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Journal Abstract Search

289 related items for PubMed ID: 10386880

  • 21. Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-L-aspartate?
    Foote J, Schachman HK.
    J Mol Biol; 1985 Nov 05; 186(1):175-84. PubMed ID: 3908690
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  • 25. A cis-proline to alanine mutant of E. coli aspartate transcarbamoylase: kinetic studies and three-dimensional crystal structures.
    Jin L, Stec B, Kantrowitz ER.
    Biochemistry; 2000 Jul 11; 39(27):8058-66. PubMed ID: 10891088
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  • 27. Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase.
    Tauc P, Vachette P, Middleton SA, Kantrowitz ER.
    J Mol Biol; 1990 Jul 05; 214(1):327-35. PubMed ID: 1973463
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  • 28. Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase.
    Newton CJ, Kantrowitz ER.
    Biochemistry; 1990 Feb 13; 29(6):1444-51. PubMed ID: 2185840
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  • 31. Importance of domain closure for the catalysis and regulation of Escherichia coli aspartate transcarbamoylase.
    Macol CP, Tsuruta H, Kantrowitz ER.
    J Biol Chem; 2002 Jul 26; 277(30):26852-7. PubMed ID: 12016227
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  • 32. Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase.
    Robey EA, Wente SR, Markby DW, Flint A, Yang YR, Schachman HK.
    Proc Natl Acad Sci U S A; 1986 Aug 26; 83(16):5934-8. PubMed ID: 3526345
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  • 33. 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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  • 34. Threonine 82 in the regulatory chain is important for nucleotide affinity and for the allosteric stabilization of Escherichia coli aspartate transcarbamoylase.
    Williams MK, Kantrowitz ER.
    Biochim Biophys Acta; 1998 Dec 08; 1429(1):249-58. PubMed ID: 9920401
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  • 36. A fluorescent probe-labeled Escherichia coli aspartate transcarbamoylase that monitors the allosteric conformational state.
    West JM, Tsuruta H, Kantrowitz ER.
    J Biol Chem; 2004 Jan 09; 279(2):945-51. PubMed ID: 14581486
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  • 37. Stabilization of the R allosteric structure of Escherichia coli aspartate transcarbamoylase by disulfide bond formation.
    West JM, Tsuruta H, Kantrowitz ER.
    J Biol Chem; 2002 Dec 06; 277(49):47300-4. PubMed ID: 12359710
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  • 38. Discrimination between nucleotide effector responses of aspartate transcarbamoylase due to a single site substitution in the allosteric binding site.
    Corder TS, Wild JR.
    J Biol Chem; 1989 May 05; 264(13):7425-30. PubMed ID: 2651439
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  • 39. Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions.
    Peterson CB, Schachman HK.
    J Biol Chem; 1992 Feb 05; 267(4):2443-50. PubMed ID: 1733944
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