Zobrazeno 1 - 8
of 8
pro vyhledávání: '"G C Scott-Woo"'
Publikováno v:
Journal of Molecular and Cellular Cardiology. 31:1413-1417
The high abundance of caldesmon in smooth muscle and its ability to inhibit actomyosin ATPase activity have led to the hypothesis that caldesmon modulates contractile activity. It has also been proposed, however, that caldesmon acts as a structural p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::698a4f8f5a89efb4e1596e875cf7cc92
https://doi.org/10.1006/jmcc.1999.0980
https://doi.org/10.1006/jmcc.1999.0980
Publikováno v:
The Biochemical journal. 334
Caldesmon has been detected in smooth muscle and in a number of non-muscle cells. It binds both actin and myosin and may act as a regulator of contraction or a structural element in smooth muscle. The presence of caldesmon in striated muscle has not
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8902f50caf0a5ffb5d6462934412f46e
https://pubmed.ncbi.nlm.nih.gov/9693116
https://pubmed.ncbi.nlm.nih.gov/9693116
Publikováno v:
Biochemistry. 29(51)
Previously, it was reported that smooth muscle caldesmon is a protein kinase and is autophosphorylated [Scott-Woo, G. C., & Walsh, M. P. (1988) Biochem. J. 252, 463-472]. We separated a Ca 2+ /calmodulin-dependent protein kinase from caldesmon in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9d7620685512e23bd5767b72a4938e4
https://pubmed.ncbi.nlm.nih.gov/2176896
https://pubmed.ncbi.nlm.nih.gov/2176896
The relationship of the kinase which co-purifies with caldesmon to Ca2+/calmodulin-dependent protein kinase II (CaM-kinase II) was investigated by studying the phosphorylation of bovine brain synapsin I, as well-characterized substrate of CaM-kinase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3655f6a126f96b6f1370c02e226cbb2
https://europepmc.org/articles/PMC1131441/
https://europepmc.org/articles/PMC1131441/
Publikováno v:
Biochemical Pharmacology. 37:1569-1580
We have examined the effects on the activities of three calmodulin-dependent enzymes (cAMP phosphodiesterase, caldesmon kinase and myosin light chain kinase) of the dihydropyridine Ca2+ channel blocker felodipine and three analogues (p-chloro, oxidiz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3652b5aa3e93b5fd03eb171482fa9806
https://doi.org/10.1016/0006-2952(88)90020-2
https://doi.org/10.1016/0006-2952(88)90020-2
Publikováno v:
Journal of Biological Chemistry. 262:5352-5359
Application of the myosin competition test (Lehman, W., and Szent-Gyorgyi, A. G. (1975) J. Gen. Physiol. 66, 1-30) to chicken gizzard actomyosin indicated that this smooth muscle contains a thin filament-linked regulatory mechanism. Chicken gizzard t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::10dc02943d7bcbdcde7d42319aa87d10
https://doi.org/10.1016/s0021-9258(18)61195-0
https://doi.org/10.1016/s0021-9258(18)61195-0
Autor:
G C Scott-Woo, Michael P. Walsh
Caldesmon, a major actin- and calmodulin-binding protein of smooth muscle, has been implicated in regulation of the contractile state of smooth muscle. The isolated protein can be phosphorylated by a co-purifying Ca2+/calmodulin-dependent protein kin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a315227ba935482eb36d30ccf46d9893
https://europepmc.org/articles/PMC1149167/
https://europepmc.org/articles/PMC1149167/
Publikováno v:
Proceedings in Life Sciences ISBN: 9783642730443
It is widely accepted that myosin-linked regulation, specifically the reversible phosphorylation of myosin, represents the primary Ca2+-dependent mechanism for the regulation of smooth muscle contraction. This mechanism is illustrated schematically i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2776acd880615d8a25f56b749495e5d
https://doi.org/10.1007/978-3-642-73042-9_6
https://doi.org/10.1007/978-3-642-73042-9_6