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Journal Abstract Search

307 related items for PubMed ID: 8619984

  • 1. Expressing functional domains of mouse calponin: involvement of the region around alanine 145 in the actomyosin ATPase inhibitory activity of calponin.
    el-Mezgueldi M, Strasser P, Fattoum A, Gimona M.
    Biochemistry; 1996 Mar 26; 35(12):3654-61. PubMed ID: 8619984
    [Abstract] [Full Text] [Related]

  • 2. The inhibitory complex of smooth muscle caldesmon with actin and tropomyosin involves three interacting segments of the C-terminal domain 4.
    Fraser ID, Copeland O, Bing W, Marston SB.
    Biochemistry; 1997 May 06; 36(18):5483-92. PubMed ID: 9154931
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  • 3. Characterization of the regulatory domain of gizzard calponin. Interactions of the 145-163 region with F-actin, calcium-binding proteins, and tropomyosin.
    Mezgueldi M, Mendre C, Calas B, Kassab R, Fattoum A.
    J Biol Chem; 1995 Apr 14; 270(15):8867-76. PubMed ID: 7721794
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  • 6. [The effect of a caldesmon fragment with a mol. weight of 38 kDa and calponin on the capacity of actin to form a "strong" form of binding with myosin heads].
    Khoroshev MI, Borovikov IuS, Avrova SV, Horiuchi KY, Kirillina VP, Chacko S.
    Tsitologiia; 1996 Apr 14; 38(3):346-50. PubMed ID: 8768101
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  • 7. Epitope mapping of monoclonal antibodies against caldesmon and their effects on the binding of caldesmon to Ca++/calmodulin and to actin or actin-tropomyosin filaments.
    Lin JJ, Davis-Nanthakumar EJ, Jin JP, Lourim D, Novy RE, Lin JL.
    Cell Motil Cytoskeleton; 1991 Apr 14; 20(2):95-108. PubMed ID: 1721558
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  • 10. Characterization of wild type and mutant chicken gizzard alpha calponin expressed in E. coli.
    Gong BJ, Mabuchi K, Takahashi K, Nadal-Ginard B, Tao T.
    J Biochem; 1993 Oct 14; 114(4):453-6. PubMed ID: 8276752
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  • 11. The CH-domain of calponin does not determine the modes of calponin binding to F-actin.
    Galkin VE, Orlova A, Fattoum A, Walsh MP, Egelman EH.
    J Mol Biol; 2006 Jun 02; 359(2):478-85. PubMed ID: 16626733
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  • 12. Two domains of interaction with calcium binding proteins can be mapped using fragments of calponin.
    Wills FL, McCubbin WD, Gimona M, Strasser P, Kay CM.
    Protein Sci; 1994 Dec 02; 3(12):2311-21. PubMed ID: 7756987
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  • 13. The mechanism of inhibition of the actin-activated myosin MgATPase by calponin.
    Miki M, Walsh MP, Hartshorne DJ.
    Biochem Biophys Res Commun; 1992 Sep 16; 187(2):867-71. PubMed ID: 1388358
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  • 14. Precise identification of the regulatory F-actin- and calmodulin-binding sequences in the 10-kDa carboxyl-terminal domain of caldesmon.
    Mezgueldi M, Derancourt J, Calas B, Kassab R, Fattoum A.
    J Biol Chem; 1994 Apr 29; 269(17):12824-32. PubMed ID: 8175696
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  • 15. Mapping the microtubule binding regions of calponin.
    Fattoum A, Roustan C, Smyczynski C, Der Terrossian E, Kassab R.
    Biochemistry; 2003 Feb 11; 42(5):1274-82. PubMed ID: 12564930
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  • 16. Mapping of the functional domains in the amino-terminal region of calponin.
    Mezgueldi M, Fattoum A, Derancourt J, Kassab R.
    J Biol Chem; 1992 Aug 05; 267(22):15943-51. PubMed ID: 1639822
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  • 17. Structural and functional characterization of calponin fragments.
    Winder SJ, Walsh MP.
    Biochem Int; 1990 Oct 05; 22(2):335-41. PubMed ID: 2151018
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  • 18. Identification and functional characterization of protein 4.1R and actin-binding sites in erythrocyte beta spectrin: regulation of the interactions by phosphatidylinositol-4,5-bisphosphate.
    An X, Debnath G, Guo X, Liu S, Lux SE, Baines A, Gratzer W, Mohandas N.
    Biochemistry; 2005 Aug 09; 44(31):10681-8. PubMed ID: 16060676
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  • 19. Regulatory properties of recombinant tropomyosins containing 5-hydroxytryptophan: Ca2+-binding to troponin results in a conformational change in a region of tropomyosin outside the troponin binding site.
    Farah CS, Reinach FC.
    Biochemistry; 1999 Aug 10; 38(32):10543-51. PubMed ID: 10441151
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  • 20. Tropomyosin has discrete actin-binding sites with sevenfold and fourteenfold periodicities.
    Hitchcock-DeGregori SE, Varnell TA.
    J Mol Biol; 1990 Aug 20; 214(4):885-96. PubMed ID: 2143787
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