Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Yoh Okamoto"'
Publikováno v:
The Journal of Biochemistry. 111:113-122
Fast skeletal myosins were isolated from carp acclimated to 10 and 30 degrees C, and their structural and enzymatic properties were compared. Myosins in 0.5 M KCl were subjected to limited proteolysis by using various proteases including alpha-chymot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::70c02a84c3cf67161d41eaa16d05396e
https://doi.org/10.1093/oxfordjournals.jbchem.a123706
https://doi.org/10.1093/oxfordjournals.jbchem.a123706
Publikováno v:
Advances in experimental medicine and biology. 538
Molecular assemblies of actin and myosin for the contractility of smooth muscle are quite different from those of striated muscle. Another striking difference is that vascular smooth muscle has a potential to transform to migratory synthetic cell typ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ee7c04b8b33db83c8177ca1308ee563f
https://pubmed.ncbi.nlm.nih.gov/15098669
https://pubmed.ncbi.nlm.nih.gov/15098669
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461347644
Molecular assemblies of actin and myosin for the contractility of smooth muscle are quite different from those of striated muscle. Another striking difference is that vascular smooth muscle has a potential to transform to migratory synthetic cell typ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f231692a1b4db08eeb057a1ca44c715e
https://doi.org/10.1007/978-1-4419-9029-7_20
https://doi.org/10.1007/978-1-4419-9029-7_20
Publikováno v:
Seibutsu Butsuri. 52:S74-S75
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2afb8ce5c57dcbea59b0e1607ef4428
https://doi.org/10.2142/biophys.52.s74_6
https://doi.org/10.2142/biophys.52.s74_6
Publikováno v:
Seibutsu Butsuri. 50:S118-S119
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::63a0d8bf928239e31f07c055856f983b
https://doi.org/10.2142/biophys.50.s118_6
https://doi.org/10.2142/biophys.50.s118_6
Autor:
Yasushi Hasegawa, Yoh Okamoto, Shiho Tsuwaki, Katsuhiro Yamamoto, Shiho Kimura, Junya Sugawara, Naruhito Yamada, Takahiro Araki
Publikováno v:
Journal of biochemistry. 124(2)
We isolated and identified a 110-kDa myosin I from porcine aorta media smooth muscle [Y. Hasegawa et al. (1996) J. Biochem. 120, 971-976]. Partial peptide sequences of the 110-kDa myosin I fragments were homologous to amino acid sequences deduced fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64201733d474f6eec426648fff72e913
https://pubmed.ncbi.nlm.nih.gov/9685736
https://pubmed.ncbi.nlm.nih.gov/9685736
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781468460414
Interaction of myosin and actin has been studied in the presence of inhibitors in order to identify and characterize sites essential for the motor function. Acidic amino acid cluster of actin at the amino terminal region is known to interact with bas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2738c0cd3e7bb850c8fe15d973709d47
https://doi.org/10.1007/978-1-4684-6039-1_11
https://doi.org/10.1007/978-1-4684-6039-1_11
Publikováno v:
Journal of biochemistry. 120(5)
A complex of 110-kDa heavy chain and calmodulin was isolated from porcine aorta media smooth muscle and identified as myosin I. The isolated myosin I consisted of equimolar amounts of 110-kDa heavy chain and calmodulin. The addition of exogenous calm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b547ad28cabb0c654bded97733ec4631
https://pubmed.ncbi.nlm.nih.gov/8982854
https://pubmed.ncbi.nlm.nih.gov/8982854
Publikováno v:
Seibutsu Butsuri. 51:S158
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8da7e64f11862603fc215cc606465bff
https://doi.org/10.2142/biophys.51.s158_1
https://doi.org/10.2142/biophys.51.s158_1
Autor:
Christine R. Cremo, Yoh Okamoto
Publikováno v:
Mechanism of Myofilament Sliding in Muscle Contraction ISBN: 9781461362456
Myosin from rabbit skeletal muscle has been photochemically cleaved in the presence of vanadate ion and ATP. Two cleavage sites termed V1 and V2 within the S1 head region were studied. In the presence of magnesium ion both sites were cleaved, but in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6fb00fd35e53b6f17dadaff463932a13
https://doi.org/10.1007/978-1-4615-2872-2_24
https://doi.org/10.1007/978-1-4615-2872-2_24