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253 related items for PubMed ID: 8318885

  • 1. Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains.
    Powers VM, Yang YR, Fogli MJ, Schachman HK.
    Protein Sci; 1993 Jun; 2(6):1001-12. PubMed ID: 8318885
    [Abstract] [Full Text] [Related]

  • 2. In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains.
    Yang YR, Schachman HK.
    Protein Sci; 1993 Jun; 2(6):1013-23. PubMed ID: 8318886
    [Abstract] [Full Text] [Related]

  • 3. Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.
    Zhou BB, Schachman HK.
    Protein Sci; 1993 Jan; 2(1):103-12. PubMed ID: 8443583
    [Abstract] [Full Text] [Related]

  • 4. In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly.
    Zhang P, Schachman HK.
    Protein Sci; 1996 Jul; 5(7):1290-300. PubMed ID: 8819162
    [Abstract] [Full Text] [Related]

  • 5. 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
    [Abstract] [Full Text] [Related]

  • 6. Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains.
    Yang YR, Schachman HK.
    Proc Natl Acad Sci U S A; 1993 Dec 15; 90(24):11980-4. PubMed ID: 8265657
    [Abstract] [Full Text] [Related]

  • 7. A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer.
    Zhou BB, Waldrop GL, Lum L, Schachman HK.
    Protein Sci; 1994 Jun 15; 3(6):967-74. PubMed ID: 8069226
    [Abstract] [Full Text] [Related]

  • 8. Site-specific substitutions of the Tyr-165 residue in the catalytic chain of aspartate transcarbamoylase promotes a T-state preference in the holoenzyme.
    Wales ME, Hoover TA, Wild JR.
    J Biol Chem; 1988 May 05; 263(13):6109-14. PubMed ID: 3283120
    [Abstract] [Full Text] [Related]

  • 9. A cooperative Escherichia coli aspartate transcarbamoylase without regulatory subunits .
    Mendes KR, Kantrowitz ER.
    Biochemistry; 2010 Sep 07; 49(35):7694-703. PubMed ID: 20681545
    [Abstract] [Full Text] [Related]

  • 10. In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.
    Ni X, Schachman HK.
    Protein Sci; 2001 Mar 07; 10(3):519-27. PubMed ID: 11344320
    [Abstract] [Full Text] [Related]

  • 11. Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation.
    Endrizzi JA, Beernink PT, Alber T, Schachman HK.
    Proc Natl Acad Sci U S A; 2000 May 09; 97(10):5077-82. PubMed ID: 10805770
    [Abstract] [Full Text] [Related]

  • 12. Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability.
    Peterson CB, Zhou BB, Hsieh D, Creager AN, Schachman HK.
    Protein Sci; 1994 Jun 09; 3(6):960-6. PubMed ID: 8069225
    [Abstract] [Full Text] [Related]

  • 13. 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 09; 86(9):3094-8. PubMed ID: 2566165
    [Abstract] [Full Text] [Related]

  • 14. Random circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and function.
    Beernink PT, Yang YR, Graf R, King DS, Shah SS, Schachman HK.
    Protein Sci; 2001 Mar 09; 10(3):528-37. PubMed ID: 11344321
    [Abstract] [Full Text] [Related]

  • 15. 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 09; 11(5):1074-81. PubMed ID: 11967364
    [Abstract] [Full Text] [Related]

  • 16. Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.
    Endrizzi JA, Beernink PT.
    Protein Sci; 2017 Nov 09; 26(11):2221-2228. PubMed ID: 28833948
    [Abstract] [Full Text] [Related]

  • 17. Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit.
    Beernink PT, Endrizzi JA, Alber T, Schachman HK.
    Proc Natl Acad Sci U S A; 1999 May 11; 96(10):5388-93. PubMed ID: 10318893
    [Abstract] [Full Text] [Related]

  • 18. 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
    [Abstract] [Full Text] [Related]

  • 19. 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
    [Abstract] [Full Text] [Related]

  • 20. Structural modeling and electrostatic properties of aspartate transcarbamylase from Saccharomyces cerevisiae.
    Villoutreix BO, Spassov VZ, Atanasov BP, Hervé G, Ladjimi MM.
    Proteins; 1994 Jul 01; 19(3):230-43. PubMed ID: 7937736
    [Abstract] [Full Text] [Related]

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