G
Giuliano Siligardi
Researcher at University of Liverpool
Publications - 69
Citations - 3982
Giuliano Siligardi is an academic researcher from University of Liverpool. The author has contributed to research in topics: Circular dichroism & Chemistry. The author has an hindex of 29, co-authored 55 publications receiving 3757 citations. Previous affiliations of Giuliano Siligardi include Birkbeck, University of London & University of Nottingham.
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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
Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones
Chrisostomos Prodromou,Giuliano Siligardi,Ronan O'Brien,Derek N. Woolfson,Lynne Regan,Barry Panaretou,John E. Ladbury,Peter W. Piper,Laurence H. Pearl +8 more
TL;DR: An important role for TPR‐domain co‐chaperones as regulators of the ATPase activity of Hsp90 is revealed, showing that the ATP‐dependent step in HSp90‐mediated protein folding occurs after the binding of the folding client protein, and suggesting that ATP hydrolysis triggers client‐protein release.
Journal ArticleDOI
Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.
Giuliano Siligardi,Barry Panaretou,Philippe Meyer,Shradha Singh,Derek N. Woolfson,Peter W. Piper,Laurence H. Pearl,Chrisostomos Prodromou +7 more
TL;DR: It is shown that Cdc37p/p50 cdc37, like Sti1/Hop/p60, also suppresses ATP turnover by Hsp90 supporting the idea that client protein loading to HSp90 requires a “relaxed” ADP-bound conformation.
Journal ArticleDOI
Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle.
Giuliano Siligardi,Bin Hu,Barry Panaretou,Peter W. Piper,Laurence H. Pearl,Chrisostomos Prodromou +5 more
TL;DR: Data indicated that Sba1 and Aha1 regulate Hsp90 by influencing the conformational state of the “ATP lid” and consequent N-terminal dimerization, whereas Sti1 does not.