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155 related items for PubMed ID: 6236813

  • 1. Calelectrins are a ubiquitous family of Ca2+-binding proteins purified by Ca2+-dependent hydrophobic affinity chromatography by a mechanism distinct from that of calmodulin.
    Südhof TC.
    Biochem Biophys Res Commun; 1984 Aug 30; 123(1):100-7. PubMed ID: 6236813
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  • 2. Characterization of calelectrin, a Ca2+-binding protein isolated from the electric organ of Torpedo marmorata.
    Südhof TC, Walker JH, Fritsche U.
    J Neurochem; 1985 Apr 30; 44(4):1302-7. PubMed ID: 3156212
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  • 3. Isolation of mammalian calelectrins: a new class of ubiquitous Ca2+-regulated proteins.
    Südhof TC, Ebbecke M, Walker JH, Fritsche U, Boustead C.
    Biochemistry; 1984 Mar 13; 23(6):1103-9. PubMed ID: 6231954
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  • 4. Structural and functional characterization of calelectrins from bovine liver.
    Fujii T, Akashi H, Ogoma Y, Kondo Y.
    Chem Pharm Bull (Tokyo); 1991 Feb 13; 39(2):421-4. PubMed ID: 1829026
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  • 13. Monovalent cation-insensitive hydrophobic region on calmodulin facilitates the rapid isolation and quantitation of calmodulin free from other Ca2+-dependent hydrophobic proteins.
    Gopalakrishna R, Anderson WB.
    J Appl Biochem; 1985 Feb 13; 7(4-5):311-22. PubMed ID: 3005224
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  • 14. Ca2+-binding proteins from bovine brain including a potent inhibitor of protein kinase C.
    McDonald JR, Walsh MP.
    Biochem J; 1985 Dec 01; 232(2):559-67. PubMed ID: 4091808
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