BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

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]
    of 41.