Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Maki, Yoshio"'
Autor:
Ryota Ibusuki, Tatsuya Morishita, Akane Furuta, Shintaro Nakayama, Maki Yoshio, Hiroaki Kojima, Kazuhiro Oiwa, Ken’ya Furuta
Publikováno v:
Science
Intracellular transport is the basis of microscale logistics within cells and is powered by biomolecular motors. Mimicking transport for in vitro applications has been widely studied; however, the inflexibility in track design and control has hindere
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04674870749ae4dcf68d5d0d95e82554
https://pubmed.ncbi.nlm.nih.gov/35271310
https://pubmed.ncbi.nlm.nih.gov/35271310
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 1987 May 01. 84(9), 2848-2852.
Externí odkaz:
https://www.jstor.org/stable/29282
Autor:
Ken'ya Furuta, Akane Furuta, Hiroaki Kojima, Kazuhiro Oiwa, Maki Yoshio, Misaki Shiraga, Ryota Ibusuki
Publikováno v:
Biochemical and biophysical research communications. 523(4)
Dynein motor proteins usually work as a group in vesicle transport, mitosis, and ciliary/flagellar beating inside cells. Despite the obvious importance of the functions of dynein, the effect of inter-dynein interactions on collective motility remains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::615f20133dfffe6a5aa6134f84e0b979
https://pubmed.ncbi.nlm.nih.gov/31973818
https://pubmed.ncbi.nlm.nih.gov/31973818
Autor:
Saika, Takashi, Nishiguchi, Jun, Tsushima, Tomoyasu, Nasu, Yasutomo, Nagai, Atsushi, Miyaji, Yoshiyuki, Maki, Yoshio, Akaeda, Teruaki, Saegusa, Michihisa, Kumon, Hiromi
Publikováno v:
In Urology 2004 63(5):848-852
Publikováno v:
Nature Nanotechnology. 12:233-237
Biomolecular motors such as myosin, kinesin and dynein are protein machines that can drive directional movement along cytoskeletal tracks and have the potential to be used as molecule-sized actuators. Although control of the velocity and directionali
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::108c2bba0dd7960c0ad24507013f5c32
https://doi.org/10.1038/nnano.2016.238
https://doi.org/10.1038/nnano.2016.238
Publikováno v:
Journal of Muscle Research and Cell Motility. 34:115-123
Molluscan muscle twitchin, a titin/connectin-related giant protein, regulates interactions between actin and myosin filaments at low Ca(2+) concentrations. When it is dephosphorylated, actin filaments tightly bind to myosin filaments, resulting in th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16efe45c31416e2932ddcd1b1d61438c
https://doi.org/10.1007/s10974-013-9339-8
https://doi.org/10.1007/s10974-013-9339-8
Publikováno v:
Journal of Molecular Biology. 365:325-332
Catch muscles are found in some invertebrates which can maintain high passive tension with little energy expenditure for long periods after their active contraction. Twitchin in the catch muscles has the ability to facilitate the tight binding of thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c495bb0364298494a57111f99cfdb1e
https://doi.org/10.1016/j.jmb.2006.10.006
https://doi.org/10.1016/j.jmb.2006.10.006
Autor:
Himadri B. Pakrasi, Hirokazu Egashira, Kazuhiko Satoh, Masahiko Ikeuchi, Maki Yoshio, Hiroyuki Koike, Yasuhiro Kashino
Publikováno v:
Plant and Cell Physiology. 43:1366-1373
Using a recently introduced electrophoresis system [Kashino et al. (2001) Electrophoresis 22: 1004], components of low-molecular-mass polypeptides were analyzed in detail in photosystem II (PSII) complexes isolated from athermophilic cyanobacterium,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7ca64a152a08714c63670cc5d05054c
https://doi.org/10.1093/pcp/pcf168
https://doi.org/10.1093/pcp/pcf168
Publikováno v:
Proceedings of the National Academy of Sciences. 98:6635-6640
“Catch,” a state where some invertebrate muscles sustain high tension over long periods of time with little energy expenditure (low ATP hydrolysis rate) is similar to the “latch” state of vertebrate smooth muscles. Its induction and release i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2877462a4c28f220b4018edd25067007
https://doi.org/10.1073/pnas.111585098
https://doi.org/10.1073/pnas.111585098
Publikováno v:
Journal of Molecular Biology. 295:169-178
Molluscan catch muscles contain polypeptides of 110–120 kDa in size which have the same partial amino acid sequences as those of the myosin heavy chain (MHC). Here we provide evidence that these polypeptides are major components only of the catch-t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba46f3529c37c599560e48d59715f669
https://doi.org/10.1006/jmbi.1999.3349
https://doi.org/10.1006/jmbi.1999.3349