Structural basis for the regulated protease and chaperone function of DegP (Q27650659)

6

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Michael Ehrmann

object named as

Michael Ehrmann

5

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Helen Saibil

4

object named as

Helen R Saibil

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author name string

Justyna Sawa

2

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Eva Schäfer

Folding proteins in fatal ways

3

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language of work or name

English

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publication date

12 June 2008

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published in

Nature

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volume

453

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issue

7197

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page(s)

885-90

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cites work

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

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The HtrA Family of Proteases

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The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1.

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

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Regulation of the E stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress

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

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Overexpression of protease-deficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background

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Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture

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IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA.

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Advances in understanding bacterial outer-membrane biogenesis

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Identification of a Multicomponent Complex Required for Outer Membrane Biogenesis in Escherichia coli

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Regulation of the Escherichia coli sigma-dependent envelope stress response

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A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins.

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SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins

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

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

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PDZ domains of Par-3 as potential phosphoinositide signaling integrators

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Identifiers

DOI

10.1038/NATURE07004

1 reference

Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

1037830652

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Fatcat ID

release_6257434kjvdczpnbsfnc2qwsgi

0 references

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

18496527

1 reference

Consolidated OpenCitations Corpus – April 2017