Protein disaggregation mediated by heat-shock protein Hsp104. (Q27940314)

1 December 2016

title

Protein disaggregation mediated by heat-shock protein Hsp104. (English)

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PubMed

Chaperone ATPase HSP104 YLL026W

1 December 2016

main subject

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GOA release 2020-03-11

author name string

D A Parsell

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A S Kowal

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M A Singer

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S Lindquist

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language of work or name

English

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publication date

1 December 1994

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1 reference

Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes

1 December 2016

volume

372

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issue

6505

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page(s)

475-8

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cites work

1 reference

7 January 2021

Hsp104 is a highly conserved protein with two essential nucleotide-binding sites

1 reference

7 January 2021

ClpB is the Escherichia coli heat shock protein F84.1.

1 reference

7 January 2021

The Clp proteins: proteolysis regulators or molecular chaperones?

1 reference

7 January 2021

Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance

1 reference

7 January 2021

HSP104 required for induced thermotolerance

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7 January 2021

Genetic evidence for a functional relationship between Hsp104 and Hsp70.

1 reference

7 January 2021

Bacterial luciferase alpha beta fusion protein is fully active as a monomer and highly sensitive in vivo to elevated temperature

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7 January 2021

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

1 reference

7 January 2021

Ultrastructural changes in yeast following heat shock and recovery.

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7 January 2021

The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

1 reference

7 January 2021

Aggregation equilibria of Escherichia coli RNA polymerase: evidence for anion-linked conformational transitions in the protomers of core and holoenzyme

1 reference

7 January 2021

Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA

1 reference

7 January 2021

Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin

1 reference

7 January 2021

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

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7 January 2021

The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins

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7 January 2021

The consequences of expressing hsp70 in Drosophila cells at normal temperatures

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7 January 2021

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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7 January 2021

Preparation of yeast cells for thin-section electron microscopy

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7 January 2021

Immunolocalization of glyceraldehyde-3-phosphate dehydrogenase, hexokinase, and carboxypeptidase Y in yeast cells at the ultrastructural level

1 reference

7 January 2021

Identifiers

DOI

10.1038/372475A0

1 reference

Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

1052934503

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Fatcat ID

release_k347pioyfrg7dlwm7n2yl3ijhe

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/k347pioyfrg7dlwm7n2yl3ijhe

24 November 2022

mapped directly with Wikidata item

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017