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Journal Abstract Search

239 related items for PubMed ID: 8104480

  • 21. 240s loop interactions stabilize the T state of Escherichia coli aspartate transcarbamoylase.
    Alam N, Stieglitz KA, Caban MD, Gourinath S, Tsuruta H, Kantrowitz ER.
    J Biol Chem; 2004 May 28; 279(22):23302-10. PubMed ID: 15014067
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  • 22. Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure.
    Tauc P, Keiser RT, Kantrowitz ER, Vachette P.
    Protein Sci; 1994 Nov 28; 3(11):1998-2004. PubMed ID: 7703847
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  • 23. 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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  • 24. Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism.
    Lee BH, Ley BW, Kantrowitz ER, O'Leary MH, Wedler FC.
    J Biol Chem; 1995 Jun 30; 270(26):15620-7. PubMed ID: 7797560
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  • 26. Function of serine-171 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamoylase.
    Dembowski NJ, Newton CJ, Kantrowitz ER.
    Biochemistry; 1990 Apr 17; 29(15):3716-23. PubMed ID: 2111165
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  • 27. 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. Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylase.
    Stebbins JW, Zhang Y, Kantrowitz ER.
    Biochemistry; 1990 Apr 24; 29(16):3821-7. PubMed ID: 2191720
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  • 33. Site-directed alterations to the geometry of the aspartate transcarbamoylase zinc domain: selective alteration to regulation by heterotropic ligands, isoelectric point, and stability in urea.
    Strang CJ, Wales ME, Brown DM, Wild JR.
    Biochemistry; 1993 Apr 27; 32(16):4156-67. PubMed ID: 8476846
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  • 34. 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 27; 11(5):1074-81. PubMed ID: 11967364
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  • 35. 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
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  • 36. Domain bridging interactions. A necessary contribution to the function and structure of Escherichia coli aspartate transcarbamoylase.
    Sakash JB, Williams MK, Tsuruta H, Kantrowitz ER.
    J Biol Chem; 2001 Jul 13; 276(28):26441-7. PubMed ID: 11352920
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  • 37. 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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  • 38. 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 03; 8(6):1305-13. PubMed ID: 10386880
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  • 39. 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
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  • 40. Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation.
    Van Vliet F, Xi XG, De Staercke C, de Wannemaeker B, Jacobs A, Cherfils J, Ladjimi MM, Hervé G, Cunin R.
    Proc Natl Acad Sci U S A; 1991 Oct 15; 88(20):9180-3. PubMed ID: 1924381
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