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Journal Abstract Search

81 related items for PubMed ID: 8884977

  • 41.
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  • 42. A synthetic peptide encompassing two discontinuous regions of hFSH-beta subunit mimics the receptor binding surface of the hormone.
    Santa-Coloma TA, Crabb JW, Reichert LE.
    Mol Cell Endocrinol; 1991 Jul; 78(3):197-204. PubMed ID: 1778304
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  • 43. NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
    Elshorst B, Hennig M, Försterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E.
    Biochemistry; 1999 Sep 21; 38(38):12320-32. PubMed ID: 10493800
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  • 45. In vitro aging of calmodulin generates isoaspartate at multiple Asn-Gly and Asp-Gly sites in calcium-binding domains II, III, and IV.
    Potter SM, Henzel WJ, Aswad DW.
    Protein Sci; 1993 Oct 21; 2(10):1648-63. PubMed ID: 8251940
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  • 47. Apocalmodulin and Ca2+ calmodulin-binding sites on the CaV1.2 channel.
    Tang W, Halling DB, Black DJ, Pate P, Zhang JZ, Pedersen S, Altschuld RA, Hamilton SL.
    Biophys J; 2003 Sep 21; 85(3):1538-47. PubMed ID: 12944271
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  • 49. Role of the N-terminal region of the skeletal muscle myosin light chain kinase target sequence in its interaction with calmodulin.
    Findlay WA, Gradwell MJ, Bayley PM.
    Protein Sci; 1995 Nov 21; 4(11):2375-82. PubMed ID: 8563635
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  • 51. A subunit interaction site in human luteinizing hormone: identification by photoaffinity cross-linking.
    Keutmann HT, Rubin DA.
    Endocrinology; 1993 Mar 21; 132(3):1305-12. PubMed ID: 7679977
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  • 57. Structural features underlying the unusual mode of calmodulin phosphorylation by protein kinase CK2: A study with synthetic calmodulin fragments.
    Marin O, Meggio F, Pinna LA.
    Biochem Biophys Res Commun; 1999 Mar 16; 256(2):442-6. PubMed ID: 10079204
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  • 58.
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  • 60. A synthetic 33-residue analogue of bovine brain calmodulin calcium binding site III: synthesis, purification, and calcium binding.
    Reid RE.
    Biochemistry; 1987 Sep 22; 26(19):6070-3. PubMed ID: 3689760
    [Abstract] [Full Text] [Related]

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