Resultados da pesquisa - Richard A. Roth

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  1. 1
    The insulin receptor-related receptor. Tissue expression, ligand binding specificity, and signaling capabilities.

    The insulin receptor-related receptor. Tissue expression, ligand binding specificity, and signaling capabilities. Por Bing Zhang, Richard A. Roth

    Publicado em 1992
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  2. 2
    Defective internalization of insulin and its receptor in cells expressing mutated insulin receptors lacking kinase activity.

    Defective internalization of insulin and its receptor in cells expressing mutated insulin receptors lacking kinase activity. Por Joji Hari, Richard A. Roth

    Publicado em 1987
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  3. 3
    Phosphorylation of Purified Insulin Receptor by cAMP Kinase

    Phosphorylation of Purified Insulin Receptor by cAMP Kinase Por Richard A. Roth, Jacqueline Beaudoin

    Publicado em 1987
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  4. 4
    Acute insulin action requires insulin receptor kinase activity: introduction of an inhibitory monoclonal antibody into mammalian cells blocks the rapid effects of insulin.

    Acute insulin action requires insulin receptor kinase activity: introduction of an inhibitory monoclonal antibody into mammalian cells blocks the rapid effects of insulin. Por David O. Morgan, Richard A. Roth

    Publicado em 1987
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  5. 5
    An unusual active site identified in a family of zinc metalloendopeptidases.

    An unusual active site identified in a family of zinc metalloendopeptidases. Por Andrew B. Becker, Richard A. Roth

    Publicado em 1992
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  6. 6
    Modulation of Insulin Receptor Substrate-1 Tyrosine Phosphorylation and Function by Mitogen-activated Protein Kinase

    Modulation of Insulin Receptor Substrate-1 Tyrosine Phosphorylation and Function by Mitogen-activated Protein Kinase Por Kathryn De Fea, Richard A. Roth

    Publicado em 1997
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  7. 7
    Phosphatidylinositol kinase or an associated protein is a substrate for the insulin receptor tyrosine kinase.

    Phosphatidylinositol kinase or an associated protein is a substrate for the insulin receptor tyrosine kinase. Por Gerda Endemann, Kazuyoshi Yonezawa, Richard A. Roth

    Publicado em 1990
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  8. 8
    Protein Kinase B/Akt Induces Resumption of Meiosis in Xenopus Oocytes

    Protein Kinase B/Akt Induces Resumption of Meiosis in Xenopus Oocytes Por Carsten Andersen, Richard A. Roth, Marco Conti

    Publicado em 1998
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  9. 9
    Akt, a Pleckstrin Homology Domain Containing Kinase, Is Activated Primarily by Phosphorylation

    Akt, a Pleckstrin Homology Domain Containing Kinase, Is Activated Primarily by Phosphorylation Por Aimee D. Kohn, Fumito Takeuchi, Richard A. Roth

    Publicado em 1996
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  10. 10
    Insulin stimulates the kinase activity of RAC-PK, a pleckstrin homology domain containing ser/thr kinase.

    Insulin stimulates the kinase activity of RAC-PK, a pleckstrin homology domain containing ser/thr kinase. Por Aimee D. Kohn, Kristina S. Kovacina, Richard A. Roth

    Publicado em 1995
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  11. 11
    Activation of Protein Kinase B/Akt Is Sufficient to Repress the Glucocorticoid and cAMP Induction of Phosphoenolpyruvate Carboxykinase Gene

    Activation of Protein Kinase B/Akt Is Sufficient to Repress the Glucocorticoid and cAMP Induction of Phosphoenolpyruvate Carboxykinase Gene Por Jinfang Liao, Andreas Barthel, Kaname Nakatani, Richard A. Roth

    Publicado em 1998
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  12. 12
    Modulation of Insulin Receptor Substrate-1 Tyrosine Phosphorylation by an Akt/Phosphatidylinositol 3-Kinase Pathway

    Modulation of Insulin Receptor Substrate-1 Tyrosine Phosphorylation by an Akt/Phosphatidylinositol 3-Kinase Pathway Por Jin‐Ping Li, Kathryn DeFea, Richard A. Roth

    Publicado em 1999
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  13. 13
    Modulation of human insulin receptor substrate-1 tyrosine phosphorylation by protein kinase Cdelta

    Modulation of human insulin receptor substrate-1 tyrosine phosphorylation by protein kinase Cdelta Por Michael W. Greene, Nick Morrice, Robert S. Garofalo, Richard A. Roth

    Publicado em 2004
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  14. 14
    Purification and characterization of the human brain insulin receptor.

    Purification and characterization of the human brain insulin receptor. Por Richard A. Roth, David O. Morgan, Jacqueline Beaudoin, V. R. Sara

    Publicado em 1986
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  15. 15
    Dual regulation of glycogen metabolism by insulin and insulin-like growth factors in human hepatoma cells (HEP-G2). Analysis with an anti-receptor monoclonal antibody.

    Dual regulation of glycogen metabolism by insulin and insulin-like growth factors in human hepatoma cells (HEP-G2). Analysis with an anti-receptor monoclonal antibody. Por E. J. Verspohl, Richard A. Roth, Riccardo Vigneri, Ira D. Goldfine

    Publicado em 1984
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  16. 16
    Expression of a Constitutively Active Akt Ser/Thr Kinase in 3T3-L1 Adipocytes Stimulates Glucose Uptake and Glucose Transporter 4 Translocation

    Expression of a Constitutively Active Akt Ser/Thr Kinase in 3T3-L1 Adipocytes Stimulates Glucose Uptake and Glucose Transporter 4 Translocation Por Aimee D. Kohn, Scott A. Summers, Morris J. Birnbaum, Richard A. Roth

    Publicado em 1996
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  17. 17
    Insulin action is blocked by a monoclonal antibody that inhibits the insulin receptor kinase.

    Insulin action is blocked by a monoclonal antibody that inhibits the insulin receptor kinase. Por David O. Morgan, Lee Dong Ho, Laurence Jay Korn, Richard A. Roth

    Publicado em 1986
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  18. 18
    Inorganic polyphosphate stimulates mammalian TOR, a kinase involved in the proliferation of mammary cancer cells

    Inorganic polyphosphate stimulates mammalian TOR, a kinase involved in the proliferation of mammary cancer cells Por Lihong Wang, Cresson D. Fraley, Jesika S. Faridi, Arthur Kornberg, Richard A. Roth

    Publicado em 2003
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  19. 19
    Protein Kinase B/akt and Rab5 Mediate Ras Activation of Endocytosis

    Protein Kinase B/akt and Rab5 Mediate Ras Activation of Endocytosis Por M. Alejandro Barbieri, Aimee D. Kohn, Richard A. Roth, Philip D. Stahl

    Publicado em 1998
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  20. 20
    Identification of a Human Akt3 (Protein Kinase B γ) Which Contains the Regulatory Serine Phosphorylation Site

    Identification of a Human Akt3 (Protein Kinase B γ) Which Contains the Regulatory Serine Phosphorylation Site Por Kaname Nakatani, Hiroshi Sakaue, Devon A. Thompson, Ronald J. Weigel, Richard A. Roth

    Publicado em 1999
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