Turned on for degradation: ATPase-independent degradation by ClpP. (Q36206215)

12 August 2017

Turned on for degradation: ATPase-independent degradation by ClpP. (English)

1 reference

12 August 2017

Maria C Bewley

1

1 reference

12 August 2017

Vito Graziano

series ordinal

2

1 reference

12 August 2017

Kathleen Griffin

series ordinal

3

1 reference

12 August 2017

John M Flanagan

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4

1 reference

12 August 2017

11 November 2008

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Journal of Structural Biology

12 August 2017

1 reference

12 August 2017

165

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12 August 2017

2

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12 August 2017

118-125

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

12 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

The ClpP N-terminus coordinates substrate access with protease active site reactivity

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP.

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Translocation pathway of protein substrates in ClpAP protease.

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

ClpA mediates directional translocation of substrate proteins into the ClpP protease

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

The AAA team: related ATPases with diverse functions

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

A molecular chaperone, ClpA, functions like DnaK and DnaJ.

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Clp P represents a unique family of serine proteases.

2 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation

2 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Communication between ClpX and ClpP during substrate processing and degradation

22 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation

22 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone

22 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP.

22 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Dynamics of substrate denaturation and translocation by the ClpXP degradation machine

22 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis.

22 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES.

22 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetradecamer with an axial pore.

22 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433037

Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask

22 September 2018

1 reference

12 December 2020

ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease

1 reference

12 December 2020

Substrate recognition by the ClpA chaperone component of ClpAP protease

1 reference

12 December 2020

Processing of X-ray diffraction data collected in oscillation mode

1 reference

12 December 2020

Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP

1 reference

12 December 2020

10.1016/J.JSB.2008.10.005

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DOI

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12 August 2017

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12 August 2017

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