These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

156 related articles for article (PubMed ID: 2285780)

  • 1. Amino acid substitutions which stabilize aspartate transcarbamoylase in the R state disrupt both homotropic and heterotropic effects.
    Newell JO; Schachman HK
    Biophys Chem; 1990 Aug; 37(1-3):183-96. PubMed ID: 2285780
    [TBL] [Abstract][Full Text] [Related]  

  • 2. 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; 86(9):3094-8. PubMed ID: 2566165
    [TBL] [Abstract][Full Text] [Related]  

  • 3. 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; 275(2):752-8. PubMed ID: 10625604
    [TBL] [Abstract][Full Text] [Related]  

  • 4. 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; 349(2):413-23. PubMed ID: 15890205
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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; 5(11):2276-86. PubMed ID: 8931146
    [TBL] [Abstract][Full Text] [Related]  

  • 6. 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
    [TBL] [Abstract][Full Text] [Related]  

  • 7. 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; 4(2):258-67. PubMed ID: 7757014
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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; 3(11):1998-2004. PubMed ID: 7703847
    [TBL] [Abstract][Full Text] [Related]  

  • 9. 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; 97(10):5077-82. PubMed ID: 10805770
    [TBL] [Abstract][Full Text] [Related]  

  • 10. A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylase.
    Middleton SA; Stebbins JW; Kantrowitz ER
    Biochemistry; 1989 Feb; 28(4):1617-26. PubMed ID: 2655696
    [TBL] [Abstract][Full Text] [Related]  

  • 11. 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; 1(11):1435-46. PubMed ID: 1303763
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase.
    Eisenstein E; Markby DW; Schachman HK
    Biochemistry; 1990 Apr; 29(15):3724-31. PubMed ID: 2187530
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments.
    Werner WE; Schachman HK
    J Mol Biol; 1989 Mar; 206(1):221-30. PubMed ID: 2649684
    [TBL] [Abstract][Full Text] [Related]  

  • 14. 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; 8(6):1305-13. PubMed ID: 10386880
    [TBL] [Abstract][Full Text] [Related]  

  • 15. 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; 263(13):6109-14. PubMed ID: 3283120
    [TBL] [Abstract][Full Text] [Related]  

  • 16. 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; 32(16):4156-67. PubMed ID: 8476846
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Cooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamoylase and the heterotropic effects of ATP and CTP.
    Newell JO; Markby DW; Schachman HK
    J Biol Chem; 1989 Feb; 264(5):2476-81. PubMed ID: 2644262
    [TBL] [Abstract][Full Text] [Related]  

  • 18. T-state inhibitors of E. coli aspartate transcarbamoylase that prevent the allosteric transition.
    Heng S; Stieglitz KA; Eldo J; Xia J; Cardia JP; Kantrowitz ER
    Biochemistry; 2006 Aug; 45(33):10062-71. PubMed ID: 16906764
    [TBL] [Abstract][Full Text] [Related]  

  • 19. 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; 279(22):23302-10. PubMed ID: 15014067
    [TBL] [Abstract][Full Text] [Related]  

  • 20. 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; 87(6):2309-13. PubMed ID: 2179954
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 8.