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Details on Person Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

Class:IdLiteratureReference:8938575
_displayNameStructural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions
_timestamp2016-09-09 21:52:32
author[Person:110642] Meyer, P
[Person:1221656] Prodromou, C
[Person:453286] Hu, B
[Person:8938579] Vaughan, Cara
[Person:196205] Roe, S Mark
[Person:1221653] Panaretou, B
[Person:3371559] Piper, Peter W
[Person:196207] Pearl, Laurence H
created[InstanceEdit:8938553] Shamovsky, Veronica, 2016-09-09
journalMol. Cell
pages647-58
pubMedIdentifier12667448
titleStructural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions
volume11
year2003
(literatureReference)[Summation:8938541] The molecular chaperone heat-shock protein 90 (HSP90) functi...
[Summation:8948955] The chaperoning function of HSP90 is coupled to its ATPase a...
[Summation:9035372] The unliganded mineralocorticoid receptor (MR or NR3C2) is l...
[Summation:9605365] Ligand binding triggers NLS exposure due to the replacement ...
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