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Journal Abstract Search

343 related items for PubMed ID: 3066911

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  • 4. Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study.
    Ladner JE, Kitchell JP, Honzatko RB, Ke HM, Volz KW, Kalb AJ, Ladner RC, Lipscomb WN.
    Proc Natl Acad Sci U S A; 1982 May; 79(10):3125-8. PubMed ID: 6954462
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  • 7. 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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  • 10. Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.
    Zhou BB, Schachman HK.
    Protein Sci; 1993 Jan 08; 2(1):103-12. PubMed ID: 8443583
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  • 12. A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition.
    Stieglitz KA, Pastra-Landis SC, Xia J, Tsuruta H, Kantrowitz ER.
    J Mol Biol; 2005 Jun 03; 349(2):413-23. PubMed ID: 15890205
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  • 13. 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 03; 11(5):1074-81. PubMed ID: 11967364
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  • 15. Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.
    Eisenstein E, Markby DW, Schachman HK.
    Proc Natl Acad Sci U S A; 1989 May 03; 86(9):3094-8. PubMed ID: 2566165
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  • 16. Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate.
    Van Boxstael S, Cunin R, Khan S, Maes D.
    J Mol Biol; 2003 Feb 07; 326(1):203-16. PubMed ID: 12547202
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  • 18. Kinetics of the interaction of N-(phosphonacetyl)-L-aspartate with the catalytic subunit of aspartate transcarbamoylase. A slow conformational change subsequent to binding.
    Cohen RE, Schachman HK.
    J Biol Chem; 1986 Feb 25; 261(6):2623-31. PubMed ID: 3949739
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  • 20. 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 25; 1(11):1435-46. PubMed ID: 1303763
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