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Journal Abstract Search

125 related items for PubMed ID: 2285793

  • 1. Differential scanning calorimetric studies of E. coli aspartate transcarbamylase. III. The denaturational thermodynamics of the holoenzyme with single-site mutations in the catalytic chain.
    Burz DS, Allewell NM, Ghosaini L, Hu CQ, Sturtevant JM.
    Biophys Chem; 1990 Aug 31; 37(1-3):31-41. PubMed ID: 2285793
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  • 2. Effects of assembly and mutations outside the active site on the functional pH dependence of Escherichia coli aspartate transcarbamylase.
    Yuan X, LiCata VJ, Allewell NM.
    J Biol Chem; 1996 Jan 19; 271(3):1285-94. PubMed ID: 8576114
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  • 3. Kinetic consequences of site-specific mutation of Glu-239----Gln in E. coli aspartate transcarbamylase: comparison with catalytic subunits and Phe-240 mutant enzyme.
    Hsuanyu Y, Wedler FC, Middleton SA, Kantrowitz ER.
    Biochim Biophys Acta; 1989 Mar 16; 995(1):54-8. PubMed ID: 2647154
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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 16; 4(2):258-67. PubMed ID: 7757014
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  • 6. Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase.
    Sakash JB, Chan RS, Tsuruta H, Kantrowitz ER.
    J Biol Chem; 2000 Jan 14; 275(2):752-8. PubMed ID: 10625604
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  • 11. Differential scanning calorimetric study of the thermal denaturation of aspartate transcarbamoylase of Escherichia coli.
    Edge V, Allewell NM, Sturtevant JM.
    Biochemistry; 1988 Oct 18; 27(21):8081-7. PubMed ID: 3069128
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  • 12. Negative complementation in aspartate transcarbamylase. Analysis of hybrid enzyme molecules containing different arrangements of polypeptide chains from wild-type and inactive mutant catalytic subunits.
    Eisenstein E, Han MS, Woo TS, Ritchey JM, Gibbons I, Yang YR, Schachman HK.
    J Biol Chem; 1992 Nov 05; 267(31):22148-55. PubMed ID: 1429567
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  • 14. 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 05; 86(9):3094-8. PubMed ID: 2566165
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  • 15. 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 05; 5(11):2276-86. PubMed ID: 8931146
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  • 16. 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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  • 17. The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain.
    Newton CJ, Kantrowitz ER.
    Proc Natl Acad Sci U S A; 1990 Mar 07; 87(6):2309-13. PubMed ID: 2179954
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  • 18. Primary structure of murine major histocompatibility complex alloantigens: amino acid sequence of the amino-terminal one hundred and seventy-three residues of the H-2Kb glycoprotein.
    Uehara H, Ewenstein BM, Martinko JM, Nathenson SG, Coligan JE, Kindt TJ.
    Biochemistry; 1980 Jan 22; 19(2):306-15. PubMed ID: 6986168
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  • 19. 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 22; 1(11):1435-46. PubMed ID: 1303763
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  • 20. Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylase.
    Middleton SA, Kantrowitz ER.
    Biochemistry; 1988 Nov 15; 27(23):8653-60. PubMed ID: 3146350
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