Zobrazeno 1 - 10
of 138
pro vyhledávání: '"David J Hartshorne"'
Autor:
Masaya Taniguchi, Ryuji Okamoto, Masaaki Ito, Itaru Goto, Satoshi Fujita, Katsuhisa Konishi, Hideo Mizutani, Kaoru Dohi, David J Hartshorne, Takeo Itoh
Publikováno v:
PLoS ONE, Vol 10, Iss 10, p e0141130 (2015)
Cardiac myosin light chain kinase (cMLCK) plays an obligatory role in maintaining the phosphorylation levels of regulatory myosin light chain (MLC2), which is thought to be crucial for regulation of cardiac function. To test this hypothesis, the role
Externí odkaz:
https://doaj.org/article/907e8100638b451eac1e2a85f6d50acd
Autor:
Masaya Taniguchi, Naoki Makino, Ryuji Okamoto, Katsuya Onishi, Kaoru Dohi, Masaaki Ito, Katsuhisa Konishi, Shinji Satoh, Hideo Mizutani, Takeo Itoh, Nobuyuki Moriki, David J. Hartshorne, Noboru Suzuki, Satoshi Fujita
Publikováno v:
Circulation Journal. 74:120-128
Background: Phosphorylation of the regulatory light chain of myosin (MLC) has roles in cardiac function. In vitro, myosin phosphatase target subunit 2 (MYPT2) is a strongly suspected regulatory subunit of cardiac myosin phosphatase (MP), but there is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52ff5f550d88c0ebbb4bad222412f7ed
https://doi.org/10.1253/circj.cj-09-0462
https://doi.org/10.1253/circj.cj-09-0462
Publikováno v:
Journal of Biological Chemistry. 284:18015-18020
Molluscan smooth muscles exhibit a low energy cost contraction called catch. Catch is regulated by twitchin phosphorylation and dephosphorylation. Recently, we found that the D2 fragment of twitchin containing the D2 site (Ser-4316) and flanking immu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6f838e34ebcfd0668fb95136bc68397
https://doi.org/10.1074/jbc.m109.016485
https://doi.org/10.1074/jbc.m109.016485
Autor:
Yoshihiko Yamakita, Kozo Kaibuchi, Go Totsukawa, Hidemasa Goto, David J. Hartshorne, Shigeko Yamashiro, Fumio Matsumura, Masaaki Ito
Publikováno v:
Developmental Cell. 14:787-797
Myosin phosphatase-targeting subunit 1 (MYPT1) binds to the catalytic subunit of protein phosphatase 1 (PP1C). This binding is believed to target PP1C to specific substrates including myosin II, thus controlling cellular contractility. Surprisingly,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8b8dd03d918f12313ed7faaced0ca8a
https://doi.org/10.1016/j.devcel.2008.02.013
https://doi.org/10.1016/j.devcel.2008.02.013
Autor:
David J. Hartshorne, Fumio Matsumura
Publikováno v:
Biochemical and Biophysical Research Communications. 369:149-156
Phosphorylation of myosin II is important in many aspects of cell function and involves a myosin kinase, e.g. myosin light chain kinase, and a myosin phosphatase (MP). MP is regulated by the myosin phosphatase target subunit (MYPT1). The domain struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0486e108adcb365d42625def797ef587
https://doi.org/10.1016/j.bbrc.2007.12.090
https://doi.org/10.1016/j.bbrc.2007.12.090
Autor:
Shugo Watabe, Daisuke Funabara, David J. Hartshorne, Miki Ueda, Koji Yamamoto, Satoshi Kanoh, Chieko Hamamoto, Akinori Inoue, Suechika Suzuki, Rika Osawa
Publikováno v:
Journal of Experimental Biology. 210:4399-4410
SUMMARY Molluscan smooth muscle can maintain tension over extended periods with little energy expenditure, a process termed catch. Catch is thought to be regulated by phosphorylation of a thick filament protein, twitchin, and involves two phosphoryla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b31af2a898225fdc7ca0eed19fb3447
https://doi.org/10.1242/jeb.008722
https://doi.org/10.1242/jeb.008722
Autor:
Katsuhisa Konishi, Satoshi Fujita, David J. Hartshorne, Kaoru Dohi, Itaru Goto, Masaya Taniguchi, Masaaki Ito, Ryuji Okamoto, Hideo Mizutani, Takeo Itoh
Publikováno v:
PLoS ONE
PLoS ONE, Vol 10, Iss 10, p e0141130 (2015)
PLoS ONE, Vol 10, Iss 10, p e0141130 (2015)
Background & Aims Cardiac myosin light chain kinase (cMLCK) plays an obligatory role in maintaining the phosphorylation levels of regulatory myosin light chain (MLC2), which is thought to be crucial for regulation of cardiac function. To test this hy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e68b45f9551380e23a554d0da098a162
http://europepmc.org/articles/PMC4626101
http://europepmc.org/articles/PMC4626101
Autor:
Akira Mizoguchi, Tetsuya Nakakuki, Ryuji Okamoto, David J. Hartshorne, Zhaojiang Lu, Takaaki Kato, Kozo Kaibuchi, Nobuaki Takahashi, Kyoko Imanaka-Yoshida, Terenc Tao, Naoki Isaka, Takeshi Nakano, Masaaki Ito, Katsuhide Mabuchi, Hideo Mizutani
Publikováno v:
Cellular Signalling. 18:1408-1416
Characterization of cardiac MYPT2 (an isoform of the smooth muscle phosphatase [MP] target subunit, MYPT1) is described. Several features of MYPT2 and MYPT1 were similar, including: a specific interaction with the catalytic subunit of type 1 phosphat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52be31172e8a38f92276eaac933c2776
https://doi.org/10.1016/j.cellsig.2005.11.001
https://doi.org/10.1016/j.cellsig.2005.11.001
Autor:
Shugo Watabe, David J. Hartshorne, Tom Butler, Satoshi Kanoh, Daisuke Funabara, Marion J. Siegman
Publikováno v:
Journal of Muscle Research and Cell Motility. 26:455-460
Molluscan catch muscle can maintain tension for a long time with little energy consumption. This unique phenomenon is regulated by phosphorylation and dephosphorylation of twitchin, a member of the titin/connectin family. The catch state is induced b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48481b206c77499bd8ace7cf069fbf1d
https://doi.org/10.1007/s10974-005-9029-2
https://doi.org/10.1007/s10974-005-9029-2
Publikováno v:
Cellular Signalling. 17:1265-1275
It was determined that the myosin phosphatase (MP) activity and content of myosin phosphatase target subunit 1 (MYPT1) were correlated in subcellular fractions of human hepatocarcinoma (HepG2) cells. In control cells MYPT1 was localized in the cytopl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d63aa2b62d6c75aaa8360a8c5c4b3410
https://doi.org/10.1016/j.cellsig.2005.01.008
https://doi.org/10.1016/j.cellsig.2005.01.008