Hsp90: a specialized but essential protein-folding tool.
By J. Young, I. Moarefi, U. Hartl. Journal of Cell Biology, 2001
832 citations recorded by the source corpus.
Subfields: Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/0b304357e945b555a8ba5da1646e1e54d356c393
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Immunology
In Molecular Biology
- Susan Lindquist
- J. Buchner
- William E. Balch
- P. Schulte
- D. Krappmann
- A. Todgham
- C. Scheidereit
- Richard I. Morimoto
Citations in the corpus
- Rab‐αGDI activity is regulated by a Hsp90 chaperone complex (2002, methodology): “…of endogenous aGDI with Hsp90; (ii) the ability of GA/ radicicol, inhibitors of Hsp90 chaperone complex function (Richter and Buchner, 2001; Young et al., 2001), to prevent recycling of Rab3A by endogenous aGDI; (iii) the ability of GA/radicicol to prevent the ability of exogenous GST±aGDI…”
- Heat shock protein genes and their functional significance in fish. (2002, background): “Hsp90 is active in supporting various components of the cytoskeleton and steroid hormone receptors (Csermely et al., 1998; Pearl and Prodromou, 2000; Young et al., 2001).”
- Hsp70 and Hsp90--a relay team for protein folding. (2004, background): “…a wide variety of in vivo substrates is known for the Hsp70/Hsp90 chaperone network (Table 1) (Buchner 1999; Jolly and Morimoto 2000; Mayer et al. 2001; Picard 2002; Pratt and Toft 1997; Richter and Buchner 2001; Smith and Toft 1993; Walter and Buchner 2002; Young et al. 2001; Zylicz et al. 2001).”
- Hsp90 as a capacitor of phenotypic variation (2002, background): “The requirement of many principal regulatory proteins for Hsp90 renders entire pathways sensitive to decreases in its functio”
- Requirement of Hsp90 activity for IκB kinase (IKK) biosynthesis and for constitutive and inducible IKK and NF-κB activation (2004, background): “This drug specifically inhibits the ATPase activity of Hsp90, which results in the degradation of many Hsp90 client proteins by the ubiquitin–proteasome machinery (Hohfeld et al., 2001; Young et al., 2001).”