scholarly article | Q13442814 |
P50 | author | Meera Unnikrishnan | Q63860319 |
Eric Rubin | Q29887908 | ||
P2093 | author name string | Alfred L Goldberg | |
Olga Kandror | |||
Ravikiran M Raju | |||
Vidhya Krishnamoorthy | |||
Daniel H F Rubin | |||
Tatos N Akopian | |||
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ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage | Q28486713 | ||
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The proteasome of Mycobacterium tuberculosis is required for resistance to nitric oxide | Q28487442 | ||
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Protein degradation and protection against misfolded or damaged proteins | Q29618400 | ||
Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin). | Q30408156 | ||
Controlled degradation by ClpXP protease tunes the levels of the excision repair protein UvrA to the extent of DNA damage | Q33841737 | ||
Prokaryotic ubiquitin-like protein provides a two-part degron to Mycobacterium proteasome substrates | Q33876875 | ||
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Stress-induced ClpP serine protease of Listeria monocytogenes is essential for induction of listeriolysin O-dependent protective immunity. | Q34008601 | ||
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Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La. | Q34336717 | ||
The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease | Q34615400 | ||
Depletion of antibiotic targets has widely varying effects on growth | Q34651942 | ||
Broad yet high substrate specificity: the challenge of AAA+ proteins | Q35705299 | ||
Lon and Clp family proteases and chaperones share homologous substrate-recognition domains | Q36378628 | ||
Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria | Q36736444 | ||
Proteases in bacterial pathogenesis | Q37602770 | ||
Effects of production of abnormal proteins on the rate of killing of Escherichia coli by streptomycin | Q39815632 | ||
Identifying vulnerable pathways in Mycobacterium tuberculosis by using a knockdown approach | Q41849520 | ||
The natural product cyclomarin kills Mycobacterium tuberculosis by targeting the ClpC1 subunit of the caseinolytic protease | Q42740574 | ||
Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. | Q44563531 | ||
Beta-lactones as specific inhibitors of ClpP attenuate the production of extracellular virulence factors of Staphylococcus aureus | Q46321774 | ||
Mycobacterial recombineering | Q47814886 | ||
The ClpP serine protease is essential for the intracellular parasitism and virulence of Listeria monocytogenes | Q47870369 | ||
ClpP participates in the degradation of misfolded protein in Lactococcus lactis | Q47988611 | ||
P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
P6216 | copyright status | copyrighted | Q50423863 |
P433 | issue | 2 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Mycobacterium tuberculosis | Q130971 |
P304 | page(s) | e1002511 | |
P577 | publication date | 2012-02-16 | |
P1433 | published in | PLOS Pathogens | Q283209 |
P1476 | title | Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection | |
P478 | volume | 8 |
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