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Barry Panaretou
Researcher at King's College London
Publications - 49
Citations - 6517
Barry Panaretou is an academic researcher from King's College London. The author has contributed to research in topics: Hsp90 & Chaperone (protein). The author has an hindex of 32, co-authored 45 publications receiving 5984 citations. Previous affiliations of Barry Panaretou include University College London & Institute of Cancer Research.
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Journal ArticleDOI
Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
Maruf M.U. Ali,S. Mark Roe,Cara K. Vaughan,Phillipe Meyer,Phillipe Meyer,Barry Panaretou,Peter W. Piper,Chrisostomos Prodromou,Laurence H. Pearl +8 more
TL;DR: The structure reveals the complex architecture of the ‘closed’ state of the Hsp90 chaperone, the extensive interactions between domains and between protein chains, the detailed conformational changes in the amino-terminal domain that accompany ATP binding, and the structural basis for stabilization of the closed state by p23/Sba1.
Journal ArticleDOI
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
Barry Panaretou,Chrisostomos Prodromou,S. Mark Roe,Ronan O'Brien,John E. Ladbury,Peter W. Piper,Laurence H. Pearl +6 more
TL;DR: This work demonstrates in vitro an inherent ATPase activity in both yeast Hsp90 and the Escherichia coli homologue HtpG, which is sensitive to inhibition by the Hsp 90‐specific antibiotic geldanamycin, and suggests an ATP‐coupled chaperone cycle for HSp90‐mediated protein folding.
Journal ArticleDOI
Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.
Barry Panaretou,Giuliano Siligardi,Philippe Meyer,Alison Maloney,Janis K. Sullivan,Shradha Singh,Stefan H. Millson,Paul A. Clarke,Soren Naaby-Hansen,Soren Naaby-Hansen,Robert Stein,Robert Stein,Rainer Cramer,Rainer Cramer,Mehdi Mollapour,Paul Workman,Peter W. Piper,Laurence H. Pearl,Chrisostomos Prodromou +18 more
TL;DR: A ubiquitous family of stress-regulated proteins have been identified (Aha1, activator of Hsp90 ATPase) that bind directly to HSp90 and are required for the in vivo Hsp 90-dependent activation of clients such as v-Src, implicating them as cochaperones of the Hsp80 system.
Journal ArticleDOI
The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the N-terminal domains
Chrisostomos Prodromou,Barry Panaretou,Barry Panaretou,Shahzad Chohan,Giuliano Siligardi,Ronan O'Brien,John E. Ladbury,S. Mark Roe,Peter W. Piper,Laurence H. Pearl +9 more
TL;DR: Data show that Hsp90 has a molecular ‘clamp’ mechanism, similar to DNA gyrase and MutL, whose opening and closing by transient N‐terminal dimerization are directly coupled to the ATPase cycle.
Journal ArticleDOI
Structural and Functional Analysis of the Middle Segment of Hsp90 Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions
Philippe Meyer,Chrisostomos Prodromou,Bin Hu,Cara K. Vaughan,S. Mark Roe,Barry Panaretou,Peter W. Piper,Laurence H. Pearl +7 more
TL;DR: From this structure, residues implicated in the ATPase-coupled conformational cycle and in interactions with client proteins and the activating cochaperone Aha1 have been identified, and their roles functionally characterized in vitro and in vivo.