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- W2099403391 abstract "Significance The proteasome of Mycobacterium tuberculosis is required to cause lethal infections and is thus a potential drug target. Bacterial proteasomes degrade proteins modified by pupylation, but evidence suggests that the M. tuberculosis proteasome possesses additional functions. In this work, we describe a degradation pathway in M. tuberculosis controlled by a previously unidentified proteasomal cofactor, Rv3780. Rv3780 enhanced the ATP-independent proteasomal degradation of peptides and proteins and was required to maintain levels of a unique set of putative proteasome substrates. Importantly, an Rv3780 mutant was attenuated for growth in mice. To our knowledge, these studies show for the first time that an ATP-independent proteasomal-degradation pathway plays a role in the physiology of an important human pathogen." @default.
- W2099403391 created "2016-06-24" @default.
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- W2099403391 date "2015-03-23" @default.
- W2099403391 modified "2023-10-16" @default.
- W2099403391 title "An adenosine triphosphate-independent proteasome activator contributes to the virulence of <i>Mycobacterium tuberculosis</i>" @default.
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- W2099403391 doi "https://doi.org/10.1073/pnas.1423319112" @default.
- W2099403391 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4394314" @default.
- W2099403391 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25831519" @default.
- W2099403391 hasPublicationYear "2015" @default.
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