Heat-shock protein 90, a chaperone for folding and regulation

By Didier Picard. Cellular and Molecular Life Sciences (CMLS), 2002

818 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/dbfb65a6faf37b4686b51ad1f4e988d277654693

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

1. M. Haslbeck
2. J. Buchner
3. K. Richter

In Molecular Biology

1. M. Haslbeck
2. J. Buchner
3. K. Richter

Citations in the corpus

• 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).”
• The heat shock response: life on the verge of death. (2010, background): “First, it does not seem as promiscuous in its substrate spectrum as GroE or Hsp70 (Picard, 2002; Pratt and Toft, 2003; Smith, 1998).”
• Apoptosis and Molecular Targeting Therapy in Cancer (2014, background): “Heat shock proteins 90 (Hsp90s) are abundantly and ubiquitously expressed proteins required for the energy-driven stabilisation, conformation, and function of a large number of cellular proteins, named clinets [266, 267].”