron nuclear double resonance (ENDOR) studies of native and isotopically enriched MoFe proteins hold the promise of individually characterizing every atom of the catalytically active FeMo-co cluster of the nitrogenase MoFe protein. This report presents ... Full text Cite

ESR and ENDOR applications of loop-gap resonators with distributed circuit coupling

Journal Article Journal of Magnetic Resonance 1969 · October 15, 1985 Full text Cite

ENDOR with a loop-gap resonator

Journal Article Journal of Magnetic Resonance 1969 · January 1, 1984 Full text Cite

General theory of polycrystalline ENDOR patterns. g and hyperfine tensors of arbitrary symmetry and relative orientation

Journal Article Journal of Magnetic Resonance 1969 · January 1, 1984 A general formulation is presented for the ENDOR spectra of a randomly oriented, polycrystalline (powder) S = 1 2 paramagnet, assuming slow cross-relaxation, g anisotropy domination of the EPR spectrum, arbitrary symmetries and relative orientations of g a ... Full text Cite

Coordination environment for the type 3 copper center of tree laccase and CuB of cytochrome c oxidase as determined by electron nuclear double resonance.

Journal Article J Biol Chem · April 25, 1983 A new rhombic EPR signal was recently discovered in the partially reduced type 2 copper-depleted Rhus vernicifera laccase (Reinhammar, B. (1983) J. Inorg. Biochem., in press). The signal originates from one of the type 3 Cu(II) ions that becomes EPR-detect ... Link to item Cite

57Fe ENDOR of the Nitrogenase MoFe Protein

Journal Article Journal of the American Chemical Society · January 1, 1982 Full text Cite