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Journal Abstract Search

129 related items for PubMed ID: 33272

  • 1. The stimulation of Escherichia coli aspartate transcarbamylase activity by adenosine triphosphate. Relation with the other regulatory conformational changes; a model.
    Thiry L, Hervé G.
    J Mol Biol; 1978 Nov 15; 125(4):515-34. PubMed ID: 33272
    [No Abstract] [Full Text] [Related]

  • 2. Interactions of ionizable groups in Escherichia coli aspartate transcarbamylase with adenosine and cytidine 5'-triphosphates.
    Burz DS, Allewell NM.
    Biochemistry; 1982 Dec 21; 21(26):6647-55. PubMed ID: 6760892
    [No Abstract] [Full Text] [Related]

  • 3. Intramolecular transmission of the ATP regulatory signal in Escherichia coli aspartate transcarbamylase: specific involvement of a clustered set of amino acid interactions at an interface between regulatory and catalytic subunits.
    De Staercke C, Van Vliet F, Xi XG, Rani CS, Ladjimi M, Jacobs A, Triniolles F, Hervé G, Cunin R.
    J Mol Biol; 1995 Feb 10; 246(1):132-43. PubMed ID: 7853393
    [Abstract] [Full Text] [Related]

  • 4. Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase.
    Newton CJ, Kantrowitz ER.
    Biochemistry; 1990 Feb 13; 29(6):1444-51. PubMed ID: 2185840
    [Abstract] [Full Text] [Related]

  • 5. A kinetic model of cooperativity in aspartate transcarbamylase.
    Dembo M, Rubinow SI.
    Biophys J; 1977 Jun 13; 18(3):245-67. PubMed ID: 329911
    [Abstract] [Full Text] [Related]

  • 6. Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions.
    Silver RS, Daigneault JP, Teague PD, Kantrowitz ER.
    J Mol Biol; 1983 Aug 25; 168(4):729-45. PubMed ID: 6350607
    [Abstract] [Full Text] [Related]

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  • 9. An aspartate transcarbamylase lacking catalytic subunit interactions. II. Regulatory subunits are responsible for the lack of co-operative interactions between catalytic sites. Drastic feedback inhibition does not restore these interactions.
    Kerbiriou D, Hervé G.
    J Mol Biol; 1973 Aug 25; 78(4):687-702. PubMed ID: 4587135
    [No Abstract] [Full Text] [Related]

  • 10. Bohr effect in Escherichia coli aspartate transcarbamylase. Linkages between substrate binding, proton binding, and conformational transitions.
    Allwell NM, Hofmann GE, Zaug A, Lennick M.
    Biochemistry; 1979 Jul 10; 18(14):3008-15. PubMed ID: 37893
    [No Abstract] [Full Text] [Related]

  • 11. Three-dimensional structures at 5.5 A resolution and regulatory processes in aspartate transcarbamylase from E. coli.
    Lipscomb WN, Evans DR, Edwards BF, Warren SG, Pastra-Landis S, Wiley DC.
    J Supramol Struct; 1974 Jul 10; 2(2-4):82-98. PubMed ID: 4612257
    [No Abstract] [Full Text] [Related]

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  • 13. Coupling of homotropic and heterotropic interactions in Escherichia coli aspartate transcarbamylase.
    Tauc P, Leconte C, Kerbiriou D, Thiry L, Hervé G.
    J Mol Biol; 1982 Feb 25; 155(2):155-68. PubMed ID: 7042988
    [No Abstract] [Full Text] [Related]

  • 14. Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association.
    Lennick M, Allewell NM.
    Proc Natl Acad Sci U S A; 1981 Nov 25; 78(11):6759-63. PubMed ID: 7031660
    [Abstract] [Full Text] [Related]

  • 15. Lysine-60 in the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for the discrimination between CTP and ATP.
    Zhang Y, Kantrowitz ER.
    Biochemistry; 1989 Sep 05; 28(18):7313-8. PubMed ID: 2510822
    [Abstract] [Full Text] [Related]

  • 16. Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution.
    Stevens RC, Gouaux JE, Lipscomb WN.
    Biochemistry; 1990 Aug 21; 29(33):7691-701. PubMed ID: 2271528
    [Abstract] [Full Text] [Related]

  • 17. The allosteric activator Mg-ATP modifies the quaternary structure of the R-state of Escherichia coli aspartate transcarbamylase without altering the T<-->R equilibrium.
    Fetler L, Vachette P.
    J Mol Biol; 2001 Jun 08; 309(3):817-32. PubMed ID: 11397099
    [Abstract] [Full Text] [Related]

  • 18. Solvent perturbation of the allosteric regulation of aspartate transcarbamylase.
    LiCata VJ, Allewell NM.
    Biochim Biophys Acta; 1998 May 19; 1384(2):306-14. PubMed ID: 9659392
    [Abstract] [Full Text] [Related]

  • 19. Effectors of Escherichia coli aspartate transcarbamoylase differentially perturb aspartate binding rather than the T-R transition.
    Hsuanyu YC, Wedler FC.
    J Biol Chem; 1988 Mar 25; 263(9):4172-81. PubMed ID: 3279030
    [Abstract] [Full Text] [Related]

  • 20. The activation of Escherichia coli aspartate transcarbamylase by ATP. Specific involvement of helix H2' at the hydrophobic interface between the two domains of the regulatory chains.
    Xi XG, De Staercke C, Van Vliet F, Triniolles F, Jacobs A, Stas PP, Ladjimi MM, Simon V, Cunin R, Hervé G.
    J Mol Biol; 1994 Sep 16; 242(2):139-49. PubMed ID: 8089837
    [Abstract] [Full Text] [Related]

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