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Journal Abstract Search

48 related items for PubMed ID: 9010620

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  • 25. The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits.
    Fushman D, Najmabadi-Haske T, Cahill S, Zheng J, LeVine H, Cowburn D.
    J Biol Chem; 1998 Jan 30; 273(5):2835-43. PubMed ID: 9446593
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  • 27. Ligand-gated split-kinases.
    Camacho-Soto K, Castillo-Montoya J, Tye B, Ghosh I.
    J Am Chem Soc; 2014 Mar 12; 136(10):3995-4002. PubMed ID: 24533431
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  • 28. Exceptional disfavor for proline at the P + 1 position among AGC and CAMK kinases establishes reciprocal specificity between them and the proline-directed kinases.
    Zhu G, Fujii K, Belkina N, Liu Y, James M, Herrero J, Shaw S.
    J Biol Chem; 2005 Mar 18; 280(11):10743-8. PubMed ID: 15647260
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  • 31. Comparative study of the prereactive protein kinase A Michaelis complex with kemptide substrate.
    Montenegro M, Garcia-Viloca M, González-Lafont A, Lluch JM.
    J Comput Aided Mol Des; 2007 Mar 18; 21(10-11):603-15. PubMed ID: 18008170
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  • 35. Substrate recognition mechanism of human beta-adrenergic receptor kinase 1 based on a three-dimensional model structure.
    Iino M, Shibano T.
    Drug Des Discov; 1996 Oct 18; 14(2):145-55. PubMed ID: 9010620
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  • 36. Asp278 of human beta-adrenergic receptor kinase 1 is essential for phosphorylation activity.
    Iino M, Furugohri T, Fukuzawa A, Shibano T.
    Biochem Biophys Res Commun; 1997 Oct 20; 239(2):548-51. PubMed ID: 9344867
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  • 38. The beta-adrenergic receptor kinase interacts with the amino terminus of the G protein beta subunit.
    Goldman PS, DeMaggio AJ, Hoekstra MF, Goodman RH.
    Biochem Biophys Res Commun; 1997 Nov 17; 240(2):425-9. PubMed ID: 9388495
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  • 40. Substrate recognition mechanism of human beta-adrenergic receptor kinase 1 based on a three-dimensional model structure.
    Iino M, Shibano T.
    Drug Des Discov; 1996 Oct 17; 14(2):145-55. PubMed ID: 9010620
    [Abstract] [Full Text] [Related]

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