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412 related items for PubMed ID: 10600394

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  • 2. Allosteric regulation in a family of enterobacterial aspartate transcarbamylases: intramolecular transmission of regulatory signals in chimeric enzymes.
    Cunin R, Wales ME, Van Vliet F, De Staercke C, Scapozza L, Rani CS, Wild JR.
    J Mol Biol; 1996 Sep 20; 262(2):258-69. PubMed ID: 8831792
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  • 3. Divergent allosteric patterns verify the regulatory paradigm for aspartate transcarbamylase.
    Wales ME, Madison LL, Glaser SS, Wild JR.
    J Mol Biol; 1999 Dec 17; 294(5):1387-400. PubMed ID: 10600393
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  • 11. 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
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  • 12. Comparative modeling of mammalian aspartate transcarbamylase.
    Scully JL, Evans DR.
    Proteins; 1991 Jun 08; 9(3):191-206. PubMed ID: 2006137
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  • 13. Allosteric regulation in Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase revisited: association of concerted homotropic cooperative interactions and local heterotropic effects.
    Tricot C, Villeret V, Sainz G, Dideberg O, Stalon V.
    J Mol Biol; 1998 Oct 30; 283(3):695-704. PubMed ID: 9784377
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  • 14. T-state inhibitors of E. coli aspartate transcarbamoylase that prevent the allosteric transition.
    Heng S, Stieglitz KA, Eldo J, Xia J, Cardia JP, Kantrowitz ER.
    Biochemistry; 2006 Aug 22; 45(33):10062-71. PubMed ID: 16906764
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  • 16. Conversion of the allosteric regulatory patterns of aspartate transcarbamoylase by exchange of a single beta-strand between diverged regulatory chains.
    Liu L, Wales ME, Wild JR.
    Biochemistry; 1997 Mar 18; 36(11):3126-32. PubMed ID: 9115988
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  • 17. In vivo formation of hybrid aspartate transcarbamoylases from native subunits of divergent members of the family Enterobacteriaceae.
    Foltermann KF, Beck DA, Wild JR.
    J Bacteriol; 1986 Jul 18; 167(1):285-90. PubMed ID: 3722124
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  • 19. Discrimination between nucleotide effector responses of aspartate transcarbamoylase due to a single site substitution in the allosteric binding site.
    Corder TS, Wild JR.
    J Biol Chem; 1989 May 05; 264(13):7425-30. PubMed ID: 2651439
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  • 20. Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylase.
    Baker DP, Fetler L, Keiser RT, Vachette P, Kantrowitz ER.
    Protein Sci; 1995 Feb 05; 4(2):258-67. PubMed ID: 7757014
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