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Journal Abstract Search

146 related items for PubMed ID: 4365501

  • 1. The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Mechanism of the amino-acid activation reaction catalyzed by the native and the trypsin-modified enzymes.
    Blanquet S, Fayat G, Waller JP.
    Eur J Biochem; 1974 May 15; 44(2):343-51. PubMed ID: 4365501
    [No Abstract] [Full Text] [Related]

  • 2. Couplings between the sites for methionine and adenosine 5'-triphosphate in the amino acid activation reaction catalyzed by trypsin-modified methionyl-transfer RNA synthetase from Escherichia coli.
    Fayat G, Fromant M, Blanquet S.
    Biochemistry; 1977 May 31; 16(11):2570-9. PubMed ID: 193563
    [No Abstract] [Full Text] [Related]

  • 3. The amino acid activation reaction catalyzed by methionyl-transfer rna synthetase: evidence for synergistic coupling between the sites for methionine adenosine and pyrophosphate.
    Blanquet S, Fayat G, Waller JP.
    J Mol Biol; 1975 May 05; 94(1):1-15. PubMed ID: 167177
    [No Abstract] [Full Text] [Related]

  • 4. The mechanism of action of methionyl-tRNA synthetase. 3. Ion requirements and kinetic parameters of the ATP-PPi exchange and methionine-transfer reactions catalyzed by the native and trypsin-modified enzymes.
    Lawrence F, Blanquet S, Poiret M, Robert-Gero M, Waller JP.
    Eur J Biochem; 1973 Jul 02; 36(1):234-43. PubMed ID: 4581819
    [No Abstract] [Full Text] [Related]

  • 5. Methionyl-tRNA synthetase from Escherichia coli: active stoichiometry and stopped-flow analysis of methionyl adenylate formaiton.
    Hyafil F, Jacques Y, Fayat G, Fromant M, Dessen P, Blanquet S.
    Biochemistry; 1976 Aug 24; 15(17):3678-85. PubMed ID: 182214
    [Abstract] [Full Text] [Related]

  • 6. The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Inhibition by adenosine and 8-aminoadenosine of the amino-acid activation reaction.
    Blanquet S, Fayat G, Poiret M, Waller JP.
    Eur J Biochem; 1975 Feb 21; 51(2):567-71. PubMed ID: 168070
    [Abstract] [Full Text] [Related]

  • 7. The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Equilibrium-dialysis studies on the binding of methionine, ATP and ATP-Mg2+ by the native and trypsin-modified enzymes.
    Fayat G, Waller JP.
    Eur J Biochem; 1974 May 15; 44(2):335-42. PubMed ID: 4600363
    [No Abstract] [Full Text] [Related]

  • 8. Interrelation between transfer RNA and amino-acid-activating sites of methionyl transfer RNA synthetase from Escherichia coli.
    Jacques Y, Blanquet S.
    Eur J Biochem; 1977 Oct 03; 79(2):433-41. PubMed ID: 336359
    [Abstract] [Full Text] [Related]

  • 9. The mechanism of reaction of methionyl-tRNA synthetase from Escherichia coli. Interaction of the enzyme with ligands of the amino-acid-activation reaction.
    Blanquet S, Fayat G, Waller JP, Iwatsubo M.
    Eur J Biochem; 1972 Jan 21; 24(3):461-9. PubMed ID: 4621706
    [No Abstract] [Full Text] [Related]

  • 10. The aminoacylation of transfer ribonucleic acid. Recognition of methionine by Escherichia coli methionyl-transfer ribonucleic acid synthetase.
    Old JM, Jones DS.
    Biochem J; 1977 Aug 01; 165(2):367-73. PubMed ID: 336037
    [Abstract] [Full Text] [Related]

  • 11. Role of the beta-phosphate-gamma-phosphate interchange reaction of adenosine triphosphate in amino acid discrimination by valyl- and methionyl-tRNA synthetases from Escherichia coli.
    Smith LT, Cohn M.
    Biochemistry; 1981 Jan 20; 20(2):385-91. PubMed ID: 6258639
    [No Abstract] [Full Text] [Related]

  • 12. The effect of adenosine analogues on the ATP-pyrophosphate exchange reaction catalysed by methionyl-tRNA synthetase.
    Lawrence F, Shire DJ, Waller JP.
    Eur J Biochem; 1974 Jan 03; 41(1):73-81. PubMed ID: 4361287
    [No Abstract] [Full Text] [Related]

  • 13. Two enzymatically active forms of valyl-tRNA-synthetase from E. coli.
    Paradies HH.
    Biochem Biophys Res Commun; 1975 Jun 16; 64(4):1253-62. PubMed ID: 166643
    [No Abstract] [Full Text] [Related]

  • 14. Isoleucyl transfer ribonucleic acid synthetase from Escherichia coli. Effect of limited cleavage by trypsin on activity and structure.
    Piszkiewicz D, Goitein RD.
    Biochemistry; 1974 Jun 04; 13(12):2505-11. PubMed ID: 4364833
    [No Abstract] [Full Text] [Related]

  • 15. The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. 1. Fluorescence studies on tRNAMet binding as a function of ligands, ions and pH.
    Blanquet S, Iwatsubo M, Waller JP.
    Eur J Biochem; 1973 Jul 02; 36(1):213-26. PubMed ID: 4581817
    [No Abstract] [Full Text] [Related]

  • 16. The catalytic mechanism of glutamyl-tRNA synthetase of Escherichia coli. Evidence for a two-step aminoacylation pathway, and study of the reactivity of the intermediate complex.
    Kern D, Lapointe J.
    Eur J Biochem; 1980 May 02; 106(1):137-50. PubMed ID: 6280993
    [No Abstract] [Full Text] [Related]

  • 17. Proteolytic cleavage of methionyl transfer ribonucleic acid synthetase from Bacillus stearothermophilus: effects on activity and structure.
    Kalogerakos T, Dessen P, Fayat G, Blanquet S.
    Biochemistry; 1980 Aug 05; 19(16):3712-23. PubMed ID: 6250575
    [Abstract] [Full Text] [Related]

  • 18. Affinity labeling of aminoacyl-tRNA synthetases with adenosine triphosphopyridoxal: probing the Lys-Met-Ser-Lys-Ser signature sequence as the ATP-binding site in Escherichia coli methionyl-and valyl-tRNA synthetases.
    Hountondji C, Schmitter JM, Fukui T, Tagaya M, Blanquet S.
    Biochemistry; 1990 Dec 25; 29(51):11266-73. PubMed ID: 2271710
    [Abstract] [Full Text] [Related]

  • 19. ATP-induced specificity of binding of serin tRNAs from rat liver to seryl-tRNA synthetase from yeast.
    Maelicke A, Engel G, Cramer F, Staehelin M.
    Eur J Biochem; 1974 Feb 15; 42(1):311-4. PubMed ID: 4598104
    [No Abstract] [Full Text] [Related]

  • 20. Phenylalanyl-tRNA synthetase from Escherichia coli K10. Synergistic coupling between the sites for binding of L-phenylalanine and ATP.
    Kosakowski HM, Holler E.
    Eur J Biochem; 1973 Oct 05; 38(2):274-82. PubMed ID: 4359386
    [No Abstract] [Full Text] [Related]

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