Rezultati pretrage - Jean‐Pierre Samama

  • Prikaz rezultata 1 – 12 od 12
Detaljiziraj rezultate
  1. 1
    Site-directed mutagenesis at the active site of Escherichia coli TEM-1 beta-lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis.

    Site-directed mutagenesis at the active site of Escherichia coli TEM-1 beta-lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in cata... od Myriam Delaire, Roger Labia, Jean‐Pierre Samama, Jean‐Michel Masson

    Izdano 1992
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  2. 2
    Crystal structure of <i>Escherichia coli</i> TEM1 β‐lactamase at 1.8 Å resolution

    Crystal structure of <i>Escherichia coli</i> TEM1 β‐lactamase at 1.8 Å resolution od Christian Jelsch, Lionel Mourey, Jean‐Michel Masson, Jean‐Pierre Samama

    Izdano 1993
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  3. 3
    Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase.

    Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase. od H. Eklund, Bryce V. Plapp, Jean‐Pierre Samama, C.-I. Brändén

    Izdano 1982
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  4. 4
    X-Ray Studies of the Binding of Cibacron Blue F3GA to Liver Alcohol Dehydrogenase

    X-Ray Studies of the Binding of Cibacron Blue F3GA to Liver Alcohol Dehydrogenase od Jean‐François Biellmann, Jean‐Pierre Samama, C.-I. Brändén, Hans Eklund

    Izdano 1979
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  5. 5
    Critical involvement of a carbamylated lysine in catalytic function of class D β-lactamases

    Critical involvement of a carbamylated lysine in catalytic function of class D β-lactamases od Dasantila Golemi, Laurent Maveyraud, Sergei B. Vakulenko, Jean‐Pierre Samama, Shahriar Mobashery

    Izdano 2001
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  6. 6
    Crystal Structure of Cleaved Bovine Antithrombin III at 3·2 Å Resolution

    Crystal Structure of Cleaved Bovine Antithrombin III at 3·2 Å Resolution od Lionel Mourey, Jean‐Pierre Samama, Marc Delarue, Maurice Petitou, J Choay, Dino Moras

    Izdano 1993
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  7. 7
    Antithrombin III: structural and functional aspects

    Antithrombin III: structural and functional aspects od Lionel Mourey, Jean‐Pierre Samama, M. Delarue, J Choay, J C Lormeau, Maurice Petitou, Dino Moras

    Izdano 1990
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  8. 8
    Insights into Class D β-Lactamases Are Revealed by the Crystal Structure of the OXA10 Enzyme from Pseudomonas aeruginosa

    Insights into Class D β-Lactamases Are Revealed by the Crystal Structure of the OXA10 Enzyme from Pseudomonas aeruginosa od Laurent Maveyraud, Dasantila Golemi, Lakshmi P. Kotra, S. Tranier, Sergei B. Vakulenko, Shahriar Mobashery, Jean‐Pierre Samama

    Izdano 2000
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  9. 9
    Structural Basis for Clinical Longevity of Carbapenem Antibiotics in the Face of Challenge by the Common Class A β-Lactamases from the Antibiotic-Resistant Bacteria

    Structural Basis for Clinical Longevity of Carbapenem Antibiotics in the Face of Challenge by the Common Class A β-Lactamases from the Antibiotic-Resistant Bacteria od Laurent Maveyraud, Lionel Mourey, Lakshmi P. Kotra, J.D. Pédelacq, Valérie Guillet, Shahriar Mobashery, Jean‐Pierre Samama

    Izdano 1998
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  10. 10
    Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis

    Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis od Lionel Mourey, Sandra Da Re, J.D. Pédelacq, Tatiana Tolstykh, Cécile Faurie, Valérie Guillet, Jeffry B. Stock, Jean‐Pierre Samama

    Izdano 2001
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  11. 11
    The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins

    The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins od J.D. Pédelacq, Laurent Maveyraud, Gilles Prévost, Lamine Baba‐Moussa, Ana María González Noya, Emmanuel Courcelle, William Shepard, H. Monteil, Jean‐Pierre Samama, Lionel Mourey

    Izdano 1999
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  12. 12
    X-ray Analysis of the NMC-A β-Lactamase at 1.64-Å Resolution, a Class A Carbapenemase with Broad Substrate Specificity

    X-ray Analysis of the NMC-A β-Lactamase at 1.64-Å Resolution, a Class A Carbapenemase with Broad Substrate Specificity od Peter Swarén, Laurent Maveyraud, Xavier Raquet, Stéphanie Cabantous, Colette Duez, J.D. Pédelacq, Sophie Mariotte-Boyer, Lionel Mourey, Roger Labia, Marie-Hélène Nicolas-Chanoine, Patrice Nordmann, Jean‐Marie Frère, Jean‐Pierre Samama

    Izdano 1998
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