PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits (Q74037500)

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8 November 2019

title

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

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8 November 2019

4

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8 November 2019

author name string

I Levchenko

1

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8 November 2019

C K Smith

2

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8 November 2019

N P Walsh

3

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8 November 2019

T A Baker

5

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8 November 2019

language of work or name

English

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publication date

1 December 1997

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8 November 2019

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8 November 2019

volume

91

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8 November 2019

issue

7

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8 November 2019

page(s)

939-947

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Division of labor among monomers within the Mu transposase tetramer

8 November 2019

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Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ

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Protein-protein interactions: PDZ domain networks

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Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

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Regulation of SOS mutagenesis by proteolysis

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Frameshift mutations in the bacteriophage Mu repressor gene can confer a trans-dominant virulent phenotype to the phage

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Peptide-surface association: the case of PDZ and PTB domains

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Binding of neuroligins to PSD-95

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Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA

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

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Bacteriophage Mu repressor as a target for the Escherichia coli ATP-dependent Clp Protease

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Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli

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7 January 2021

Disassembly of the Mu transposase tetramer by the ClpX chaperone

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ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway.

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Disassembly of the Bacteriophage Mu Transposase for the Initiation of Mu DNA Replication

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7 January 2021

Hsp104 is a highly conserved protein with two essential nucleotide-binding sites

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7 January 2021

Protein disaggregation mediated by heat-shock protein Hsp104.

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7 January 2021

Evidence for PDZ domains in bacteria, yeast, and plants

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7 January 2021

Interaction of Hsp70 chaperones with substrates

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7 January 2021

PDZ domains bind carboxy-terminal sequences of target proteins

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A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade

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7 January 2021

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Identifiers

DOI

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8 November 2019

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