STIP1 wt Allele

Known as: STI1, HOP, Stress-Induced-Phosphoprotein 1 wt Allele 
Human STIP1 wild-type allele is located in the vicinity of 11q13 and is approximately 19 kb in length. This allele, which encodes stress-induced… (More)
National Institutes of Health

Papers overview

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Highly Cited
2012
Highly Cited
2012
Sti1/Hop is a modular protein required for the transfer of client proteins from the Hsp70 to the Hsp90 chaperone system in… (More)
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Highly Cited
2011
Highly Cited
2011
The chaperone cycle of heat shock protein-90 (Hsp90) involves progression through defined complexes with different cochaperones… (More)
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2010
2010
Transmissible spongiform encephalopathies are fatal neurodegenerative diseases caused by the conversion of prion protein (PrP(C… (More)
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Highly Cited
2010
Highly Cited
2010
Recognition of pathogen-associated molecular patterns (PAMPs) by pattern recognition receptors (PRRs) represents a critical first… (More)
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Highly Cited
2009
Highly Cited
2009
The molecular chaperone heat-shock protein 90 (Hsp90) couples ATP hydrolysis to conformational changes driving a reaction cycle… (More)
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Highly Cited
2005
Highly Cited
2005
Understanding the physiological function of the cellular prion (PrPc) depends on the investigation of PrPc-interacting proteins… (More)
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Highly Cited
2004
Highly Cited
2004
ATP hydrolysis by the Hsp90 molecular chaperone requires a connected set of conformational switches triggered by ATP binding to… (More)
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Highly Cited
2003
Highly Cited
2003
The molecular chaperone Hsp90 is known to be involved in the activation of key regulatory proteins such as kinases, steroid… (More)
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Highly Cited
2002
Highly Cited
2002
Prions are composed of an isoform of a normal sialoglycoprotein called PrP(c), whose physiological role has been under… (More)
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Highly Cited
1999
Highly Cited
1999
The in vivo function of the heat shock protein 90 (Hsp90) molecular chaperone is dependent on the binding and hydrolysis of ATP… (More)
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