(Q37142807)

English

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

scientific article published on 06 October 2008

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

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 (English)

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

5

object named as

Chin Ha Chung

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

author name string

Eunyong Park

1

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Jung Wook Lee

2

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Soo Hyun Eom

3

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Jae Hong Seol

4

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

language of work or name

0 references

publication date

6 October 2008

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

283

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

48

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

33258-33266

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

Proteasome inhibitors: from research tools to drug candidates

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

Crystal and solution structures of an HslUV protease-chaperone complex

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

A gated channel into the proteasome core particle

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

The AAA team: related ATPases with diverse functions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

Crystal structure of heat shock locus V (HslV) from Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

Translational efficiency of the Escherichia coli adenylate cyclase gene: mutating the UUG initiation codon to GUG or AUG results in increased gene expression

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

6 September 2017

Asymmetric nucleotide transactions of the HslUV protease.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

27 June 2018

Mutagenesis of two N-terminal Thr and five Ser residues in HslV, the proteolytic component of the ATP-dependent HslVU protease.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

27 June 2018

The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

27 June 2018

Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

3 September 2018

Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

3 September 2018

Communication between ClpX and ClpP during substrate processing and degradation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

3 September 2018

The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

3 September 2018

Autocatalytic processing of the 20S proteasome

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662256

3 September 2018

Coupled assay of Na+,K+-ATPase activity

1 reference

https://pubmed.ncbi.nlm.nih.gov/18838376

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/18838376

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae

1 reference

https://pubmed.ncbi.nlm.nih.gov/18838376

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis

1 reference

https://pubmed.ncbi.nlm.nih.gov/18838376

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M805411200

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

ResearchGate publication ID

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