Results 161 to 170 of about 1,206 (173)
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Journal of Structural Biology, 2014
Although PIN (PilT N-terminal)-domain proteins are known to have ribonuclease activity, their specific mechanism of action remains unknown. VapCs form a family of ribonucleases that possess a PIN-domain assembly and are known as toxins. The activities of VapCs are impaired by VapB antitoxins.
Uddipan Das +5 more
semanticscholar +4 more sources
Although PIN (PilT N-terminal)-domain proteins are known to have ribonuclease activity, their specific mechanism of action remains unknown. VapCs form a family of ribonucleases that possess a PIN-domain assembly and are known as toxins. The activities of VapCs are impaired by VapB antitoxins.
Uddipan Das +5 more
semanticscholar +4 more sources
Journal of Molecular Biology, 2009
The largest family of bacterial toxin-antitoxin (TA) modules is formed by the vapBC operons, and these are grouped together by virtue of their toxin components belonging to the PilT N-terminal domain family of proteins that are thought to function as ribonucleases.
Jennifer R Robson +4 more
semanticscholar +4 more sources
The largest family of bacterial toxin-antitoxin (TA) modules is formed by the vapBC operons, and these are grouped together by virtue of their toxin components belonging to the PilT N-terminal domain family of proteins that are thought to function as ribonucleases.
Jennifer R Robson +4 more
semanticscholar +4 more sources
Protein science : a publication of the Protein Society, 2013
VapBC pairs account for 45 out of 88 identified toxin-antitoxin (TA) pairs in the Mycobacterium tuberculosis (Mtb) H37Rv genome. A working model suggests that under times of stress, antitoxin molecules are degraded, releasing the toxins to slow the metabolism of the cell, which in the case of VapC toxins is via their RNase activity.
Andrew B, Min +5 more
openaire +1 more source
VapBC pairs account for 45 out of 88 identified toxin-antitoxin (TA) pairs in the Mycobacterium tuberculosis (Mtb) H37Rv genome. A working model suggests that under times of stress, antitoxin molecules are degraded, releasing the toxins to slow the metabolism of the cell, which in the case of VapC toxins is via their RNase activity.
Andrew B, Min +5 more
openaire +1 more source
Structure of VapBC from Shigella sonnei
, 2020S. Lea, S. Hollingshead
semanticscholar +1 more source
Crystal structure of DNA bound VapBC from Salmonella typhimurium
, 2020D. Park, B. Lee
semanticscholar +1 more source
2.2 A resolution structure of VapBC-1 from nontypeable Haemophilus influenzae
, 2019S. Lovell +4 more
semanticscholar +1 more source
VapBC from Mycobacterium tuberculosis
, 2017S. M. Kang, D. H. Kim, H. Yoon, B. Lee
semanticscholar +1 more source
, 2008