Both ATPase domains of ClpA are critical for processing of stable protein structures. - Wikidata - wikimedia - TriplyDB

Both ATPase domains of ClpA are critical for processing of stable protein structures.

Both ATPase domains of ClpA are critical for processing of stable protein structures.

http://www.wikidata.org/entity/Q41932006

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The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits.The ClpS Adaptor Mediates Staged Delivery of N-End Rule Substrates to the AAA+ ClpAP Protease Fundamental Characteristics of AAA+ Protein Family Structure and Function Mechanochemical basis of protein degradation by a double-ring AAA+ machine The complexities of p97 function in health and disease Assaying the kinetics of protein denaturation catalyzed by AAA+ unfolding machines and proteases The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1 ClpP-deletion impairs the virulence of Legionella pneumophila and the optimal translocation of effector proteins Functional analysis of conserved cis- and trans-elements in the Hsp104 protein disaggregating machine E. coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP.ATPγS competes with ATP for binding at Domain 1 but not Domain 2 during ClpA catalyzed polypeptide translocation.Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Mini review: ATP-dependent proteases in bacteria.Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.Molecular Mechanism of Substrate Processing by the Cdc48 ATPase Complex.

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P2860

Both ATPase domains of ClpA are critical for processing of stable protein structures.

http://www.wikidata.org/entity/Q41932006

description

2009 nî lūn-bûn

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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2009年论文

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2009年论文

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name

Both ATPase domains of ClpA are critical for processing of stable protein structures.

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type

label

Both ATPase domains of ClpA are critical for processing of stable protein structures.

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prefLabel

Both ATPase domains of ClpA are critical for processing of stable protein structures.

@en

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JBC.M109.022319

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Journal of Biological Chemistry

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Both ATPase domains of ClpA are critical for processing of stable protein structures.

@en

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Hannes Mutschler

http://www.w3.org/2001/XMLSchema#string

Wolfgang Kress

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P2860

The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system

The N-end rule: functions, mysteries, uses

Structural basis of chaperone function and pilus biogenesis

X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli

Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA

Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA

Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation

Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation

Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation

The Molecular Basis of N-End Rule Recognition

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31441-31452

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10.1074/JBC.M109.022319

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45

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284

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Eilika Weber-Ban

Hannes Mutschler

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2009-09-02T00:00:00Z

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26786006

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2781540

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