Literature DB >> 9749880

The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review.

P Csermely1, T Schnaider, C Soti, Z Prohászka, G Nardai.   

Abstract

The 90-kDa molecular chaperone family (which comprises, among other proteins, the 90-kDa heat-shock protein, hsp90 and the 94-kDa glucose-regulated protein, grp94, major molecular chaperones of the cytosol and of the endoplasmic reticulum, respectively) has become an increasingly active subject of research in the past couple of years. These ubiquitous, well-conserved proteins account for 1-2% of all cellular proteins in most cells. However, their precise function is still far from being elucidated. Their involvement in the aetiology of several autoimmune diseases, in various infections, in recognition of malignant cells, and in antigen-presentation already demonstrates the essential role they likely will play in clinical practice of the next decade. The present review summarizes our current knowledge about the cellular functions, expression, and clinical implications of the 90-kDa molecular chaperone family and some approaches for future research.

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Year:  1998        PMID: 9749880     DOI: 10.1016/s0163-7258(98)00013-8

Source DB:  PubMed          Journal:  Pharmacol Ther        ISSN: 0163-7258            Impact factor:   12.310


  265 in total

1.  Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 In vivo.

Authors:  S Bharadwaj; A Ali; N Ovsenek
Journal:  Mol Cell Biol       Date:  1999-12       Impact factor: 4.272

2.  The Hsp90 chaperone complex A potential target for cancer therapy?

Authors:  Beatrice D Darimont
Journal:  World J Gastroenterol       Date:  1999-06       Impact factor: 5.742

3.  The Hsp90 family of proteins in Arabidopsis thaliana.

Authors:  P Krishna; G Gloor
Journal:  Cell Stress Chaperones       Date:  2001-07       Impact factor: 3.667

4.  MOD-D, a Galpha subunit of the fungus Podospora anserina, is involved in both regulation of development and vegetative incompatibility.

Authors:  G Loubradou; J Bégueret; B Turcq
Journal:  Genetics       Date:  1999-06       Impact factor: 4.562

5.  Combined in silico and experimental approach for drug design: the binding mode of peptidic and non-peptidic inhibitors to hsp90 N-terminal domain.

Authors:  Simona Tomaselli; Massimiliano Meli; Janet Plescia; Lucia Zetta; Dario C Altieri; Giorgio Colombo; Laura Ragona
Journal:  Chem Biol Drug Des       Date:  2010-11       Impact factor: 2.817

6.  Alternative approaches to Hsp90 modulation for the treatment of cancer.

Authors:  Jessica A Hall; Leah K Forsberg; Brian S J Blagg
Journal:  Future Med Chem       Date:  2014-09       Impact factor: 3.808

Review 7.  Macrocyclic inhibitors of hsp90.

Authors:  Victoria A Johnson; Erinprit K Singh; Lidia A Nazarova; Leslie D Alexander; Shelli R McAlpine
Journal:  Curr Top Med Chem       Date:  2010       Impact factor: 3.295

8.  Combinatorial interaction of cis elements specifies the expression of the Arabidopsis AtHsp90-1 gene.

Authors:  Kosmas Haralampidis; Dimitra Milioni; Stamatis Rigas; Polydefkis Hatzopoulos
Journal:  Plant Physiol       Date:  2002-07       Impact factor: 8.340

9.  CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.

Authors:  Yoshihiko Miyata; Eisuke Nishida
Journal:  Mol Cell Biol       Date:  2004-05       Impact factor: 4.272

10.  Heat shock protein 90-α mediates aldo-keto reductase 1B10 (AKR1B10) protein secretion through secretory lysosomes.

Authors:  Dixian Luo; Yiwen Bu; Jun Ma; Sandeep Rajput; Yingchun He; Guangxian Cai; Duan-Fang Liao; Deliang Cao
Journal:  J Biol Chem       Date:  2013-11-11       Impact factor: 5.157

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