Zobrazeno 1 - 10
of 110
pro vyhledávání: '"Michio Yazawa"'
Publikováno v:
The Journal of Physical Chemistry C. 120:16035-16041
Calcium ion (Ca2+)-induced functional expression of calmodulin (CaM), which is a signal transmitter in living cell, is known to be associated with its conformation change; however, it is difficult to correlate the conformational change and functional
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7c98684d32bdbcb314c33712dd5fa69b
https://doi.org/10.1021/acs.jpcc.5b12724
https://doi.org/10.1021/acs.jpcc.5b12724
Publikováno v:
Journal of Biochemistry. 152:27-35
The vertebrate calmodulin is configured with two structurally independent globular lobes in N- and C-terminus, and a flexible central linker. Distinctly, two lobes of calmodulin from Saccharomyces cerevisiae (yCaM) interact and influence the Ca(2+)-b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d2f454ddbaa43f36a2a1a329c35c819
https://doi.org/10.1093/jb/mvs048
https://doi.org/10.1093/jb/mvs048
Autor:
Hiroyuki Itoh, Hiroyuki Kumeta, Michio Yazawa, Yoshihiro Kobashigawa, Kenji Ogura, Ryosuke Yoshida, Kiyohiro Takahasi, Fuyuhiko Inagaki
Publikováno v:
Genes to Cells. 17:159-172
We determined the solution structures of the calmodulin (CaM) isoform from yeast Saccharomyces cerevisiae (yCaM) in the calcium-bound form and in complex with a target peptide using NMR spectroscopy and small-angle X-ray scattering (SAXS). yCaM shows
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c6a40e136a4e81b947c90e31d076c71f
https://doi.org/10.1111/j.1365-2443.2012.01580.x
https://doi.org/10.1111/j.1365-2443.2012.01580.x
Publikováno v:
Marine Biotechnology. 14:479-490
Calcineurin is a calcium/calmodulin-dependent protein phosphatase that plays important roles in the transduction of calcium signals in a variety of tissues. In addition, calcineurin has been implicated in the process of spermatogenesis. A novel calci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32df597a0e09539cf3145c845c8d7cb3
https://doi.org/10.1007/s10126-011-9429-9
https://doi.org/10.1007/s10126-011-9429-9
Autor:
Yoshinori Iida, Michio Yazawa, Akiko Nakatomi, Shinya Ohki, Nobuaki Nemoto, Noriyoshi Isozumi
Publikováno v:
The Journal of Biochemistry. 149:463-474
Calmodulin (CaM), a Ca(2+)-binding protein, is a well-known regulator of various cellular functions. One of the targets of CaM is metabotropic glutamate receptor 7 (mGluR7), which serves as a low-pass filter for glutamate in the pre-synaptic terminal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f69ebd48171e820778579326aa61b31
https://doi.org/10.1093/jb/mvr006
https://doi.org/10.1093/jb/mvr006
Publikováno v:
Biochemical and Biophysical Research Communications. 381:682-687
The actomyosin cytoskeleton plays prominent roles in cell spreading and migration. To address the roles of myosin II isoforms and to estimate the region where the myosin IIs are activated in spreading cells, we examined the immunolocalization of myos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce9275fda509054fc1a51f306108941c
https://doi.org/10.1016/j.bbrc.2009.02.121
https://doi.org/10.1016/j.bbrc.2009.02.121
Autor:
Jui Yoa Chang, Potchanapond Graidist, Amornrat Phongdara, Akiko Nakatomi, Michio Yazawa, Kenichi Fujise, Curtis Chun Jen Lin, Moltira Tonganunt
Publikováno v:
Biochemical Journal. 408:181-191
Fortilin, a 172-amino-acid polypeptide present both in the cytosol and nucleus, possesses potent anti-apoptotic activity. Although fortilin is known to bind Ca2+, the biochemistry and biological significance of such an interaction remains unknown. In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd8686c9448c9fac2163014739156189
https://doi.org/10.1042/bj20070679
https://doi.org/10.1042/bj20070679
Publikováno v:
Molecular biology of the cell. 18(3):1009-1017
To function in the cell, nonmuscle myosin II molecules assemble into filaments through their C-terminal tails. Because myosin II isoforms most likely assemble into homo-filaments in vivo, it seems that some self-recognition mechanisms of individual m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::feaed1cf42f1dbd27dae89b42ef03d8f
http://hdl.handle.net/2115/52174
http://hdl.handle.net/2115/52174
Autor:
Naoya Hirata, Michio Yazawa, Mariko Mitsuhashi, Takashi Nakasawa, Masayuki Takahashi, Masaaki Sato
Publikováno v:
Seibutsu Butsuri. 46:15-19
All vertebrate cells, including muscle cells, contain nonmuscle myosin II which plays a role in a number of cell motility processes. Dynamic filament assembly-disassembly transition of myosin II molecules is particularly important in nonmuscle cells.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9481107e2a3267d0beca10bf9e7b5c9a
https://doi.org/10.2142/biophys.46.15
https://doi.org/10.2142/biophys.46.15
Publikováno v:
Biochemical and Biophysical Research Communications. 333:1060-1065
The interaction between calmodulin (CaM) and Al(3+) was studied by spectroscopic methods. Heteronuclear two-dimensional NMR data indicated that peaks related to the both lobes and middle of the central helix of CaM are largely affected by Al(3+). But
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67085691d786fb14785d59866c76f435
https://doi.org/10.1016/j.bbrc.2005.06.016
https://doi.org/10.1016/j.bbrc.2005.06.016