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ATP5O — HSP90AA1
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Young et al., EMBO J 2000
:
The molecular chaperone Hsp90 binds and hydrolyses ATP, but how this
ATPase activity
regulates the interaction of
Hsp90 with a polypeptide substrate is not yet understood
Miyata et al., Nihon Yakurigaku Zasshi 2003
(Neoplasms) :
An
HSP90 inhibitor, geldanamycin, binds the ATP binding pocket of HSP90 and specifically
inhibits the essential
ATPase activity of HSP90
Zhang et al., J Mol Biol 2004
:
In carrying out these functions
Hsp90 hydrolyses ATP as it cycles between ADP- and ATP bound forms, and this
ATPase activity is
regulated by the transient association with a variety of co-chaperones
Alekseev et al., J Biol Chem 2005
:
In vitro assays demonstrate that the association of tNASP with
HSP90 stimulated the
ATPase activity of HSP90 and increased the binding of H1t to tNASP
McLaughlin et al., J Mol Biol 2006
:
Complex formation between Hsp90 and p23 increased the apparent affinity of
Hsp90 for AMP-PNP and completely
inhibited the
ATPase activity
Hawkins et al., Development 2008
:
The
ATPase dependent chaperoning activity of
Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis
Duerfeldt et al., Organic letters 2009
:
These new compounds exhibited
Hsp90 ATPase inhibition and induced Hsp90 dependent client protein degradation in a dose dependent manner
Narayan et al., J Biol Chem 2009
:
Conversely, the half-life of IRF-1 is increased by
Hsp90 in an
ATPase dependent manner leading to the accumulation of nuclear but not cytoplasmic IRF-1
Schmid et al., Mol Cell 2011
:
In this issue of Molecular Cell, Mollapour et al. ( 2011 ) show that phosphorylation of
Hsp90 affects the
ATPase function, chaperone function, and cochaperone binding in various ways