Zobrazeno 1 - 10
of 51
pro vyhledávání: '"Peter D. Chantler"'
Publikováno v:
International Journal of Vascular Medicine, Vol 2013 (2013)
Myosin VI (Myo6) functions in endocytosis in conjunction with binding partners including adaptor protein (AP)-2, disabled 2 (Dab2), and GAIP interacting protein C terminus 1 (GIPC1). This study aimed to investigate the expression and function of Myo6
Externí odkaz:
https://doaj.org/article/969be39f48f045bcbdd9aa37cb181e3d
Autor:
Peter D. Chantler
Scallop aquaculture owes its commercial success to a global appreciation of the gastronomic delights of scallop striated adductor muscle. Early physiologists were also impressed by the high muscle to body weight ratio, the apparent purity of the fibr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::036e9166e3ba8737912ed743cd2a49b6
https://doi.org/10.1016/b978-0-444-62710-0.00004-3
https://doi.org/10.1016/b978-0-444-62710-0.00004-3
Autor:
Steven R. Wylie, Peter D. Chantler
Publikováno v:
Molecular Biology of the Cell. 19:3956-3968
Neuronal dynamics result from the integration of forces developed by molecular motors, especially conventional myosins. Myosin IIC is a recently discovered nonsarcomeric conventional myosin motor, the function of which is poorly understood, particula
Publikováno v:
Journal of Biological Chemistry. 275:4880-4888
Scallop striated adductor muscle myosin is a regulatory myosin, its activity being controlled directly through calcium binding. Here, we show that millimolar concentrations of trifluoperazine were effective at removal of all regulatory light chains f
Publikováno v:
Journal of Muscle Research and Cell Motility. 21:415-422
We have determined the complete cDNA and deduced amino acid sequences of the heavy chain, regulatory light chain and essential light chain which constitute the molecular structure of myosin from the striated adductor muscle of the scallop, Pecten max
Autor:
Mark R. Deziel, Henry S. Slayter, James B. Caulfield, Paul Norton, Peter D. Chantler, Sarkis S. Margossian, Rhea J. C. Levine
Publikováno v:
Molecular and Cellular Biochemistry. 195:1-10
A neutral protease, mekratin, active in human hearts at end stage idiopathic dilated cardiomyopathy (IDC), mediates the breakdown of cardiac myosin LC2. Myosin purified from IDC heart tissue forms unusually short synthetic thick filaments. Therefore,
Autor:
H. S. Slayter, Peter D. Chantler, P. Norton, P. K. Umeda, J. B. Caulfield, P. A. W. Anderson, H. Patel, Fan Yang, A. Malhotra, Mark R. Deziel, Walter F. Stafford, S. S. Margossian
Publikováno v:
Molecular and Cellular Biochemistry. 194:301-313
Calcium regulation in the human heart is impaired during idiopathic dilated cardiomyopathy (IDC). Here, we analyze the structural basis for impairment in the regulatory mechanism. Regulation of contractility was monitored by MgATPase and Ca2+-binding
Publikováno v:
Proceedings of the National Academy of Sciences. 95:12967-12972
Neuritic outgrowth is a striking example of directed motility, powered through the actions of molecular motors. Members of the myosin superfamily of actin-associated motors have been implicated in this complex process. Although conventional myosin II
Publikováno v:
Journal of Molecular Biology
We show that negative-stain electron microscopy and image processing of nucleotide-free (apo) striated muscle myosin-2 subfragment-1 (S1), possessing one light chain or both light chains, is capable of resolving significant amounts of structural deta
Publikováno v:
International Journal of Vascular Medicine
International Journal of Vascular Medicine, Vol 2013 (2013)
International Journal of Vascular Medicine, Vol 2013 (2013)
Myosin VI (Myo6) functions in endocytosis in conjunction with binding partners including adaptor protein (AP)-2, disabled 2 (Dab2), and GAIP interacting protein C terminus 1 (GIPC1). This study aimed to investigate the expression and function of Myo6