Zobrazeno 1 - 8
of 8
pro vyhledávání: '"M E, Hemric"'
Publikováno v:
Journal of Biological Chemistry. 269:4125-4128
Activation of platelets with physiological agents results in distinct cellular events such as shape change, cell aggregation, granule secretion, and clot retraction. Translocation of soluble cytoplasmic myosin to the actin cytoskeleton occurs during
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5753446e44f6e93615fd04415450d5e2
https://doi.org/10.1016/s0021-9258(17)41752-2
https://doi.org/10.1016/s0021-9258(17)41752-2
Publikováno v:
Journal of Biological Chemistry. 267:23001-23006
The movement of reconstituted thin filaments over an immobilized surface of thiophosphorylated smooth muscle myosin was examined using an in vitro motility assay. Reconstituted thin filaments contained actin, tropomyosin, and either purified chicken
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7fbafd3f559b38705bb886182ac06fa6
https://doi.org/10.1016/s0021-9258(18)50047-8
https://doi.org/10.1016/s0021-9258(18)50047-8
Publikováno v:
The Journal of biological chemistry. 269(6)
Activation of platelets with physiological agents results in distinct cellular events such as shape change, cell aggregation, granule secretion, and clot retraction. Translocation of soluble cytoplasmic myosin to the actin cytoskeleton occurs during
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cb69dc470677f7a146046299316f7a6e
https://pubmed.ncbi.nlm.nih.gov/8307972
https://pubmed.ncbi.nlm.nih.gov/8307972
Publikováno v:
The Journal of biological chemistry. 268(20)
Caldesmon, an actin-binding protein from smooth muscle and non-muscle cells, has previously been shown to bind stoichiometrically to smooth muscle myosin in an ATP-dependent manner. We now show quantitatively the effects of Ca(2+)-calmodulin and phos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::12caa38bcff82122f945dd4e55758b64
https://pubmed.ncbi.nlm.nih.gov/8325900
https://pubmed.ncbi.nlm.nih.gov/8325900
Publikováno v:
The Journal of biological chemistry. 267(32)
The movement of reconstituted thin filaments over an immobilized surface of thiophosphorylated smooth muscle myosin was examined using an in vitro motility assay. Reconstituted thin filaments contained actin, tropomyosin, and either purified chicken
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0051fc61a8c583c954d949ce229455af
https://pubmed.ncbi.nlm.nih.gov/1429647
https://pubmed.ncbi.nlm.nih.gov/1429647
Autor:
M E, Hemric, J M, Chalovich
Publikováno v:
The Journal of biological chemistry. 265(32)
Caldesmon inhibits the binding of skeletal muscle subfragment-1 (S-1).ATP to actin but enhances the binding of smooth muscle heavy meromyosin (HMM).ATP to actin. This effect results from the direct binding of caldesmon to myosin in the order of affin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::08b5f6c9daf41b30eba6564c25947afe
https://pubmed.ncbi.nlm.nih.gov/2246251
https://pubmed.ncbi.nlm.nih.gov/2246251
Autor:
M E, Hemric, J M, Chalovich
Publikováno v:
The Journal of biological chemistry. 263(4)
We have previously shown that inhibition of the ATPase activity of skeletal muscle myosin subfragment 1 (S1) by caldesmon is correlated with the inhibition of S1 binding in the presence of ATP or pyrophosphate (Chalovich, J., Cornelius, P., and Benso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::979a0af0ee8a1dae28d3fe0163ff695e
https://pubmed.ncbi.nlm.nih.gov/2962997
https://pubmed.ncbi.nlm.nih.gov/2962997
Publikováno v:
The Journal of biological chemistry. 264(16)
The binding of 125I- and 14C-caldesmon to actin and actin-tropomyosin was studied using a cosedimentation technique and was analyzed by the method of McGhee and von Hippel [1974) J. Mol. Biol. 86, 469-489) for the binding of large ligands to a homoge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b62c948e8470f41ecd8a8df89b74c17a
https://pubmed.ncbi.nlm.nih.gov/2524487
https://pubmed.ncbi.nlm.nih.gov/2524487