These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Journal Abstract Search


269 related items for PubMed ID: 10336454

  • 1.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 2. The X-ray structure of Escherichia coli enoyl reductase with bound NAD+ at 2.1 A resolution.
    Baldock C, Rafferty JB, Stuitje AR, Slabas AR, Rice DW.
    J Mol Biol; 1998 Dec 18; 284(5):1529-46. PubMed ID: 9878369
    [Abstract] [Full Text] [Related]

  • 3.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 4. Binding of the tautomeric forms of isoniazid-NAD adducts to the active site of the Mycobacterium tuberculosis enoyl-ACP reductase (InhA): a theoretical approach.
    Stigliani JL, Arnaud P, Delaine T, Bernardes-Génisson V, Meunier B, Bernadou J.
    J Mol Graph Model; 2008 Nov 18; 27(4):536-45. PubMed ID: 18955002
    [Abstract] [Full Text] [Related]

  • 5.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 6. Crystallographic and pre-steady-state kinetics studies on binding of NADH to wild-type and isoniazid-resistant enoyl-ACP(CoA) reductase enzymes from Mycobacterium tuberculosis.
    Oliveira JS, Pereira JH, Canduri F, Rodrigues NC, de Souza ON, de Azevedo WF, Basso LA, Santos DS.
    J Mol Biol; 2006 Jun 09; 359(3):646-66. PubMed ID: 16647717
    [Abstract] [Full Text] [Related]

  • 7.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 8.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 9. Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis.
    Parikh S, Moynihan DP, Xiao G, Tonge PJ.
    Biochemistry; 1999 Oct 12; 38(41):13623-34. PubMed ID: 10521269
    [Abstract] [Full Text] [Related]

  • 10.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 11.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 12.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 13.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 14.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 15.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 16. InhA, the enoyl-thioester reductase from Mycobacterium tuberculosis forms a covalent adduct during catalysis.
    Vögeli B, Rosenthal RG, Stoffel GMM, Wagner T, Kiefer P, Cortina NS, Shima S, Erb TJ.
    J Biol Chem; 2018 Nov 02; 293(44):17200-17207. PubMed ID: 30217823
    [Abstract] [Full Text] [Related]

  • 17.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 18. Evidence from Raman spectroscopy that InhA, the mycobacterial enoyl reductase, modulates the conformation of the NADH cofactor to promote catalysis.
    Bell AF, Stratton CF, Zhang X, Novichenok P, Jaye AA, Nair PA, Parikh S, Rawat R, Tonge PJ.
    J Am Chem Soc; 2007 May 23; 129(20):6425-31. PubMed ID: 17472376
    [Abstract] [Full Text] [Related]

  • 19. Conformational changes in 2-trans-enoyl-ACP (CoA) reductase (InhA) from M. tuberculosis induced by an inorganic complex: a molecular dynamics simulation study.
    da Costa AL, Pauli I, Dorn M, Schroeder EK, Zhan CG, de Souza ON.
    J Mol Model; 2012 May 23; 18(5):1779-90. PubMed ID: 21833828
    [Abstract] [Full Text] [Related]

  • 20.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]


    Page: [Next] [New Search]
    of 14.