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Literature DB >> 14627194

What is a co-chaperone?

Avrom J Caplan¹.

Abstract

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Year: 2003 PMID： 14627194 PMCID： PMC514860 DOI： 10.1379/1466-1268(2003)008<0105:wiac>2.0.co;2

Source DB: PubMed Journal: Cell Stress Chaperones ISSN： 1355-8145 Impact factor: 3.667

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8 in total

Review 1. The tetratricopeptide repeat: a structural motif mediating protein-protein interactions.

Authors: G L Blatch; M Lässle
Journal: Bioessays Date: 1999-11 Impact factor: 4.345

Review 2. Structure, function, and mechanism of the Hsp90 molecular chaperone.

Authors: L H Pearl; C Prodromou
Journal: Adv Protein Chem Date: 2001

Review 3. Folding of newly translated proteins in vivo: the role of molecular chaperones.

Authors: J Frydman
Journal: Annu Rev Biochem Date: 2001 Impact factor: 23.643

4. Disassembly of transcriptional regulatory complexes by molecular chaperones.

Authors: Brian C Freeman; Keith R Yamamoto
Journal: Science Date: 2002-06-21 Impact factor: 47.728

5. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding.

Authors: T Langer; C Lu; H Echols; J Flanagan; M K Hayer; F U Hartl
Journal: Nature Date: 1992-04-23 Impact factor: 49.962

6. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.

Authors: Laurent Meunier; Young-Kwang Usherwood; Kyung Tae Chung; Linda M Hendershot
Journal: Mol Biol Cell Date: 2002-12 Impact factor: 4.138

7. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle.

Authors: J Höhfeld; Y Minami; F U Hartl
Journal: Cell Date: 1995-11-17 Impact factor: 41.582

8. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.

Authors: K Liberek; J Marszalek; D Ang; C Georgopoulos; M Zylicz
Journal: Proc Natl Acad Sci U S A Date: 1991-04-01 Impact factor: 11.205

8 in total

30 in total

1. Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.

Authors: Fulai Ran; Nidhi Gadura; Corinne A Michels
Journal: J Biol Chem Date: 2010-02-22 Impact factor: 5.157

2. Stress response in the ascidian Ciona intestinalis: transcriptional profiling of genes for the heat shock protein 70 chaperone system under heat stress and endoplasmic reticulum stress.

Authors: Tetsuya Fujikawa; Takeo Munakata; Shin-ichi Kondo; Nori Satoh; Shuichi Wada
Journal: Cell Stress Chaperones Date: 2009-07-23 Impact factor: 3.667

3. The L279P mutation of nuclear distribution gene C (NudC) influences its chaperone activity and lissencephaly protein 1 (LIS1) stability.

Authors: Xiao-Jing Zhu; Xunyan Liu; Qi Jin; Yuqi Cai; Yuehong Yang; Tianhua Zhou
Journal: J Biol Chem Date: 2010-07-30 Impact factor: 5.157

What is a co-chaperone?

Review 1. The tetratricopeptide repeat: a structural motif mediating protein-protein interactions.

Review 2. Structure, function, and mechanism of the Hsp90 molecular chaperone.

Review 3. Folding of newly translated proteins in vivo: the role of molecular chaperones.

4. Disassembly of transcriptional regulatory complexes by molecular chaperones.

5. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding.

6. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.

7. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle.

8. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.

1. Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.

2. Stress response in the ascidian Ciona intestinalis: transcriptional profiling of genes for the heat shock protein 70 chaperone system under heat stress and endoplasmic reticulum stress.

3. The L279P mutation of nuclear distribution gene C (NudC) influences its chaperone activity and lissencephaly protein 1 (LIS1) stability.

Review 4. Targeting Hsp90 and its co-chaperones to treat Alzheimer's disease.

Review 5. Getting folded: chaperone proteins in muscle development, maintenance and disease.

6. HOP expression is regulated by p53 and RAS and characteristic of a cancer gene signature.

Review 7. TPR-containing proteins control protein organization and homeostasis for the endoplasmic reticulum.

Review 8. Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket.

9. An AlphaScreen-based high-throughput screen to identify inhibitors of Hsp90-cochaperone interaction.

Review 10. Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases.