(Q39320913)

11 September 2017

Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. (English)

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11 September 2017

Saccharomyces cerevisiae

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Martin Haslbeck

1

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11 September 2017

Nathalie Braun

2

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11 September 2017

Thusnelda Stromer

3

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11 September 2017

Bettina Richter

4

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11 September 2017

Natascha Model

5

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11 September 2017

Sevil Weinkauf

6

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11 September 2017

Johannes Buchner

7

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11 September 2017

language of work or name

English

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publication date

29 January 2004

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11 September 2017

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11 September 2017

23

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3

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11 September 2017

638-649

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describes a project that uses

11 September 2017

ImageQuant

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11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC1271810/fullTextXML

inferred from PubMed Central ID database lookup

cites work

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Global analysis of protein expression in yeast

11 September 2017

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Trigger Factor and DnaK possess overlapping substrate pools and binding specificities

11 September 2017

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11 September 2017

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sHsps and their role in the chaperone network

11 September 2017

1 reference

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sHsp-phosphorylation: enzymes, signaling pathways and functional implications

11 September 2017

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Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.

11 September 2017

1 reference

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Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones

11 September 2017

1 reference

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Crystal structure and assembly of a eukaryotic small heat shock protein

11 September 2017

1 reference

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Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Mec1p

11 September 2017

1 reference

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Identification of peroxisomal membrane proteins of Saccharomyces cerevisiae by mass spectrometry

11 September 2017

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Phosphorylation-induced change of the oligomerization state of alpha B-crystallin

11 September 2017

1 reference

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The current state of two-dimensional electrophoresis with immobilized pH gradients

11 September 2017

1 reference

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A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein

11 September 2017

1 reference

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Hsp26: a temperature-regulated chaperone

11 September 2017

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The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species

11 September 2017

1 reference

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Crystal structure of a small heat-shock protein

11 September 2017

1 reference

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Exploring the metabolic and genetic control of gene expression on a genomic scale

11 September 2017

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In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

11 September 2017

1 reference

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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

11 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

11 September 2017

1 reference

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A new generation of the IMAGIC image processing system

11 September 2017

1 reference

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Multimerization of Hsp42p, a novel heat shock protein of Saccharomyces cerevisiae, is dependent on a conserved carboxyl-terminal sequence.

11 September 2017

1 reference

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Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis

11 September 2017

1 reference

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[12] One-step gene disruption in yeast

11 September 2017

1 reference

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10 Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast

11 September 2017

1 reference

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Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases

11 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

hsp26 of Saccharomyces cerevisiae is related to the superfamily of small heat shock proteins but is without a demonstrable function

11 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

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

11 September 2017

1 reference

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Tackling the protease problem in Saccharomyces cerevisiae

11 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Alpha-crystallin can function as a molecular chaperone

11 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies

11 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Genealogy of the alpha-crystallin--small heat-shock protein superfamily

17 June 2018

1 reference

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A review of phenotypes in Saccharomyces cerevisiae

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Small heat shock proteins are molecular chaperones.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

The small heat-shock protein Hsp26 of Saccharomyces cerevisiae assembles into a high molecular weight aggregate

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

In vivo observation of polypeptide flux through the bacterial chaperonin system.

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Conformational properties of substrate proteins bound to a molecular chaperone alpha-crystallin

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea.

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Structure and expression of a yeast gene encoding the small heat-shock protein Hsp26.

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Analysis of the Interaction of Small Heat Shock Proteins with Unfolding Proteins

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271810

Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures

2 December 2018

1 reference

12 December 2020

Osmostress-induced changes in yeast gene expression

1 reference

12 December 2020

Thermal protein denaturation and protein aggregation in cells made thermotolerant by various chemicals: role of heat shock proteins

1 reference

12 December 2020

HySP26 gene transcription is strongly induced during Saccharomyces cerevisiae growth at low pH

1 reference

12 December 2020

Analysis of chaperone function using citrate synthase as nonnative substrate protein

1 reference

12 December 2020

Identification of in vivo substrates of the chaperonin GroEL

1 reference

12 December 2020

Chaperone activity and homo- and hetero-oligomer formation of bacterial small heat shock proteins

1 reference

12 December 2020

Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity

1 reference

12 December 2020

Subunit Exchange of Multimeric Protein Complexes

1 reference

12 December 2020

Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro

1 reference

12 December 2020

Hsp26 is not required for growth at high temperatures, nor for thermotolerance, spore development, or germination

1 reference

12 December 2020

Chaperone-like function of lipocortin 1

1 reference

12 December 2020

One-step gene disruption in yeast

1 reference

12 December 2020

Identifiers

DOI

10.1038/SJ.EMBOJ.7600080

1 reference

release_p5wskhtp2zewfgdjzzv2g7skdq

11 September 2017

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/p5wskhtp2zewfgdjzzv2g7skdq

24 November 2022

mapped directly with Wikidata item

1 reference

11 September 2017

PubMed publication ID

14749732

1 reference