A novel mode of chaperone action: heme activation of Hap1 by enhanced association of Hsp90 with the repressed Hsp70-Hap1 complex. (Q27930628)

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A novel mode of chaperone action: heme activation of Hap1 by enhanced association of Hsp90 with the repressed Hsp70-Hap1 complex

Language	Label	Description	Also known as
English	A novel mode of chaperone action: heme activation of Hap1 by enhanced association of Hsp90 with the repressed Hsp70-Hap1 complex.	scientific article	A novel mode of chaperone action: heme activation of Hap1 by enhanced association of Hsp90 with the repressed Hsp70-Hap1 complex

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scholarly article

2 references

1 December 2016

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15102838%20AND%20SRC:MED&resulttype=core&format=json

27 December 2019

A novel mode of chaperone action: heme activation of Hap1 by enhanced association of Hsp90 with the repressed Hsp70-Hap1 complex (English)

1 reference

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27 December 2019

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molecular chaperones

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Hsp90 family chaperone HSP82 YPL240C

1 reference

GOA release 2020-03-11

4

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27 December 2019

author name string

Shan Tang

3

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27 December 2019

Hee Chul Lee

2

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27 December 2019

Changgui Lan

1

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language of work or name

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publication date

21 April 2004

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27 December 2019

Journal of Biological Chemistry

2 references

1 December 2016

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15102838%20AND%20SRC:MED&resulttype=core&format=json

27 December 2019

279

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27 December 2019

26

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27 December 2019

27607-27612

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27 December 2019

Hsp90's secrets unfold: new insights from structural and functional studies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

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.M402777200

21 January 2018

Protein folding in vivo: unraveling complex pathways

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Hsp90 as a capacitor for morphological evolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

The Hsp70 and Hsp60 chaperone machines

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Visualization and mechanism of assembly of a glucocorticoid receptor.Hsp70 complex that is primed for subsequent Hsp90-dependent opening of the steroid binding cleft

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Reduced levels of hsp90 compromise steroid receptor action in vivo

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Functional dissection and sequence of yeast HAP1 activator.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

The molecular chaperone Hsp90 mediates heme activation of the yeast transcriptional activator Hap1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Isolation of Hsp90 mutants by screening for decreased steroid receptor function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Molecular mechanism governing heme signaling in yeast: a higher-order complex mediates heme regulation of the transcriptional activator HAP1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

A new class of repression modules is critical for heme regulation of the yeast transcriptional activator Hap1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Two yeast La motif-containing proteins are RNA-binding proteins that associate with polyribosomes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

A heat shock transcription factor with reduced activity suppresses a yeast HSP70 mutant

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

The yeast activator HAP1--a GAL4 family member--binds DNA in a directly repeated orientation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Structural environment dictates the biological significance of heme-responsive motifs and the role of Hsp90 in the activation of the heme activator protein Hap1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Hormone-dependent transactivation by the human androgen receptor is regulated by a dnaJ protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

The 90 kDa heat-shock protein (hsp90) modulates the binding of the oestrogen receptor to its cognate DNA.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

The molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Molecular mechanism of heme signaling in yeast: the transcriptional activator Hap1 serves as the key mediator.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

The yeast galactose genetic switch is mediated by the formation of a Gal4p-Gal80p-Gal3p complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Nondissociation of GAL4 and GAL80 in vivo after galactose induction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Two heme-binding domains of heme-regulated eukaryotic initiation factor-2alpha kinase. N terminus and kinase insertion

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

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.M402777200

21 January 2018

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402777200

21 January 2018

Identifiers

10.1074/JBC.M402777200

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15102838%20AND%20SRC:MED&resulttype=core&format=json

27 December 2019

2 references

1 December 2016

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15102838%20AND%20SRC:MED&resulttype=core&format=json

27 December 2019

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