804 related articles for article (PubMed ID: 25622615)
1. Structure-function analysis of VapB4 antitoxin identifies critical features of a minimal VapC4 toxin-binding module.
Jin G; Pavelka MS; Butler JS
J Bacteriol; 2015 Apr; 197(7):1197-207. PubMed ID: 25622615
[TBL] [Abstract][Full Text] [Related]
2. 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; 188(3):249-58. PubMed ID: 25450593
[TBL] [Abstract][Full Text] [Related]
3. Structural Determinants for Antitoxin Identity and Insulation of Cross Talk between Homologous Toxin-Antitoxin Systems.
Walling LR; Butler JS
J Bacteriol; 2016 Dec; 198(24):3287-3295. PubMed ID: 27672196
[TBL] [Abstract][Full Text] [Related]
4. Homologous VapC Toxins Inhibit Translation and Cell Growth by Sequence-Specific Cleavage of tRNA
Walling LR; Butler JS
J Bacteriol; 2018 Feb; 200(3):. PubMed ID: 29109187
[TBL] [Abstract][Full Text] [Related]
5. 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; 284(23):4066-4082. PubMed ID: 28986943
[TBL] [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; 201(12):. PubMed ID: 30936373
[TBL] [Abstract][Full Text] [Related]
7. Analysis of non-typeable Haemophilous influenzae VapC1 mutations reveals structural features required for toxicity and flexibility in the active site.
Hamilton B; Manzella A; Schmidt K; DiMarco V; Butler JS
PLoS One; 2014; 9(11):e112921. PubMed ID: 25391136
[TBL] [Abstract][Full Text] [Related]
8. Characterization of the Deep-Sea Streptomyces sp. SCSIO 02999 Derived VapC/VapB Toxin-Antitoxin System in Escherichia coli.
Guo Y; Yao J; Sun C; Wen Z; Wang X
Toxins (Basel); 2016 Jul; 8(7):. PubMed ID: 27376329
[TBL] [Abstract][Full Text] [Related]
9. 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; 9(7):e101678. PubMed ID: 25047537
[TBL] [Abstract][Full Text] [Related]
10. The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation.
Robson J; McKenzie JL; Cursons R; Cook GM; Arcus VL
J Mol Biol; 2009 Jul; 390(3):353-67. PubMed ID: 19445953
[TBL] [Abstract][Full Text] [Related]
11. 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; 352(1):69-77. PubMed ID: 24417293
[TBL] [Abstract][Full Text] [Related]
12. tRNA
Chauhan U; Barth VC; Woychik NA
Antimicrob Agents Chemother; 2022 May; 66(5):e0189621. PubMed ID: 35404073
[TBL] [Abstract][Full Text] [Related]
13. 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; 286(6):1174-1190. PubMed ID: 30576065
[TBL] [Abstract][Full Text] [Related]
14. Structural and Functional Study of the
Kang SM; Jin C; Kim DH; Lee Y; Lee BJ
J Med Chem; 2020 Nov; 63(22):13669-13679. PubMed ID: 33146528
[No Abstract] [Full Text] [Related]
15. 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; 6(6):e21738. PubMed ID: 21738782
[TBL] [Abstract][Full Text] [Related]
16. Stay or Go: Sulfolobales Biofilm Dispersal Is Dependent on a Bifunctional VapB Antitoxin.
Lewis AM; Willard DJ; H Manesh MJ; Sivabalasarma S; Albers SV; Kelly RM
mBio; 2023 Apr; 14(2):e0005323. PubMed ID: 37036347
[TBL] [Abstract][Full Text] [Related]
17. 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; 45(14):8564-8580. PubMed ID: 28575388
[TBL] [Abstract][Full Text] [Related]
18. Higher-Order Structure in Bacterial VapBC Toxin-Antitoxin Complexes.
Bendtsen KL; Brodersen DE
Subcell Biochem; 2017; 83():381-412. PubMed ID: 28271484
[TBL] [Abstract][Full Text] [Related]
19. 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; 284(1):276-283. PubMed ID: 18952600
[TBL] [Abstract][Full Text] [Related]
20. Preliminary crystallographic analysis of recombinant VapBC-15 toxin-antitoxin complex from Mycobacterium tuberculosis.
Das U; Kumar N; Gourinath S; Srinivasan A
Acta Crystallogr Sect F Struct Biol Cryst Commun; 2013 Nov; 69(Pt 11):1242-5. PubMed ID: 24192359
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]