Molecular chaperones: clamps for the Clps? (Q47890014)

6 February 2018

review article

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title

Molecular chaperones: clamps for the Clps? (English)

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6 February 2018

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Feng HP

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6 February 2018

Gierasch LM

series ordinal

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6 February 2018

language of work or name

English

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publication date

1 June 1998

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6 February 2018

published in

Current Biology

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6 February 2018

volume

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6 February 2018

issue

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6 February 2018

page(s)

R464-7

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6 February 2018

HSP100/Clp proteins: a common mechanism explains diverse functions

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

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Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition

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Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY.

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Mechanism of protein remodeling by ClpA chaperone

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The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

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Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

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

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7 January 2021

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Identifiers

DOI

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6 February 2018

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6 February 2018