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Journal Abstract Search
254 related items for PubMed ID: 18952600
1. Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. Miallau L, Faller M, Chiang J, Arbing M, Guo F, Cascio D, Eisenberg D. J Biol Chem; 2009 Jan 02; 284(1):276-283. PubMed ID: 18952600 [Abstract] [Full Text] [Related]
2. Functional details of the Mycobacterium tuberculosis VapBC26 toxin-antitoxin system based on a structural study: insights into unique binding and antibiotic peptides. Kang SM, Kim DH, Lee KY, Park SJ, Yoon HJ, Lee SJ, Im H, Lee BJ. Nucleic Acids Res; 2017 Aug 21; 45(14):8564-8580. PubMed ID: 28575388 [Abstract] [Full Text] [Related]
3. The crystal structure of the Rv0301-Rv0300 VapBC-3 toxin-antitoxin complex from M. tuberculosis reveals a Mg²⁺ ion in the active site and a putative RNA-binding site. Min AB, Miallau L, Sawaya MR, Habel J, Cascio D, Eisenberg D. Protein Sci; 2012 Nov 21; 21(11):1754-67. PubMed ID: 23011806 [Abstract] [Full Text] [Related]
4. Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis reveals a two-metal ion dependent PIN-domain ribonuclease and a variable mode of toxin-antitoxin assembly. Das U, Pogenberg V, Subhramanyam UK, Wilmanns M, Gourinath S, Srinivasan A. J Struct Biol; 2014 Dec 21; 188(3):249-58. PubMed ID: 25450593 [Abstract] [Full Text] [Related]
5. Structural characterization of VapB46 antitoxin from Mycobacterium tuberculosis: insights into VapB46-DNA binding. Roy M, Kundu A, Bhunia A, Das Gupta S, De S, Das AK. FEBS J; 2019 Mar 21; 286(6):1174-1190. PubMed ID: 30576065 [Abstract] [Full Text] [Related]
6. Crystal Structure of VapBC-1 from Nontypeable Haemophilus influenzae and the Effect of PIN Domain Mutations on Survival during Infection. Molinaro AL, Kashipathy MM, Lovell S, Battaile KP, Coussens NP, Shen M, Daines DA. J Bacteriol; 2019 Jun 15; 201(12):. PubMed ID: 30936373 [Abstract] [Full Text] [Related]
8. Crystal structure of Mycobacterium tuberculosis VapC20 toxin and its interactions with cognate antitoxin, VapB20, suggest a model for toxin-antitoxin assembly. Deep A, Kaundal S, Agarwal S, Singh R, Thakur KG. FEBS J; 2017 Dec 15; 284(23):4066-4082. PubMed ID: 28986943 [Abstract] [Full Text] [Related]
9. The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array. Arcus VL, McKenzie JL, Robson J, Cook GM. Protein Eng Des Sel; 2011 Jan 15; 24(1-2):33-40. PubMed ID: 21036780 [Abstract] [Full Text] [Related]
10. VapC from the leptospiral VapBC toxin-antitoxin module displays ribonuclease activity on the initiator tRNA. Lopes AP, Lopes LM, Fraga TR, Chura-Chambi RM, Sanson AL, Cheng E, Nakajima E, Morganti L, Martins EA. PLoS One; 2014 Jan 15; 9(7):e101678. PubMed ID: 25047537 [Abstract] [Full Text] [Related]
13. Toxin-antitoxin vapBC locus participates in formation of the dormant state in Mycobacterium smegmatis. Demidenok OI, Kaprelyants AS, Goncharenko AV. FEMS Microbiol Lett; 2014 Mar 15; 352(1):69-77. PubMed ID: 24417293 [Abstract] [Full Text] [Related]
15. Phosphorylation of VapB antitoxins affects intermolecular interactions to regulate VapC toxin activity in Mycobacterium tuberculosis. Malakar B, Barth VC, Puffal J, Woychik NA, Husson RN. J Bacteriol; 2024 Oct 24; 206(10):e0023324. PubMed ID: 39315797 [Abstract] [Full Text] [Related]
16. VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate VapB antitoxins. Ahidjo BA, Kuhnert D, McKenzie JL, Machowski EE, Gordhan BG, Arcus V, Abrahams GL, Mizrahi V. PLoS One; 2011 Oct 24; 6(6):e21738. PubMed ID: 21738782 [Abstract] [Full Text] [Related]
17. Structural and Functional Study of the Klebsiella pneumoniae VapBC Toxin-Antitoxin System, Including the Development of an Inhibitor That Activates VapC. Kang SM, Jin C, Kim DH, Lee Y, Lee BJ. J Med Chem; 2020 Nov 25; 63(22):13669-13679. PubMed ID: 33146528 [Abstract] [Full Text] [Related]