(Q24681597)

Hsp90 family chaperone HSC82 YMR186W

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

Jun Imai

1

0 references

Mikako Maruya

2

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Hideki Yashiroda

3

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Ichiro Yahara

4

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Keiji Tanaka

Hsp90: a specialized but essential protein-folding tool

5

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language of work or name

English

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publication date

15 July 2003

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published in

The EMBO Journal

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volume

22

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page(s)

3557-67

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issue

14

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cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Mechanisms underlying ubiquitination

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Rpn9 is required for efficient assembly of the yeast 26S proteasome

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly.

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Calcium-sensitive cls mutants of Saccharomyces cerevisiae showing a Pet- phenotype are ascribable to defects of vacuolar membrane H(+)-ATPase activity

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Folding of newly translated proteins in vivo: the role of molecular chaperones

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

The proteasome: paradigm of a self-compartmentalizing protease

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Hsp90: chaperoning signal transduction

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

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

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

In vivo reactivation of heat-denatured protein in the endoplasmic reticulum of yeast

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Durable synthesis of high molecular weight heat shock proteins in G0 cells of the yeast and other eucaryotes

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Assembly of the 26 S complex that degrades proteins ligated to ubiquitin is accompanied by the formation of ATPase activity.

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20 S proteasome.

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=165619

Proteasomes (multi-protease complexes) as 20 S ring-shaped particles in a variety of eukaryotic cells

28 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12853471

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

The proteasome (multicatalytic protease) is a component of the 1500-kDa proteolytic complex which degrades ubiquitin-conjugated proteins

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12853471

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Growth-dependent change of the 26S proteasome in budding yeast

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12853471

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1093/EMBOJ/CDG349

1 reference

4445382

4445382

1 reference

1 reference

1 reference