BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

253 related articles for article (PubMed ID: 22366418)

  • 1. A VapBC toxin-antitoxin module is a posttranscriptional regulator of metabolic flux in mycobacteria.
    McKenzie JL; Robson J; Berney M; Smith TC; Ruthe A; Gardner PP; Arcus VL; Cook GM
    J Bacteriol; 2012 May; 194(9):2189-204. PubMed ID: 22366418
    [TBL] [Abstract][Full Text] [Related]  

  • 2. 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]  

  • 3. 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]  

  • 4. 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]  

  • 5. Toxin-antitoxin systems of Mycobacterium smegmatis are essential for cell survival.
    Frampton R; Aggio RB; Villas-Bôas SG; Arcus VL; Cook GM
    J Biol Chem; 2012 Feb; 287(8):5340-56. PubMed ID: 22199354
    [TBL] [Abstract][Full Text] [Related]  

  • 6. 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]  

  • 7. Growth and translation inhibition through sequence-specific RNA binding by Mycobacterium tuberculosis VapC toxin.
    Sharp JD; Cruz JW; Raman S; Inouye M; Husson RN; Woychik NA
    J Biol Chem; 2012 Apr; 287(16):12835-47. PubMed ID: 22354968
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Regulation of the vapBC-1 toxin-antitoxin locus in nontypeable Haemophilus influenzae.
    Cline SD; Saleem S; Daines DA
    PLoS One; 2012; 7(3):e32199. PubMed ID: 22427824
    [TBL] [Abstract][Full Text] [Related]  

  • 9. 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]  

  • 10. The mycobacterial PhoH2 proteins are type II toxin antitoxins coupled to RNA helicase domains.
    Andrews ES; Arcus VL
    Tuberculosis (Edinb); 2015 Jul; 95(4):385-94. PubMed ID: 25999286
    [TBL] [Abstract][Full Text] [Related]  

  • 11. 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]  

  • 12. 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]  

  • 13. 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]  

  • 14. [VapC toxin inhibition as a method for prevention of the formation of resting forms of mycobacteria].
    Demidenok OI; Shumkov MS; Goncharenko AV
    Prikl Biokhim Mikrobiol; 2016; 52(6):579-83. PubMed ID: 29513477
    [TBL] [Abstract][Full Text] [Related]  

  • 15. 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]  

  • 16. 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]  

  • 17. Crystal structure of the toxin Msmeg_6760, the structural homolog of Mycobacterium tuberculosis Rv2035, a novel type II toxin involved in the hypoxic response.
    Bajaj RA; Arbing MA; Shin A; Cascio D; Miallau L
    Acta Crystallogr F Struct Biol Commun; 2016 Dec; 72(Pt 12):863-869. PubMed ID: 27917833
    [TBL] [Abstract][Full Text] [Related]  

  • 18. 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(11):1754-67. PubMed ID: 23011806
    [TBL] [Abstract][Full Text] [Related]  

  • 19. VapC proteins from Mycobacterium tuberculosis share ribonuclease sequence specificity but differ in regulation and toxicity.
    Sharrock A; Ruthe A; Andrews ESV; Arcus VA; Hicks JL
    PLoS One; 2018; 13(8):e0203412. PubMed ID: 30169502
    [TBL] [Abstract][Full Text] [Related]  

  • 20. tRNA
    Chauhan U; Barth VC; Woychik NA
    Antimicrob Agents Chemother; 2022 May; 66(5):e0189621. PubMed ID: 35404073
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 13.