ReviewTopics in current chemistry2012
NMR as a unique tool in assessment and complex determination of weak protein-protein interactions.
Review in Topics in current chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed.
- Targeting protein protein interactions and their modulators to enable new therapeutic strategies for human diseases.NPJ systems biology and applications · 2026Review
- Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.Current research in structural biology · 2024Review
- A Novel Interaction Between RAD23A/B and Y-family DNA Polymerases.Journal of molecular biology · 2023Article
- Mutations to the BTN2A1 Linker Region Impact Its Homodimerization and Its Cytoplasmic Interaction with Phospho-Antigen-Bound BTN3A1.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- PP2A is activated by cytochromeComputational and structural biotechnology journal · 2022Article
- Assessing Protein Interactions for Clustering of Mitochondrial Urea Cycle Enzymes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Fragment-Based Drug Discovery by NMR. Where Are the Successes and Where can It Be Improved?Frontiers in molecular biosciences · 2022Article
- Beyond history and "on a roll": The list of the most well-studied human protein structures and overall trends in the protein data bank.Protein science : a publication of the Protein Society · 2021Review
- Protein LY6E as a candidate for mediating transport of adeno-associated virus across the human blood-brain barrier.Journal of neurovirology · 2020Article
- Understanding the Impacts of Conformational Dynamics on the Regulation of Protein-Protein Association by a Multiscale Simulation Method.Journal of chemical theory and computation · 2020Article
- Rapid Quantification of Protein-Ligand Binding viaBiophysical journal · 2020Article
- Collagen I Weakly Interacts with the β-Sheets of βJournal of the American Chemical Society · 2020Article
- Current Methods for Detecting Cell Membrane Transient Interactions.Frontiers in chemistry · 2020Review
- K-Ras G-domain binding with signaling lipid phosphatidylinositol (4,5)-phosphate (PIP2): membrane association, protein orientation, and function.The Journal of biological chemistry · 2019Article
- Building Bridges Between Structural and Network-Based Systems Biology.Molecular biotechnology · 2019Review
- The butyrophilin 3A1 intracellular domain undergoes a conformational change involving the juxtamembrane region.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017Article
- Entire-Dataset Analysis of NMR Fast-Exchange Titration Spectra: A MgThe journal of physical chemistry. B · 2016Article
- Protein Neighbors and Proximity Proteomics.Molecular & cellular proteomics : MCP · 2015Review
- Electron-capture dissociation and ion mobility mass spectrometry for characterization of the hemoglobin protein assembly.Protein science : a publication of the Protein Society · 2015Article
- The low-affinity complex of cytochrome c and its peroxidase.Nature communications · 2015Article
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Abstract
Protein-protein interactions are crucial for a wide variety of biological processes. These interactions range from high affinity (K (d)<nM) to very low affinity (K (d)>mM). While much is known about the nature of high affinity protein complexes, our knowledge about structural characteristics of weak protein-protein interactions (wPPIs) remains limited: in addition to the technical difficulties associated with their investigation, historically wPPIs used to be considered physiologically irrelevant. However, emerging evidence suggests that wPPIs, either in the form of intact protein complexes or as part of large molecular machineries, are fundamentally important for promoting rapid on/off switches of signal transduction, reversible cell-cell contacts, transient assembly/disassembly of signaling complexes, and enzyme-substrate recognition. Therefore an atomic-level elucidation of wPPIs is vital to understanding a cornucopia of diverse cellular events. Nuclear magnetic resonance (NMR) is famous for its unique abilities to study wPPIs and, by utilization of the new technical developments combined with sparse data based computational analysis, it now allows rapid identification and structural characterization of wPPIs. Here we present our perspective on the NMR methods employed.
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