Turned on for degradation: ATPase-independent degradation by ClpP. - Test2 - elhamkhani - TriplyDB

Turned on for degradation: ATPase-independent degradation by ClpP.

Turned on for degradation: ATPase-independent degradation by ClpP.

http://www.wikidata.org/entity/Q36206215

about

Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.Structural Switching of Staphylococcus aureus Clp Protease: A KEY TO UNDERSTANDING PROTEASE DYNAMICS Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad N-Terminal-oriented proteogenomics of the marine bacterium roseobacter denitrificans Och114 using N-Succinimidyloxycarbonylmethyl)tris(2,4,6-trimethoxyphenyl)phosphonium bromide (TMPP) labeling and diagonal chromatography.The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans Binding of the ClpA unfoldase opens the axial gate of ClpP peptidase Assembly and proteolytic processing of mycobacterial ClpP1 and ClpP2.ClpXP, an ATP-powered unfolding and protein-degradation machine Structure and Functional Properties of the Active Form of the Proteolytic Complex, ClpP1P2, from Mycobacterium tuberculosis.Degradation of SsrA-tagged proteins in streptococci.mazEF-mediated programmed cell death in bacteria: "what is this?".Control of substrate gating and translocation into ClpP by channel residues and ClpX binding.Structural determinants stabilizing the axial channel of ClpP for substrate translocation.

P2860

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P2860

Turned on for degradation: ATPase-independent degradation by ClpP.

http://www.wikidata.org/entity/Q36206215

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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name

Turned on for degradation: ATPase-independent degradation by ClpP.

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Turned on for degradation: ATPase-independent degradation by ClpP.

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Turned on for degradation: ATPase-independent degradation by ClpP.

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Turned on for degradation: ATPase-independent degradation by ClpP.

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Turned on for degradation: ATPase-independent degradation by ClpP.

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J.JSB.2008.10.005

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Journal of Structural Biology

P1476

Turned on for degradation: ATPase-independent degradation by ClpP.

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P2093

John M Flanagan

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

Kathleen Griffin

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

Maria C Bewley

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Vito Graziano

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

P2860

Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis

AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes

Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli

Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

ClpP hydrolyzes a protein substrate processively in the absence of the ClpA ATPase: mechanistic studies of ATP-independent proteolysis.

The AAA team: related ATPases with diverse functions.

Control of peptide product sizes by the energy-dependent protease ClpAP.

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118-125

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10.1016/J.JSB.2008.10.005

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2

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165

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2008-11-11T00:00:00Z

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19038348

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3433037

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