Communication between ClpX and ClpP during substrate processing and degradation. - Wikidata - awgldk - TriplyDB

Communication between ClpX and ClpP during substrate processing and degradation.

Communication between ClpX and ClpP during substrate processing and degradation.

http://www.wikidata.org/entity/Q44830501

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Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.Insights into Structural Network Responsible for Oligomerization and Activity of Bacterial Virulence Regulator Caseinolytic Protease P (ClpP) Protein Structural Dynamics of the MecA-ClpC Complex: A TYPE II AAA+ PROTEIN UNFOLDING MACHINE Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.The ClpP N-terminus coordinates substrate access with protease active site reactivity.Synchrotron protein footprinting supports substrate translocation by ClpA via ATP-induced movements of the D2 loop.ClpXP, an ATP-powered unfolding and protein-degradation machine Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine.ClpXP proteases positively regulate alginate overexpression and mucoid conversion in Pseudomonas aeruginosa Measuring chromosome dynamics on different time scales using resolvases with varying half-lives.Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery.AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.The molecular architecture of the metalloprotease FtsH.A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases.The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease.Distinct quaternary structures of the AAA+ Lon protease control substrate degradation.Computer simulation of assembly and co-operativity of hexameric AAA ATPases The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes.Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1 Sculpting the proteome with AAA(+) proteases and disassembly machines.Turned on for degradation: ATPase-independent degradation by ClpP.Insights into ClpXP proteolysis: heterooligomerization and partial deactivation enhance chaperone affinity and substrate turnover in Listeria monocytogenes.Identification of potential mitochondrial CLPXP protease interactors and substrates suggests its central role in energy metabolism.Structure and Functional Properties of the Active Form of the Proteolytic Complex, ClpP1P2, from Mycobacterium tuberculosis.Sclerotiamide: The First Non-Peptide-Based Natural Product Activator of Bacterial Caseinolytic Protease P.ClpX(P) generates mechanical force to unfold and translocate its protein substrates Binding of MG132 or deletion of the Thr active sites in HslV subunits increases the affinity of HslV protease for HslU ATPase and makes this interaction nucleotide-independent.Examination of a Structural Model of Peptidomimicry by Cyclic Acyldepsipeptide Antibiotics in Their Interaction with the ClpP Peptidase ATP-dependent proteases differ substantially in their ability to unfold globular proteins Mini review: ATP-dependent proteases in bacteria.Two isoforms of Clp peptidase in Pseudomonas aeruginosa control distinct aspects of cellular physiology.The development of small-molecule modulators for ClpP protease activity.Restriction of the conformational dynamics of the cyclic acyldepsipeptide antibiotics improves their antibacterial activity.Small-molecule control of protein degradation using split adaptors.Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease.ATP binding to neighbouring subunits and intersubunit allosteric coupling underlie proteasomal ATPase function.Control of substrate gating and translocation into ClpP by channel residues and ClpX binding.Highly Dynamic Interactions Maintain Kinetic Stability of the ClpXP Protease During the ATP-Fueled Mechanical Cycle.A simple fragment of cyclic acyldepsipeptides is necessary and sufficient for ClpP activation and antibacterial activity

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P2860

Communication between ClpX and ClpP during substrate processing and degradation.

http://www.wikidata.org/entity/Q44830501

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年學術文章

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name

Communication between ClpX and ClpP during substrate processing and degradation.

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Communication between ClpX and ClpP during substrate processing and degradation.

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type

label

Communication between ClpX and ClpP during substrate processing and degradation.

@en

Communication between ClpX and ClpP during substrate processing and degradation.

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prefLabel

Communication between ClpX and ClpP during substrate processing and degradation.

@en

Communication between ClpX and ClpP during substrate processing and degradation.

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Nature Structural & Molecular Biology

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Communication between ClpX and ClpP during substrate processing and degradation.

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P2093

Greg L Hersch

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

Robert T Sauer

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Shilpa A Joshi

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Tania A Baker

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P2860

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

The structures of HsIU and the ATP-dependent protease HsIU-HsIV

A gated channel into the proteasome core particle

Structural basis for the activation of 20S proteasomes by 11S regulators

Crystal and solution structures of an HslUV protease-chaperone complex

Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism

Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU

Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU

Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease

Crystal structure of ClpX molecular chaperone from Helicobacter pylori

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10.1038/NSMB752

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5

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11

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