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Literature DB >> 11732320

Isolation and quantification of the heat shock protein 90 alpha and beta isoforms from rat liver.

Abstract

Heat shock protein 90 (Hsp90) is an abundant cytosolic protein. In higher eukaryotes two isoforms of Hsp90 exist, Hsp90 alpha and Hsp90 beta. Hsp90 was purified from rat liver and after sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a double band at about 90 kDa. The two bands were separated and identified as the Hsp90 alpha and Hsp90 beta isoforms. There was no entry in the protein databases for the Hsp90 alpha isoform from rat. Furthermore, the ratio of the two Hsp90 isoforms was determined.

Entities: Chemical Gene Species

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Year: 2001 PMID： 11732320 DOI： 10.1007/bf01288360

Source DB: PubMed Journal: Protoplasma ISSN： 0033-183X Impact factor: 3.356

14 in total

Review 1. Structure and in vivo function of Hsp90.

Authors: L H Pearl; C Prodromou
Journal: Curr Opin Struct Biol Date: 2000-02 Impact factor: 6.809

Review 2. Hsp90 & Co. - a holding for folding.

Authors: J Buchner
Journal: Trends Biochem Sci Date: 1999-04 Impact factor: 13.807

Review 3. Molecular chaperones: the busy life of Hsp90.

Authors: M P Mayer; B Bukau
Journal: Curr Biol Date: 1999-05-06 Impact factor: 10.834

4. Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence.

Authors: T Scheibel; T Weikl; J Buchner
Journal: Proc Natl Acad Sci U S A Date: 1998-02-17 Impact factor: 11.205

5. The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding.

Authors: B C Freeman; R I Morimoto
Journal: EMBO J Date: 1996-06-17 Impact factor: 11.598

Review 6. The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase.

Authors: W B Pratt
Journal: Annu Rev Pharmacol Toxicol Date: 1997 Impact factor: 13.820

7. Two-step purification and N-terminal amino acid sequence analysis of the rat Mr 90,000 heat shock protein.

Authors: M Denis
Journal: Anal Biochem Date: 1988-09 Impact factor: 3.365

8. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors: U K Laemmli
Journal: Nature Date: 1970-08-15 Impact factor: 49.962

9. Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo.

Authors: U Jakob; H Lilie; I Meyer; J Buchner
Journal: J Biol Chem Date: 1995-03-31 Impact factor: 5.157

Isolation and quantification of the heat shock protein 90 alpha and beta isoforms from rat liver.

Review 1. Structure and in vivo function of Hsp90.

Review 2. Hsp90 & Co. - a holding for folding.

Review 3. Molecular chaperones: the busy life of Hsp90.

4. Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence.

5. The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding.

Review 6. The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase.

7. Two-step purification and N-terminal amino acid sequence analysis of the rat Mr 90,000 heat shock protein.

8. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

9. Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo.

10. Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein.

1. A novel function for the 90 kDa heat-shock protein (Hsp90): facilitating nuclear export of 60 S ribosomal subunits.

2. A proteomic analysis of acute leukemia cells treated with 9-hydroxyoctadecadienoic acid.

Review 3. Maximizing the Therapeutic Potential of HSP90 Inhibitors.

4. Molecular cloning, phylogenetic analysis and heat shock response of Babesia gibsoni heat shock protein 90.