Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins. (Q36954523)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18697939 AND SRC:MED&resulttype=core&format=json

12 January 2020

title

Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins (English)

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12 January 2020

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4

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12 January 2020

Sui Senfang

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12 January 2020

author name string

Jiansen Jiang

1

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12 January 2020

Xuefeng Zhang

2

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12 January 2020

Yong Chen

3

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12 January 2020

Z Hong Zhou

5

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12 January 2020

Zengyi Chang

6

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12 January 2020

language of work or name

English

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publication date

12 August 2008

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Proceedings of the National Academy of Sciences of the United States of America

12 January 2020

published in

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12 January 2020

volume

105

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12 January 2020

issue

33

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12 January 2020

page(s)

11939-11944

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Structural basis for the regulated protease and chaperone function of DegP

12 January 2020

cites work

1 reference

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Allosteric activation of DegS, a stress sensor PDZ protease

29 September 2017

1 reference

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Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli

29 September 2017

1 reference

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Role of the PDZ domains in Escherichia coli DegP protein

29 September 2017

1 reference

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The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity.

29 September 2017

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Protein misfolding and human disease

29 September 2017

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29 September 2017

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Quality control in the endoplasmic reticulum protein factory

29 September 2017

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Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima

29 September 2017

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The HtrA Family of Proteases

29 September 2017

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Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi

29 September 2017

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Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine

29 September 2017

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Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli

29 September 2017

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EMAN: semiautomated software for high-resolution single-particle reconstructions

29 September 2017

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Review and update of casein chemistry

29 September 2017

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

29 September 2017

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Families of serine peptidases.

29 September 2017

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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

29 September 2017

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Isolation and characterization of protease Do from Escherichia coli, a large serine protease containing multiple subunits

29 September 2017

1 reference

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Sequence analysis and regulation of the htrA gene of Escherichia coli: a sigma 32-independent mechanism of heat-inducible transcription

29 September 2017

1 reference

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29 September 2017

The heat-shock proteins

1 reference

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Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature

29 September 2017

1 reference

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Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures

29 September 2017

1 reference

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The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase

29 September 2017

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Protease Do is essential for survival of Escherichia coli at high temperatures: its identity with the htrA gene product

29 September 2017

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Proteases and their targets in Escherichia coli

29 September 2017

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The N-terminal region of HtrA heat shock protease from Escherichia coli is essential for stabilization of HtrA primary structure and maintaining of its oligomeric structure

29 September 2017

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The mechanism of temperature-induced bacterial HtrA activation

27 June 2018

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Allosteric activation of HtrA protease DegP by stress signals during bacterial protein quality control

4 September 2018

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Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock.

4 September 2018

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Structural analysis of DegS, a stress sensor of the bacterial periplasm

4 September 2018

1 reference

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Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease

4 September 2018

1 reference

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A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.

4 September 2018

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Multi-resolution contour-based fitting of macromolecular structures

4 September 2018

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PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits

4 December 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/18697939

12 December 2020

inferred from PubMed ID database lookup

PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/18697939

12 December 2020

inferred from PubMed ID database lookup

Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein in Escherichia coli

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/18697939

12 December 2020

inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.0805464105

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18697939 AND SRC:MED&resulttype=core&format=json

12 January 2020

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release_vbonizfeafcezii2eatow5622u

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Fatcat

https://api.fatcat.wiki/v0/release/vbonizfeafcezii2eatow5622u

24 November 2022

mapped directly with Wikidata item

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12 January 2020

PubMed publication ID

18697939

1 reference