BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

110 related articles for article (PubMed ID: 14678787)

  • 1. Inversion of the allosteric response of Escherichia coli glucosamine-6-P deaminase to N-acetylglucosamine 6-P, by single amino acid replacements.
    Cisneros DA; Montero-Morán GM; Lara-González S; Calcagno ML
    Arch Biochem Biophys; 2004 Jan; 421(1):77-84. PubMed ID: 14678787
    [TBL] [Abstract][Full Text] [Related]  

  • 2. On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase.
    Montero-Morán GM; Lara-González S; Alvarez-Añorve LI; Plumbridge JA; Calcagno ML
    Biochemistry; 2001 Aug; 40(34):10187-96. PubMed ID: 11513596
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Why does Escherichia coli grow more slowly on glucosamine than on N-acetylglucosamine? Effects of enzyme levels and allosteric activation of GlcN6P deaminase (NagB) on growth rates.
    Alvarez-Añorve LI; Calcagno ML; Plumbridge J
    J Bacteriol; 2005 May; 187(9):2974-82. PubMed ID: 15838023
    [TBL] [Abstract][Full Text] [Related]  

  • 4. On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase.
    Bustos-Jaimes I; Sosa-Peinado A; Rudiño-Piñera E; Horjales E; Calcagno ML
    J Mol Biol; 2002 May; 319(1):183-9. PubMed ID: 12051945
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Evidence for two different mechanisms triggering the change in quaternary structure of the allosteric enzyme, glucosamine-6-phosphate deaminase.
    Bustos-Jaimes I; Ramírez-Costa M; De Anda-Aguilar L; Hinojosa-Ocaña P; Calcagno ML
    Biochemistry; 2005 Feb; 44(4):1127-35. PubMed ID: 15667206
    [TBL] [Abstract][Full Text] [Related]  

  • 6. The tertiary origin of the allosteric activation of E. coli glucosamine-6-phosphate deaminase studied by sol-gel nanoencapsulation of its T conformer.
    Zonszein S; Álvarez-Añorve LI; Vázquez-Núñez RJ; Calcagno ML
    PLoS One; 2014; 9(5):e96536. PubMed ID: 24787711
    [TBL] [Abstract][Full Text] [Related]  

  • 7. On the functional role of Arg172 in substrate binding and allosteric transition in Escherichia coli glucosamine-6-phosphate deaminase.
    Lucumí-Moreno A; Calcagno ML
    Arch Biochem Biophys; 2005 Oct; 442(1):41-8. PubMed ID: 16168949
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Tyr254 hydroxyl group acts as a two-way switch mechanism in the coupling of heterotropic and homotropic effects in Escherichia coli glucosamine-6-phosphate deaminase.
    Montero-Morán GM; Horjales E; Calcagno ML; Altamirano MM
    Biochemistry; 1998 May; 37(21):7844-9. PubMed ID: 9601045
    [TBL] [Abstract][Full Text] [Related]  

  • 9. On the role of the N-terminal group in the allosteric function of glucosamine-6-phosphate deaminase from Escherichia coli.
    Lara-González S; Dixon HB; Mendoza-Hernández G; Altamirano MM; Calcagno ML
    J Mol Biol; 2000 Aug; 301(1):219-27. PubMed ID: 10926504
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Asymmetric allosteric activation of Escherichia coli glucosamine-6-phosphate deaminase produced by replacements of Tyr 121.
    Altamirano MM; Plumbridge JA; Horjales E; Calcagno ML
    Biochemistry; 1995 May; 34(18):6074-82. PubMed ID: 7742311
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Allosteric kinetics of the isoform 1 of human glucosamine-6-phosphate deaminase.
    Alvarez-Añorve LI; Alonzo DA; Mora-Lugo R; Lara-González S; Bustos-Jaimes I; Plumbridge J; Calcagno ML
    Biochim Biophys Acta; 2011 Dec; 1814(12):1846-53. PubMed ID: 21807125
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Allosteric transition and substrate binding are entropy-driven in glucosamine-6-phosphate deaminase from Escherichia coli.
    Bustos-Jaimes I; Calcagno ML
    Arch Biochem Biophys; 2001 Oct; 394(2):156-60. PubMed ID: 11594728
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Allosteric Activation of Escherichia coli Glucosamine-6-Phosphate Deaminase (NagB) In Vivo Justified by Intracellular Amino Sugar Metabolite Concentrations.
    Álvarez-Añorve LI; Gaugué I; Link H; Marcos-Viquez J; Díaz-Jiménez DM; Zonszein S; Bustos-Jaimes I; Schmitz-Afonso I; Calcagno ML; Plumbridge J
    J Bacteriol; 2016 Jun; 198(11):1610-1620. PubMed ID: 27002132
    [TBL] [Abstract][Full Text] [Related]  

  • 14. The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution.
    Horjales E; Altamirano MM; Calcagno ML; Garratt RC; Oliva G
    Structure; 1999 May; 7(5):527-37. PubMed ID: 10378272
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Allosteric regulation of glucosamine-6-phosphate deaminase (NagB) and growth of Escherichia coli on glucosamine.
    Alvarez-Añorve LI; Bustos-Jaimes I; Calcagno ML; Plumbridge J
    J Bacteriol; 2009 Oct; 191(20):6401-7. PubMed ID: 19700525
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate deaminase of Escherichia coli induced by active or allosteric site ligands at steady state.
    Sosa-Peinado A; González-Andrade M
    Biochemistry; 2005 Nov; 44(46):15083-92. PubMed ID: 16285712
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Glucosamine-6-phosphate deaminase from beef kidney is an allosteric system of the V-type.
    Lara-Lemus R; Calcagno ML
    Biochim Biophys Acta; 1998 Oct; 1388(1):1-9. PubMed ID: 9774701
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase.
    Rudiño-Piñera E; Morales-Arrieta S; Rojas-Trejo SP; Horjales E
    Acta Crystallogr D Biol Crystallogr; 2002 Jan; 58(Pt 1):10-20. PubMed ID: 11752775
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study.
    Arreola R; Valderrama B; Morante ML; Horjales E
    FEBS Lett; 2003 Sep; 551(1-3):63-70. PubMed ID: 12965206
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Identification of two cysteine residues forming a pair of vicinal thiols in glucosamine-6-phosphate deaminase from Escherichia coli and a study of their functional role by site-directed mutagenesis.
    Altamirano MM; Plumbridge JA; Calcagno ML
    Biochemistry; 1992 Feb; 31(4):1153-8. PubMed ID: 1734962
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 6.