Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein. (Q34212832)

From Wikidata

Jump to navigation Jump to search

scientific article

Language	Label	Description	Also known as
English	Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein.	scientific article

Statements

scholarly article

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12851401%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein (English)

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12851401%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

Hepatitis B virus

1 reference

based on heuristic

inferred from title

1 reference

based on heuristic

inferred from title

1

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12851401%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

2

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12851401%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

author name string

Jürgen Beck

1

1 reference

Europe PubMed Central

31 July 2017

Michael Nassal

2

1 reference

Europe PubMed Central

31 July 2017

language of work or name

0 references

publication date

8 July 2003

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12851401%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

Journal of Biological Chemistry

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12851401%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

278

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12851401%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

38

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12851401%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

36128-36138

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12851401%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

Molecular chaperones in the cytosol: from nascent chain to folded protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Hsp90: a specialized but essential protein-folding tool

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Steroid receptor interactions with heat shock protein and immunophilin chaperones

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Hsp90 & Co. - a holding for folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Hsp90: chaperoning signal transduction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

The assembly of progesterone receptor-hsp90 complexes using purified proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

The role of DnaJ-like proteins in glucocorticoid receptor.hsp90 heterocomplex assembly by the reconstituted hsp90.p60.hsp70 foldosome complex.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Stable association of hsp90 and p23, but Not hsp70, with active human telomerase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Hepatitis B virus, the vaccine, and the control of primary cancer of the liver

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Hepatitis B virus replication: novel roles for virus-host interactions.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

The encapsidation signal on the hepatitis B virus RNA pregenome forms a stem-loop structure that is critical for its function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Formation of a functional hepatitis B virus replication initiation complex involves a major structural alteration in the RNA template.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Reconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Stimulation of the weak ATPase activity of human hsp90 by a client protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Experimental confirmation of a hepatitis B virus (HBV) epsilon-like bulge-and-loop structure in avian HBV RNA encapsidation signals

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

A small 2'-OH- and base-dependent recognition element downstream of the initiation site in the RNA encapsidation signal is essential for hepatitis B virus replication initiation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Initiation of HIV-1 reverse transcription is regulated by a primer activation signal

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

The human DnaJ protein, hTid-1, enhances binding of a multimer of the herpes simplex virus type 1 UL9 protein to oris, an origin of viral DNA replication

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Human T cell leukemia virus type 1 Tax associates with a molecular chaperone complex containing hTid-1 and Hsp70

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Stoichiometry, abundance, and functional significance of the hsp90/hsp70-based multiprotein chaperone machinery in reticulocyte lysate.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Macromolecular crowding: obvious but underappreciated

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301069200

21 January 2018

Identifiers

10.1074/JBC.M301069200

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12851401%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12851401%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q34212832&oldid=1979871360"