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PUBMED FOR HANDHELDS

Journal Abstract Search


229 related items for PubMed ID: 30770830

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  • 5. SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis.
    Bordes P, Cirinesi AM, Ummels R, Sala A, Sakr S, Bitter W, Genevaux P.
    Proc Natl Acad Sci U S A; 2011 May 17; 108(20):8438-43. PubMed ID: 21536872
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  • 7. TAC from Mycobacterium tuberculosis: a paradigm for stress-responsive toxin-antitoxin systems controlled by SecB-like chaperones.
    Sala A, Calderon V, Bordes P, Genevaux P.
    Cell Stress Chaperones; 2013 Mar 17; 18(2):129-35. PubMed ID: 23264229
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  • 9. SecB, a molecular chaperone with two faces.
    Driessen AJ.
    Trends Microbiol; 2001 May 17; 9(5):193-6. PubMed ID: 11336818
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  • 10. Substrate recognition and cryo-EM structure of the ribosome-bound TAC toxin of Mycobacterium tuberculosis.
    Mansour M, Giudice E, Xu X, Akarsu H, Bordes P, Guillet V, Bigot DJ, Slama N, D'urso G, Chat S, Redder P, Falquet L, Mourey L, Gillet R, Genevaux P.
    Nat Commun; 2022 May 12; 13(1):2641. PubMed ID: 35552387
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  • 12. Multitasking SecB chaperones in bacteria.
    Sala A, Bordes P, Genevaux P.
    Front Microbiol; 2014 May 12; 5():666. PubMed ID: 25538690
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  • 14. A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB.
    Volkert TL, Baleja JD, Kumamoto CA.
    Biochem Biophys Res Commun; 1999 Nov 02; 264(3):949-54. PubMed ID: 10544036
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  • 19. 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 02; 284(23):4066-4082. PubMed ID: 28986943
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  • 20. Structural, functional and biological insights into the role of Mycobacterium tuberculosis VapBC11 toxin-antitoxin system: targeting a tRNase to tackle mycobacterial adaptation.
    Deep A, Tiwari P, Agarwal S, Kaundal S, Kidwai S, Singh R, Thakur KG.
    Nucleic Acids Res; 2018 Nov 30; 46(21):11639-11655. PubMed ID: 30329074
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