| Campbell, Sharon | University of North Carolina | Editorial Board Member |
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Name:
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Campbell, Sharon
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Role:
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Editorial Board Member
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Email:
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campbesl@med.unc.edu
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Institution:
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University of North Carolina
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Department:
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Biochemistry and Biophysics
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Subject Categories:
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Expertise Terms:
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Biophysics, cell adhesion, cell adhesion proteins, cell signaling, cysteine oxidation, enzyme purification, enzyme structure, Escherichia coli (E. coli), fluorescence, focal adhesions, G protein, G-actin, GTPase, GTPase activating protein (GAP), GTPase Kras (KRAS), guanine nucleotide exchange factor (GEF), inositol phospholipid, NMR spectroscopy, nuclear magnetic resonance (NMR), nucleoside/nucleotide analogue, paxillin, phosphatidylinositide 3-kinase (PI 3-kinase), post translational modification, post-translational modification (PTM), protein chemical modification, protein purification, Rac (Rac GTPase), Raf kinase, Ras and Ras related GTPases, Ras protein, Ras-related protein 1 (Rap1), Signal Transduction, structural biology, tertiary structure, vinculin
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| Frueh, Dominique | Johns Hopkins University School of Medicine | Editorial Board Member |
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Name:
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Frueh, Dominique
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Role:
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Editorial Board Member
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Email:
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dfrueh1@jhmi.edu
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Institution:
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Johns Hopkins University School of Medicine
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Department:
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Subject Categories:
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Protein Structure and Folding
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Expertise Terms:
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acyl carrier protein (ACP), adenylation domain, Biophysics, condensation domain, conformational change, cyclization domain, enzyme, enzyme catalysis, enzyme mechanism, enzyme structure, fluorescence anisotropy, kinetics, Michaelis-Menten, natural product biosynthesis, NMR methods, non-ribosomal peptide synthestases, nonribosomal peptide synthestases, nuclear magnetic resonance (NMR), peptide biosynthesis, peptide conformation, protein chemical modification, protein conformation, protein domain, protein dynamic, protein structure, structural biology, structure-function, tertiary structure, thioesterase
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| Orlova, Elena | Birkbeck College, London | Editorial Board Member |
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Name:
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Orlova, Elena
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Role:
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Editorial Board Member
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Email:
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e.orlova@mail.cryst.bbk.ac.uk
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Institution:
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Birkbeck College, London
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Department:
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Biological Sciences
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Subject Categories:
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Computational Biology, Molecular Biophysics, Protein Structure and Folding
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Expertise Terms:
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bacteriophage, Cryo elecron microscopy, E1 helicase, electron microscopy (EM), electron tomography, herpesvirus, Image processing, Molecular Biology, p53, protein conformation, protein structure, ribosome function, ribosome structure, single particle analysis, structural biology, Structure of bacteriopahges, Structure of calcium or potassium channels, Structure of ribosomes, tertiary structure, type III secretion system (T3SS), type IV pili, virus assembly, virus structure
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| Otzen, Daniel | Aarhus University | Editorial Board Member |
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Name:
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Otzen, Daniel
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Role:
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Editorial Board Member
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Email:
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dao@inano.au.dk
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Institution:
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Aarhus University
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Department:
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Subject Categories:
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Molecular Biophysics
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Expertise Terms:
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amyloid, membrane protein, micelle, neurodegenerative disease, Parkinson disease, phospholipid vesicle, pre-steady-state kinetics, protein aggregation, protein conformation, protein denaturation, protein engineering, protein folding, protein misfolding, protein self-assembly, protein stability, protein-lipid interaction, tertiary structure, transmembrane domain
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| Pearce, F. Grant | University of Canterbury | Editorial Board Member |
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Name:
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Pearce, F. Grant
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Role:
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Editorial Board Member
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Email:
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grant.pearce@canterbury.ac.nz
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Institution:
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University of Canterbury
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Department:
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Subject Categories:
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Enzymology, Molecular Biophysics, Plant Biology
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Expertise Terms:
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Biophysics, enzyme, enzyme inhibitor, enzyme kinetics, enzyme structure, oligomerization, photosynthesis, plant biochemistry, protein purification, protein stability, protein structure, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), small-angle X-ray scattering (SAXS), tertiary structure, ultracentrifugation
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| Williams, R. | National Institutes of Health, National Institute of Environmental Health Sciences | Editorial Board Member |
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Name:
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Williams, R.
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Role:
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Editorial Board Member
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Email:
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williamsrs@niehs.nih.gov
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Institution:
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National Institutes of Health, National Institute of Environmental Health Sciences
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Department:
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Genome integrity and Structural Cell Biology Laboratory
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Subject Categories:
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DNA and Chromosomes, Molecular Bases of Disease, Protein Structure and Folding
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Expertise Terms:
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ADP-ribosylation, Aprataxin, BRCA1, BRCT, cancer biology, cancer therapy, chromatin, chromatin modification, chromatin structure, chromosomes, crystal structure, crystallography, DNA, DNA binding protein, DNA damage, DNA damage response, DNA endonuclease, DNA enzyme, DNA repair, DNA topoisomerase, DNA-protein interaction, enzyme catalysis, enzyme mechanism, enzyme structure, genomic instability, Mre11, Nbs1, nucleic acid enzymology, nucleic acid structure, oncogene, polyubiquitin chain, proliferating cell nuclear antigen (PCNA), protein chemistry, protein crystallization, protein domain, protein engineering, protein phosphorylation, protein processing, protein structure, protein-DNA interaction, protein-nucleic acid interaction, protein-protein interaction, Rad50, radiation biology, recombination, small ubiquitin-like modifier (SUMO), small-angle X-ray scattering (SAXS), SUMO-interacting motif (SIM), sumoylation, tertiary structure, Tyrosyl DNA phosphodiesterase, ubiquitin ligase, ubiquitin-conjugating enzyme (E2 enzyme), X-ray crystallography, zinc finger
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