Zobrazeno 1 - 10
of 105
pro vyhledávání: '"Tomohiro Shima"'
Publikováno v:
FEBS Open Bio, Vol 13, Iss 9, Pp 1667-1682 (2023)
Telomerase reverse transcriptase (TERT) is a protein that catalyzes the reverse transcription of telomere elongation. TERT is also expected to play a non‐canonical role beyond telomere lengthening since it localizes not only in the nucleus but also
Externí odkaz:
https://doaj.org/article/1ac1e0abd9f3499e9f1615ef8800c3a9
Publikováno v:
BMC Biology, Vol 21, Iss 1, Pp 1-12 (2023)
Abstract Background Argonaute proteins play a central role in RNA silencing by forming protein-small RNA complexes responsible for the silencing process. While most Argonaute proteins have a short N-terminal region, Argonaute2 in Drosophila melanogas
Externí odkaz:
https://doaj.org/article/7cdc5f5d4d4d492ab88073e05cf719a9
Autor:
Tomohiro Shima, Kumiko Hayashi
Publikováno v:
Biophysics and Physicobiology, Vol 20 (2023)
Externí odkaz:
https://doaj.org/article/0654e5f02011444084f669987e6a623c
Autor:
Junichi Kaneshiro, Yasushi Okada, Tomohiro Shima, Mika Tsujii, Katsumi Imada, Taro Ichimura, Tomonobu M. Watanabe
Publikováno v:
Biophysics and Physicobiology, Vol 16 (2019)
Cryo-electron microscopy and X-ray crystallography have been the major tools of protein structure analysis for decades and will certainly continue to be essential in the future. Moreover, nuclear magnetic resonance or Förster resonance energy transf
Externí odkaz:
https://doaj.org/article/2ff10fd8b62a4b01b74529d1d40bb72e
Preference of CAMSAP3 for expanded microtubule lattice contributes to stabilization of the minus end
Autor:
Hanjin Liu, Tomohiro Shima
CAMSAPs are proteins that show microtubule minus-end-specific localization, decoration and stabilization. Although the mechanism for minus-end recognition via their C-terminal CKK domain has been well described in recent studies, it is unclear how CA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edecf506935dece254c5e6b5bcfe0724
https://doi.org/10.1101/2022.08.21.504720
https://doi.org/10.1101/2022.08.21.504720
Argonaute proteins play a central role in RNA silencing by forming protein-small RNA complexes responsible for the silencing process. While most Argonaute proteins have a short N-terminal region, Argonaute2 in Drosophila melanogaster (DmAgo2) harbors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::527e8271be144a810c4b05353da78cd1
https://doi.org/10.1101/2022.08.05.502916
https://doi.org/10.1101/2022.08.05.502916
Publikováno v:
Biophys J
Cytoplasmic dynein is a two-headed molecular motor that moves to the minus end of a microtubule by ATP hydrolysis free energy. By employing its two heads (motor domains), cytoplasmic dynein exhibits various bipedal stepping motions: inchworm and hand
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b71efa00ea1041dd65c6cfc8042a51c4
https://doi.org/10.1016/j.bpj.2020.03.012
https://doi.org/10.1016/j.bpj.2020.03.012
Small stepping motion of processive dynein revealed by load-free high-speed single-particle tracking
Autor:
Mayuko Yamamoto, Takahide Kon, Riko Kanazawa, Tomohiro Shima, Rieko Shimo-Kon, Akihiko Nakamura, Ryota Iino, Jun Ando
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
Scientific Reports
Scientific Reports
Cytoplasmic dynein is a dimeric motor protein which processively moves along microtubule. Its motor domain (head) hydrolyzes ATP and induces conformational changes of linker, stalk, and microtubule binding domain (MTBD) to trigger stepping motion. He
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9da992958efa1a71df14fb9ff7ecbc8c
http://link.springer.com/article/10.1038/s41598-020-58070-y
http://link.springer.com/article/10.1038/s41598-020-58070-y
Cytoplasmic dynein 1 is almost exclusively responsible for intracellular transport toward the minus-end of microtubules in animal cells. One of the key factors for the unidirectional movement of dynein is the asymmetry of the unbinding of the motor f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cabc2d3691e3d785628e9fd1eac6d03a
https://doi.org/10.1101/2022.03.27.485981
https://doi.org/10.1101/2022.03.27.485981
Telomerase reverse transcriptase (TERT) is a protein that catalyzes the reverse transcription of telomere elongation. TERT is also expected to play a noncanonical role beyond telomere lengthening since it localizes not only in the nucleus but also in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::86b44412ce99e4a01356fcbde8dae55d
https://doi.org/10.1101/2021.12.21.473585
https://doi.org/10.1101/2021.12.21.473585