Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Elaine D. Fraser"'
Publikováno v:
Journal of Biological Chemistry. 271:8605-8611
Calponin has been implicated in the regulation of smooth muscle contraction through its interaction with F-actin and inhibition of the actin-activated MgATPase activity of phosphorylated myosin. Both properties are lost following phosphorylation (pri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4b9a1abf6f8f433a76078cb2afb72685
https://doi.org/10.1074/jbc.271.15.8605
https://doi.org/10.1074/jbc.271.15.8605
Autor:
Elaine D. Fraser, Michael P. Walsh
Publikováno v:
Biochemistry. 34:9151-9158
Calponin is a smooth muscle-specific, thin filament-associated protein which has been implicated in the regulation of contraction via its interaction with actin and inhibition of the cross-bridge cycling rate. Calponin is phosphorylated by protein ki
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a46f683a238a2d65c5bf05047152de06
https://doi.org/10.1021/bi00028a026
https://doi.org/10.1021/bi00028a026
Autor:
Marek Michalak, Elaine D. Fraser, Mary D. Pato, Jody L. Busaan, Susan Y. Fu, Michael P. Walsh
Publikováno v:
Biochemistry. 34(16)
We report that the C-terminal domain of skeletal muscle dystrophin expressed as a fusion protein with glutathione S-transferase (designated GST-CT-1) is a substrate for Ca2+/calmodulin-dependent phosphorylation and dephosphorylation. GST-CT-1 and GST
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95ced987bc90a8c57ca4111ad1fcde54
https://pubmed.ncbi.nlm.nih.gov/7727417
https://pubmed.ncbi.nlm.nih.gov/7727417
Autor:
Gary J. Kargacin, Bruce G. Allen, Michael P. Walsh, Elaine D. Fraser, Hyoung-Min Kang, Steve J. Winder
Publikováno v:
The Biochemical journal. 296
Calponin, a thin-filament-associated protein implicated in the regulation of smooth-muscle contraction, is phosphorylated in vitro by protein kinase C and Ca2+/calmodulin-dependent protein kinase II [Winder and Walsh (1990) J. Biol. Chem. 265, 10148-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0606613cd92428de71b33636cb5970ea
https://pubmed.ncbi.nlm.nih.gov/8280082
https://pubmed.ncbi.nlm.nih.gov/8280082
Autor:
Michael P. Walsh, Elaine D. Fraser
Publikováno v:
FEBS letters. 294(3)
A crude cytosolic fraction prepared from bovine brain contained protein kinase C, as shown by immunoblotting, but its activity was undetectable, suggesting the presence of interfering factors. Phosphatase, ATPase and protease activities did not accou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::891a50e59ddfb61ce29158f02362d7dd
https://pubmed.ncbi.nlm.nih.gov/1756872
https://pubmed.ncbi.nlm.nih.gov/1756872
Autor:
Robert L. Heinrikson, James D. Pearson, Michael P. Walsh, W. Rodney Mathews, Elaine D. Fraser, Ned M. Mozier, David M. Guido, Heidi A. Zurcher-Neely
Publikováno v:
European journal of biochemistry. 194(1)
The complete primary structure of a bovine-brain-derived inhibitor of protein kinase C has been established. Fragments of the purified protein were obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease, trypsin and chymotrypsi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::270f867e618707467e7a50313151f139
https://pubmed.ncbi.nlm.nih.gov/1915353
https://pubmed.ncbi.nlm.nih.gov/1915353
Publikováno v:
Biochemistry and Cell Biology. 67:260-270
Protein kinase C was purified from the cytosolic fraction of chicken gizzard by Ca2+-dependent hydrophobic interaction chromatography, anion-exchange chromatography, and hydrophobic chromatography. The molecular weight was estimated as 61 500 by gel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9109d83c917e1c82111afbb93f5cb746
https://doi.org/10.1139/o89-039
https://doi.org/10.1139/o89-039
Publikováno v:
Archives of biochemistry and biophysics. 259(2)
Using as a starting material either a detergent extract or a protein fraction eluted from membranes with ethylene glycol bis (β-aminoethyl ether)-N,N′-tetraacetic acid, we have isolated from human placental membranes a major substrate for the epid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6220392f663c6d280c8807b7b584610a
https://pubmed.ncbi.nlm.nih.gov/2962537
https://pubmed.ncbi.nlm.nih.gov/2962537