(Q27316581)

English

Metabolic and chaperone gene loss marks the origin of animals: evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clients

scientific article (publication date: 2015)

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scholarly article

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Metabolic and chaperone gene loss marks the origin of animals: evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clients (English)

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molecular chaperones

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1 reference

based on heuristic

inferred from title

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based on heuristic

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author name string

Albert J Erives

1

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Jan S Fassler

2

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language of work or name

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publication date

2015

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10

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2

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e0117192

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copyright license

Creative Commons Attribution 4.0 International

24 February 2015

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April 2022 Public Data File from Crossref

copyright status

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The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria

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The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress response element (STRE)

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HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases

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The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function

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HSP104 required for induced thermotolerance

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Unexpected repertoire of metazoan transcription factors in the unicellular holozoan Capsaspora owczarzaki

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The dawn of developmental signaling in the metazoa

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Early evolution of metazoan transcription factors.

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Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.

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Hsp104: a weapon to combat diverse neurodegenerative disorders.

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The yeast heat shock transcription factor changes conformation in response to superoxide and temperature

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28 September 2017

Identification of cis and trans components of a novel heat shock stress regulatory pathway in Saccharomyces cerevisiae

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Organization of the Drosophila melanogaster hsp70 heat shock regulation unit

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28 September 2017

Hsp104 is required for tolerance to many forms of stress

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28 September 2017

Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients.

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28 September 2017

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31 May 2018

Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in unstressed and heat-shocked cells.

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21 January 2018

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Different mechanisms are involved in the transcriptional activation by yeast heat shock transcription factor through two different types of heat shock elements.

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21 January 2018

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21 January 2018

The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The Lys20 homocitrate synthase isoform exerts most of the flux control over the lysine synthesis pathway in Saccharomyces cerevisiae

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1371/JOURNAL.PONE.0117192

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2015PLoSO..1017192E

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1 reference

release_ira76hqqhrfkxlqe3rypuqaggy

0 references

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

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