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Literature DB >> 8577714

Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.

Abstract

The heat shock protein Hsp90 is known as an essential component of several signal transduction pathways and has now been identified as an essential host factor for hepatitis B virus replication. Hsp90 interacts with the viral reverse transcriptase to facilitate the formation of a ribonucleoprotein (RNP) complex between the polymerase and an RNA ligand. This RNP complex is required early in replication for viral assembly and initiation of DNA synthesis through a protein-priming mechanism. These results thus invoke a role for the Hsp90 pathway in the formation of an RNP.

Entities: Gene Species

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Year: 1996 PMID： 8577714 PMCID： PMC40030 DOI： 10.1073/pnas.93.3.1060

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

31 in total

1. Role of RNA in enzymatic activity of the reverse transcriptase of hepatitis B viruses.

Authors: G H Wang; F Zoulim; E H Leber; J Kitson; C Seeger
Journal: J Virol Date: 1994-12 Impact factor: 5.103

2. Novel mechanism for reverse transcription in hepatitis B viruses.

Authors: G H Wang; C Seeger
Journal: J Virol Date: 1993-11 Impact factor: 5.103

Review 3. Hold 'em and fold 'em: chaperones and signal transduction.

Authors: S P Bohen; A Kralli; K R Yamamoto
Journal: Science Date: 1995-06-02 Impact factor: 47.728

Review 4. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor.

Authors: W B Pratt
Journal: J Biol Chem Date: 1993-10-15 Impact factor: 5.157

5. Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains.

Authors: C Antonsson; M L Whitelaw; J McGuire; J A Gustafsson; L Poellinger
Journal: Mol Cell Biol Date: 1995-02 Impact factor: 4.272

6. A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23.

Authors: J L Johnson; D O Toft
Journal: J Biol Chem Date: 1994-10-07 Impact factor: 5.157

7. A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.

Authors: J McGuire; M L Whitelaw; I Pongratz; J A Gustafsson; L Poellinger
Journal: Mol Cell Biol Date: 1994-04 Impact factor: 4.272

8. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.

Authors: L Whitesell; E G Mimnaugh; B De Costa; C E Myers; L M Neckers
Journal: Proc Natl Acad Sci U S A Date: 1994-08-30 Impact factor: 11.205

9. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes.

Authors: J L Johnson; T G Beito; C J Krco; D O Toft
Journal: Mol Cell Biol Date: 1994-03 Impact factor: 4.272

10. Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis.

Authors: J R Pollack; D Ganem
Journal: J Virol Date: 1994-09 Impact factor: 5.103

135 in total

9. In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90.

Authors: J Hu; D Anselmo
Journal: J Virol Date: 2000-12 Impact factor: 5.103

10. Duck hepatitis B virus virion secretion requires a double-stranded DNA genome.

Authors: David Perlman; Jianming Hu
Journal: J Virol Date: 2003-02 Impact factor: 5.103

Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.

1. Role of RNA in enzymatic activity of the reverse transcriptase of hepatitis B viruses.

2. Novel mechanism for reverse transcription in hepatitis B viruses.

Review 3. Hold 'em and fold 'em: chaperones and signal transduction.

Review 4. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor.

5. Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains.

6. A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23.

7. A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.

8. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.

9. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes.

10. Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis.

1. Functional requirement of p23 and Hsp90 in telomerase complexes.

2. Polymerization defects within human telomerase are distinct from telomerase RNA and TEP1 binding.

3. Host cell factor requirement for hepatitis C virus enzyme maturation.

4. In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins.

5. Distinct requirement for two stages of protein-primed initiation of reverse transcription in hepadnaviruses.

6. Heat shock protein 90-independent activation of truncated hepadnavirus reverse transcriptase.

7. Inhibition of heat-shock protein 90 reduces Ebola virus replication.

8. Expression of hTERT and hTR in cis reconstitutes and active human telomerase ribonucleoprotein.

9. In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90.

10. Duck hepatitis B virus virion secretion requires a double-stranded DNA genome.