P
Peter Csermely
Researcher at Semmelweis University
Publications - 273
Citations - 17895
Peter Csermely is an academic researcher from Semmelweis University. The author has contributed to research in topics: Heat shock protein & Chaperone (protein). The author has an hindex of 66, co-authored 266 publications receiving 16795 citations. Previous affiliations of Peter Csermely include Hungarian Academy of Sciences & Joslin Diabetes Center.
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The 90-kDa molecular chaperone family : structure, function, and clinical applications. A comprehensive review
TL;DR: The present review summarizes the current knowledge about the cellular functions, expression, and clinical implications of the 90-kDa molecular chaperone family and some approaches for future research.
Associate Editor: D. Shugar The 90-kDa Molecular Chaperone Family: Structure, Function, and Clinical Applications. A Comprehensive Review
TL;DR: The 90-kDa molecular chaperone family (which comprises, among other proteins, the 90- kDa heat-shock protein, hsp90 and the 94-kda glucose-regulated protein, grp94) has become an increasingly active subject of research in the past couple of years as discussed by the authors.
Journal ArticleDOI
Structure and dynamics of molecular networks: A novel paradigm of drug discovery: A comprehensive review
Peter Csermely,Tamas Korcsmaros,Tamas Korcsmaros,Huba Kiss,Gábor London,Ruth Nussinov,Ruth Nussinov +6 more
TL;DR: It is shown how network techniques can help in the identification of single-target, edgetic, multi-target and allo-network drug target candidates and an optimized protocol of network-aided drug development is suggested, and a list of systems-level hallmarks of drug quality is provided.
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The efficiency of multi-target drugs: the network approach might help drug design.
TL;DR: It is proposed that the final effect of partial, but multiple, drug actions might often surpass that of complete drug action at a single target.
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Induced fit, conformational selection and independent dynamic segments: an extended view of binding events
TL;DR: It is argued that protein segments whose dynamics are distinct from the rest of the protein ('discrete breathers') can govern conformational transitions and allosteric propagation that accompany binding processes and, as such, might be more sensitive to mutational events.