Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Hiromitsu Nagumo"'
Autor:
Go Kasuya, Toshiaki Yamaura, Xiao-Bo Ma, Ryoki Nakamura, Mizuki Takemoto, Hiromitsu Nagumo, Eiichi Tanaka, Naoshi Dohmae, Takanori Nakane, Ye Yu, Ryuichiro Ishitani, Osamu Matsuzaki, Motoyuki Hattori, Osamu Nureki
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
P2X receptors are nonselective cation channels that are gated by extracellular ATP. Here the authors present the crystal structure of chicken P2X7 with its bound competitive antagonist TNP-ATP and give mechanistic insights into TNP-ATP dependent inhi
Externí odkaz:
https://doaj.org/article/cb0f6ce882154f37b17a413f1ef7ef0d
Autor:
Motoyuki Hattori, Hiromitsu Nagumo, Mizuki Takemoto, Ye Yu, Naoshi Dohmae, Go Kasuya, Ryoki Nakamura, Eiichi Tanaka, Ryuichiro Ishitani, Toshiaki Yamaura, Takanori Nakane, Xiao-Bo Ma, Osamu Nureki, Osamu Matsuzaki
Publikováno v:
Nature Communications
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
P2X receptors are non-selective cation channels gated by extracellular ATP, and the P2X7 receptor subtype plays a crucial role in the immune and nervous systems. Altered expression and dysfunctions of P2X7 receptors caused by genetic deletions, mutat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5863cc214e1904edeec153b40c4e548c
https://pubmed.ncbi.nlm.nih.gov/29026074
https://pubmed.ncbi.nlm.nih.gov/29026074
Autor:
Hideji Hiraoka, Yasuharu Sasaki, Eishichi Miyamoto, Hiromitsu Nagumo, Hirotsugu Kato, Yasuhito Naito, Toshihiko Ikuhara, Yuri Ikeda Matsuo, Katsuhiko Sakurada, Kouji Fukunaga, Kaoru Furuya, Fumio Matsumura, Yoshihiko Yamakita
Publikováno v:
Journal of Biological Chemistry. 277:45473-45479
The function of synapsin I is regulated by phosphorylation of the molecule at multiple sites; among them, the Ser(603) residue (site 3) is considered to be a pivotal site targeted by Ca(2+)/calmodulin-dependent kinase II (CaMKII). Although phosphoryl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7db67a4ac081cd1bb9ac883c79822e74
https://doi.org/10.1074/jbc.m206673200
https://doi.org/10.1074/jbc.m206673200
Publikováno v:
American Journal of Physiology-Cell Physiology. 278:C57-C65
In smooth muscle, a Rho-regulated system of myosin phosphatase exists; however, it has yet to be established whether Rho kinase, one of the downstream effectors of Rho, mediates the regulation of myosin phosphatase activity in vivo. In the present st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc2657feabf1d3c13da72e23910bb79b
https://doi.org/10.1152/ajpcell.2000.278.1.c57
https://doi.org/10.1152/ajpcell.2000.278.1.c57
Autor:
Hirotsugu Yokoi, Ryuichi Tsujita, Masahiro Saitoh, Toshiyuki Kodama, Yuji Ohtsuka, Takashi Kubota, Kenji Naganuma, Junji Nakamura, Naoto Ohkawa, Masayoshi Takemura, Masashi Kawanishi, Akifumi Omura, Hiromitsu Nagumo, Naomi Maekawara, Koh Kawasaki
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:3174-3176
In this study the first PDE4B selective inhibitor is described. Optimization of lead 2-arylpyrimidine derivatives afforded a series of potent PDE4B inhibitors with >100-fold selectivity over the PDE4D isozyme. With a good pharmacokinetic profile, a s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71c5d21651e4ef7eb5286012e998d3b1
https://doi.org/10.1016/j.bmcl.2009.04.121
https://doi.org/10.1016/j.bmcl.2009.04.121
Publikováno v:
Biochemical and Biophysical Research Communications. 203:1502-1507
Polyclonal antibody against phosphorylated calponin was raised in rabbits by application of the peptide corresponding to residues 183-195 of calponin phosphorylated by protein kinase C. When calponin was incubated with protein kinase C, only free cal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a92f3ee76d2a8c6ffd97681c833c256
https://doi.org/10.1006/bbrc.1994.2355
https://doi.org/10.1006/bbrc.1994.2355
Autor:
Minoru Seto, Yoh Takuwa, Hiromitsu Nagumo, Kazutoshi Shindo, Junji Nakamura, Katsuaki Ito, Erika Shimomura, Mitsuya Shiraishi, Takahiro Iwanaga, Yasuharu Sasaki
Inhibition of dephosphorylation of the 20 kDa myosin light chain (MLC(20)) is an important mechanism for the Ca(2+)-induced sensitization of vascular smooth muscle contraction. We investigated whether this mechanism operates in prostaglandin F(2alpha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec66f6c3077281b6679887532bc951ff
https://europepmc.org/articles/PMC2342586/
https://europepmc.org/articles/PMC2342586/
Publikováno v:
European journal of pharmacology. 360(2-3)
Calponin is a thin filament-associated protein which has been implicated in the modulation of the contractile state of smooth muscle via its interaction with actin and inhibition of the actin-activated myosin Mg-ATPase. This inhibitory effect is alle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::863374cc7af8cc2507721b37faf4187a
https://pubmed.ncbi.nlm.nih.gov/9851593
https://pubmed.ncbi.nlm.nih.gov/9851593
Selectivity of action of staurosporine on Ca2+ movements and contractions in vascular smooth muscles
Autor:
Katsuhiko Sakurada, Katsuaki Ito, Hiromitsu Nagumo, Kaoru M. Ito, Kumi Matsunaga, Yasuharu Sasaki, Masaaki Asano, Madoka Miura, Minoru Seto
Publikováno v:
European journal of pharmacology. 294(2-3)
We examined the effects of staurosporine, a protein kinase inhibitor, on Ca2+ movements and contractions due to KCl and 12-deoxyphorbol 13-isobutyrate (DPB), which are thought to activate myosin light chain kinase and protein kinase C, respectively.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffa3a8ff037593c1369dd4deaef25b95
https://pubmed.ncbi.nlm.nih.gov/8750735
https://pubmed.ncbi.nlm.nih.gov/8750735
Publikováno v:
Japanese Journal of Pharmacology. 82:206
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::daa75a83f0718bdaa4c3db45ff72705d
https://doi.org/10.1016/s0021-5198(19)48288-7
https://doi.org/10.1016/s0021-5198(19)48288-7