Aggregation of hsp70 and hsc70in vivois distinct and ï¿½temperature-dependent and their chaperone function is ï¿½directly related to non-aggregated forms-Reference-Cited by-同舟云学术

Aggregation of hsp70 and hsc70in vivois distinct and ï¿½temperature-dependent and their chaperone function is ï¿½directly related to non-aggregated forms

Published:1999-01 Issue:1-2 Volume:259 Page:505-512
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

Angelidis Charalampos E.,Lazaridis Ioannis,Pagoulatos Gerassimos N.

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1432-1327.1999.00078.x/fullpdf

Reference50 articles.

1. Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts.;Li;Proc. Natl. Acad. Sci. USA,1982

2. Constitutive expression of heat-shock protein 70 in mammalian cells confers thermoresistance.;Angelidis;Eur. J. Biochem.,1991

3. Thermal response of rat fibroblasts stably transfected with the human 70-KDa heat shock protein-encoding gene.;Li;Proc. Natl. Acad. USA,1991

4. Overexpression of HSP70 in transgenic mice results in increased cell thermotolerance.;Angelidis;Transgenics,1996

5. Transgenic mice expressing the human heat shock protein 70 have improved post-ischemic myocardial recovery.;Plumier;J. Clin. Invest.,1995

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