(Q28480875)

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Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection

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23 January 2020

Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection (English)

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23 January 2020

Mycobacterium tuberculosis

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Meera Unnikrishnan

2

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23 January 2020

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Eric J Rubin

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23 January 2020

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Ravikiran M Raju

1

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23 January 2020

Daniel H F Rubin

3

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23 January 2020

Vidhya Krishnamoorthy

4

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23 January 2020

Olga Kandror

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23 January 2020

Tatos N Akopian

6

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23 January 2020

Alfred L Goldberg

7

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23 January 2020

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publication date

16 February 2012

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23 January 2020

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23 January 2020

8

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23 January 2020

2

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23 January 2020

e1002511

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23 January 2020

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Creative Commons Attribution 4.0 International

16 February 2012

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April 2022 Public Data File from Crossref

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ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage

1 reference

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Characterization of a Clp protease gene regulator and the reaeration response in Mycobacterium tuberculosis

1 reference

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Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis

1 reference

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Mycobacterium tuberculosis ftsH expression in response to stress and viability

1 reference

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Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1

1 reference

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19 March 2017

The proteasome of Mycobacterium tuberculosis is required for resistance to nitric oxide

1 reference

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19 March 2017

Genes required for mycobacterial growth defined by high density mutagenesis

1 reference

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19 March 2017

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

1 reference

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19 March 2017

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

1 reference

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19 March 2017

Cell cycle control by an essential bacterial two-component signal transduction protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

7 April 2017

Protein degradation and protection against misfolded or damaged proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

7 April 2017

Depletion of antibiotic targets has widely varying effects on growth

1 reference

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29 September 2017

Emerging principles in protease-based drug discovery

1 reference

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29 September 2017

Prokaryotic ubiquitin-like protein provides a two-part degron to Mycobacterium proteasome substrates

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

Proteases in bacterial pathogenesis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

Controlled degradation by ClpXP protease tunes the levels of the excision repair protein UvrA to the extent of DNA damage

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

Broad yet high substrate specificity: the challenge of AAA+ proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

Mode of action of chloramphenicol. III. Action of chloramphenicol on bacterial energy metabolism

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

Stress-induced ClpP serine protease of Listeria monocytogenes is essential for induction of listeriolysin O-dependent protective immunity.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

Lon and Clp family proteases and chaperones share homologous substrate-recognition domains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

An essential protease involved in bacterial cell-cycle control

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin).

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

A multiple-component, ATP-dependent protease from Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3280978

29 September 2017

Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La.

1 reference

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29 September 2017

Effects of production of abnormal proteins on the rate of killing of Escherichia coli by streptomycin

1 reference

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29 September 2017

Identifying vulnerable pathways in Mycobacterium tuberculosis by using a knockdown approach

1 reference

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Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine.

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PPAT.1002511

21 January 2018

Cytoplasmic degradation of ssrA-tagged proteins.

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PPAT.1002511

21 January 2018

The ClpP serine protease is essential for the intracellular parasitism and virulence of Listeria monocytogenes.

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PPAT.1002511

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Mycobacterial recombineering.

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PPAT.1002511

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ClpP participates in the degradation of misfolded protein in Lactococcus lactis.

1 reference

https://api.crossref.org/works/10.1371%2FJOURNAL.PPAT.1002511

21 January 2018

The natural product cyclomarin kills Mycobacterium tuberculosis by targeting the ClpC1 subunit of the caseinolytic protease

1 reference

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21 January 2018

Beta-lactones as specific inhibitors of ClpP attenuate the production of extracellular virulence factors of Staphylococcus aureus

1 reference

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21 January 2018

Identifiers

10.1371/JOURNAL.PPAT.1002511

2 references

Consolidated OpenCitations Corpus – April 2017

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23 January 2020

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1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Europe PubMed Central

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23 January 2020

1 reference

Europe PubMed Central

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23 January 2020

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