BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

135 related articles for article (PubMed ID: 6370303)

  • 1. Folding of aspartokinase-homoserine dehydrogenase I is dominated by tertiary interactions.
    Müller K; Garel JR
    Biochemistry; 1984 Feb; 23(4):655-60. PubMed ID: 6370303
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Stepwise inactivation of Escherichia coli aspartokinase-homoserine dehydrogenase I.
    Müller K; Garel JR
    Biochemistry; 1984 Feb; 23(4):651-4. PubMed ID: 6370302
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Independent folding regions in aspartokinase-homoserine dehydrogenase.
    Dautry-Varsat A; Garel JR
    Biochemistry; 1981 Mar; 20(5):1396-401. PubMed ID: 7225337
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Mechanism of renaturation of a large protein, aspartokinase-homoserine dehydrogenase.
    Vaucheret H; Signon L; Le Bras G; Garel JR
    Biochemistry; 1987 May; 26(10):2785-90. PubMed ID: 3606993
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Characterization of proteolysis fragments of aspartokinase I: homoserine dehydrogenase I. Fluorescence and circular dichroism studies.
    McMahon PL; Takahashi M
    J Biol Chem; 1983 Nov; 258(21):12934-9. PubMed ID: 6355098
    [TBL] [Abstract][Full Text] [Related]  

  • 6. A triglobular model for the polypeptide chain of aspartokinase I-homoserine dehydrogenase I of Escherichia coli.
    Fazel A; Müller K; Le Bras G; Garel JR; Véron M; Cohen GN
    Biochemistry; 1983 Jan; 22(1):158-65. PubMed ID: 6338915
    [TBL] [Abstract][Full Text] [Related]  

  • 7. E. coli aspartokinase II-homoserine dehydrogenase II polypeptide chain has a triglobular structure.
    Belfaiza J; Fazel A; Müller K; Cohen GN
    Biochem Biophys Res Commun; 1984 Aug; 123(1):16-20. PubMed ID: 6383377
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Proteolysis of the bifunctional methionine-repressible aspartokinase II-homoserine dehydrogenase II of Escherichia coli K12. Production of an active homoserine dehydrogenase fragment.
    Dautry-Varsat A; Cohen GN
    J Biol Chem; 1977 Nov; 252(21):7685-9. PubMed ID: 334767
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Reversible dissociation of aspartokinase I/homoserine dehydrogenase I from Escherichia coli K 12. The active species is the tetramer.
    Veron M; Guillou Y; Fazel A; Cohen GN
    Eur J Biochem; 1985 Sep; 151(3):521-4. PubMed ID: 3896789
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Isolation of the aspartokinase domain of bifunctional aspartokinase I-homoserine dehydrogenase I from E.coli K12.
    Veron M; Guillou Y; Cohen GN
    FEBS Lett; 1985 Feb; 181(2):381-4. PubMed ID: 2982665
    [TBL] [Abstract][Full Text] [Related]  

  • 11. The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Site of limited proteolytic cleavage by subtilisin.
    Briley PA; Sibilli L; Chalvignac MA; Cossart P; Le Bras G; De Wolf A; Cohen GN
    J Biol Chem; 1978 Dec; 253(24):8867-71. PubMed ID: 363710
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Guanidine hydrochloride induced unfolding of the alpha subunit of tryptophan synthase and of the two alpha proteolytic fragments: evidence for stepwise unfolding of the two alpha domains.
    Miles EW; Yutani K; Ogasahara K
    Biochemistry; 1982 May; 21(11):2586-92. PubMed ID: 7046790
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Subunit structure of the methionine-repressible aspartokinase II--homoserine dehydrogenase II from Escherichia coli K12.
    Dautry-Varsat A; Sibilli-Weill L; Cohen GN
    Eur J Biochem; 1977 Jun; 76(1):1-6. PubMed ID: 328280
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Two regions of the bifunctional protein aspartokinase I- homoserine dehydrogenase I are connected by a short hinge.
    Sibilli L; Le Bras G; Le Bras G; Cohen GN
    J Biol Chem; 1981 Oct; 256(20):10228-30. PubMed ID: 7026556
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Sequential folding of a bifunctional allosteric protein.
    Garel JR; Dautry-Varsat A
    Proc Natl Acad Sci U S A; 1980 Jun; 77(6):3379-83. PubMed ID: 6774337
    [TBL] [Abstract][Full Text] [Related]  

  • 16. The guanidine-induced conformational changes of the chaperonin GroEL from Escherichia coli. Evidence for the existence of an unfolding intermediate state.
    Mizobata T; Kawata Y
    Biochim Biophys Acta; 1994 Nov; 1209(1):83-8. PubMed ID: 7947986
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Cobalt(III) labeled aspartokinase-homoserine dehydrogenase of Escherichia coli.
    Ryzewski C; Takahashi MT
    Biochemistry; 1975 Oct; 14(20):4482-6. PubMed ID: 1100105
    [TBL] [Abstract][Full Text] [Related]  

  • 18. A hybrid proteolytic fragment of Escherichia coli aspartokinase I-homoserine dehydrogenase I. Structure, inhibition pattern, dissociation properties, and generation of two homodimers.
    Fazel A; Guillou Y; Cohen GN
    J Biol Chem; 1983 Nov; 258(22):13570-4. PubMed ID: 6315703
    [TBL] [Abstract][Full Text] [Related]  

  • 19. A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydrogenase of Escherichia coli.
    Sun ZY; Pratt EA; Simplaceanu V; Ho C
    Biochemistry; 1996 Dec; 35(51):16502-9. PubMed ID: 8987983
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Kinetic and spectroscopic effects upon binding of serine and threonine.
    Costrejean JM; Truffa-Bachi P
    J Biol Chem; 1977 Aug; 252(15):5332-6. PubMed ID: 328500
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 7.