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Journal Abstract Search

289 related items for PubMed ID: 10386880

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  • 3. Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure.
    Tauc P, Keiser RT, Kantrowitz ER, Vachette P.
    Protein Sci; 1994 Nov; 3(11):1998-2004. PubMed ID: 7703847
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  • 4. The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure.
    Baker DP, Fetler L, Vachette P, Kantrowitz ER.
    Protein Sci; 1996 Nov; 5(11):2276-86. PubMed ID: 8931146
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  • 5. 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; 4(2):258-67. PubMed ID: 7757014
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  • 6. Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase.
    Newton CJ, Stevens RC, Kantrowitz ER.
    Biochemistry; 1992 Mar 24; 31(11):3026-32. PubMed ID: 1550826
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  • 7. Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase.
    Fetler L, Tauc P, Baker DP, Macol CP, Kantrowitz ER, Vachette P.
    Protein Sci; 2002 May 24; 11(5):1074-81. PubMed ID: 11967364
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  • 8. Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study.
    Stebbins JW, Robertson DE, Roberts MF, Stevens RC, Lipscomb WN, Kantrowitz ER.
    Protein Sci; 1992 Nov 24; 1(11):1435-46. PubMed ID: 1303763
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  • 12. Function of serine-171 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamoylase.
    Dembowski NJ, Newton CJ, Kantrowitz ER.
    Biochemistry; 1990 Apr 17; 29(15):3716-23. PubMed ID: 2111165
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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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  • 17. Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylase.
    Stebbins JW, Zhang Y, Kantrowitz ER.
    Biochemistry; 1990 Apr 24; 29(16):3821-7. PubMed ID: 2191720
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  • 18. Glutamic acid 86 is important for positioning the 80's loop and arginine 54 at the active site of Escherichia coli aspartate transcarbamoylase and for the structural stabilization of the C1-C2 interface.
    Baker DP, Stebbins JW, DeSena E, Kantrowitz ER.
    J Biol Chem; 1994 Oct 07; 269(40):24608-14. PubMed ID: 7929132
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  • 19. 240s loop interactions stabilize the T state of Escherichia coli aspartate transcarbamoylase.
    Alam N, Stieglitz KA, Caban MD, Gourinath S, Tsuruta H, Kantrowitz ER.
    J Biol Chem; 2004 May 28; 279(22):23302-10. PubMed ID: 15014067
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