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Journal Abstract Search

192 related items for PubMed ID: 3518720

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  • 22. Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A.
    Jin L, Stec B, Lipscomb WN, Kantrowitz ER.
    Proteins; 1999 Dec 01; 37(4):729-42. PubMed ID: 10651286
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  • 25. Tryptophan residues at subunit interfaces used as fluorescence probes to investigate homotropic and heterotropic regulation of aspartate transcarbamylase.
    Fetler L, Tauc P, Hervé G, Cunin R, Brochon JC.
    Biochemistry; 2001 Jul 31; 40(30):8773-82. PubMed ID: 11467937
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  • 26. Long-term association of N-(phosphonacetyl)-L-aspartate with bone.
    Ardalan B, Kensler TW, Jayaram HN, Morrison W, Choie DD, Chadwick M, Liss R, Cooney DA.
    Cancer Res; 1981 Jan 31; 41(1):150-6. PubMed ID: 7448755
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  • 29. The catalytic site of Escherichia coli aspartate transcarbamylase: interaction between histidine 134 and the carbonyl group of the substrate carbamyl phosphate.
    Xi XG, Van Vliet F, Ladjimi MM, Cunin R, Hervé G.
    Biochemistry; 1990 Sep 11; 29(36):8491-8. PubMed ID: 2252907
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  • 30. The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity.
    Macol C, Dutta M, Stec B, Tsuruta H, Kantrowitz ER.
    Protein Sci; 1999 Jun 11; 8(6):1305-13. PubMed ID: 10386880
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  • 38. 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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