ArticleInternational reviews in physical chemistry2013
Partial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.
Article in International reviews in physical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 41 citations in OpenAlex.
- Structure of the DDB1-AMBRA1 E3 ligase receptor complex linked to cell cycle regulation.Nature communications · 2023Article
- Structure of a GRK5-Calmodulin Complex Reveals Molecular Mechanism of GRK Activation and Substrate Targeting.Molecular cell · 2021Article
- MS-Based Approaches Enable the Structural Characterization of Transcription Factor/DNA Response Element Complex.Biomolecules · 2019Article
- A temperature-dependent conformational shift in p38α MAPK substrate-binding region associated with changes in substrate phosphorylation profile.The Journal of biological chemistry · 2019Article
- Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab Fragment of NISTmAb.Analytical chemistry · 2019Article
- The Role of Mass Spectrometry in Structural Studies of Flavin-Based Electron Bifurcating Enzymes.Frontiers in microbiology · 2018Review
- Conformational dynamics of 1-deoxy-d-xylulose 5-phosphate synthase on ligand binding revealed by H/D exchange MS.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Conformational dynamics of a neurotransmitter:sodium symporter in a lipid bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Hydrogen Exchange Mass Spectrometry of Related Proteins with Divergent Sequences: A Comparative Study of HIV-1 Nef Allelic Variants.Journal of the American Society for Mass Spectrometry · 2016Article
- Dynamics of the Tec-family tyrosine kinase SH3 domains.Protein science : a publication of the Protein Society · 2016Article
- Subtle Dynamic Changes Accompany Hck Activation by HIV-1 Nef and are Reversed by an Antiretroviral Kinase Inhibitor.Biochemistry · 2015Article
- Hydrogen/deuterium exchange mass spectrometry applied to IL-23 interaction characteristics: potential impact for therapeutics.Expert review of proteomics · 2015Review
- Fluorescence Polarization Screening Assays for Small Molecule Allosteric Modulators of ABL Kinase Function.PloS one · 2015Article
- Analytical Aspects of Hydrogen Exchange Mass Spectrometry.Annual review of analytical chemistry (Palo Alto, Calif.) · 2015Review
- QUDeX-MS: hydrogen/deuterium exchange calculation for mass spectra with resolved isotopic fine structure.BMC bioinformatics · 2014Article
- The influence of adnectin binding on the extracellular domain of epidermal growth factor receptor.Journal of the American Society for Mass Spectrometry · 2014Article
- Conformational States of macromolecular assemblies explored by integrative structure calculation.Structure (London, England : 1993) · 2013Article
- Structure and dynamic regulation of Abl kinases.The Journal of biological chemistry · 2013Review
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Many proteins do not exist in a single rigid conformation. Protein motions, or dynamics, exist and in many cases are important for protein function. The analysis of protein dynamics relies on biophysical techniques that can distinguish simultaneously existing populations of molecules and their rates of interconversion. Hydrogen exchange (HX) detected by mass spectrometry (MS) is contributing to our understanding of protein motions by revealing unfolding and dynamics on a wide timescale, ranging from seconds to hours to days. In this review we discuss HX MS-based analyses of protein dynamics, using our studies of multi-domain kinases as examples. Using HX MS, we have successfully probed protein dynamics and unfolding in the isolated SH3, SH2 and kinase domains of the c-Src and Abl kinase families, as well as the role of inter- and intra-molecular interactions in the global control of kinase function. Coupled with high-resolution structural information, HX MS has proved to be a powerful and versatile tool for the analysis of the conformational dynamics in these kinase systems, and has provided fresh insight regarding the regulatory control of these important signaling proteins. HX MS studies of dynamics are applicable not only to the proteins we illustrate here, but to a very wide range of proteins and protein systems, and should play a role in both classification of and greater understanding of the prevalence of protein motion.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.