Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Shingo Fukuda"'
Autor:
Diego Carlero, Shingo Fukuda, Bocanegra, Rebeca, Ando, Toshio, Martin-Benito, Jaime, Ibarra, Borja
Publikováno v:
ACS Nano; 7/30/2024, Vol. 18 Issue 30, p19518-19527, 10p
Publikováno v:
Proceedings of the Combustion Institute.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6b09d0f26eccc76b0c9dead620792044
https://doi.org/10.1016/j.proci.2022.08.038
https://doi.org/10.1016/j.proci.2022.08.038
Autor:
Kenta Saito, Kaori Ohkoda, Hideharu Amano, Shingo Fukuda, Seiya Kasai, Ying Jie Yan, Masashi Aono
Publikováno v:
2021 International Conference on Field-Programmable Technology (ICFPT).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1ec21c54fbb530f408c0752e2b8166b4
https://doi.org/10.1109/icfpt52863.2021.9609882
https://doi.org/10.1109/icfpt52863.2021.9609882
Autor:
Shuhei Fuyuta, Takayuki Kawano, Mika Kitajima, Yukiko Ueno, Nobuhiro Inoue, Hiroyuki Sueyoshi, Tomomi Ikeda, Yusuke Kakizoe, Michiya Iwata, Shingo Fukuda, Osamu Kobayashi
Publikováno v:
Journal of Neurological Research And Therapy. 2:17-22
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::469288d0bd979d7c6cd33bf1b23005e0
https://doi.org/10.14302/issn.2470-5020.jnrt-17-1733
https://doi.org/10.14302/issn.2470-5020.jnrt-17-1733
Publikováno v:
Biophysical Journal
Thylakoid membranes in chloroplasts contain photosynthetic protein complexes that convert light energy into chemical energy. Photosynthetic protein complexes are considered to undergo structural reorganization to maintain the efficiency of photochemi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8baf6bd7181d73ed9eac4f1b51d50d5
https://pubmed.ncbi.nlm.nih.gov/32224302
https://pubmed.ncbi.nlm.nih.gov/32224302
Publikováno v:
Biochimica et biophysica acta. General subjects. 1864(2)
Background High-speed atomic force microscopy (HS-AFM) has successfully visualized a variety of protein molecules during their functional activity. However, it cannot visualize small molecules interacting with proteins and even protein molecules when
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23cfed5e6620c89a40e652a58c72e29e
https://pubmed.ncbi.nlm.nih.gov/30890438
https://pubmed.ncbi.nlm.nih.gov/30890438
Autor:
Shingo Fukuda, Toshio Ando
Publikováno v:
Review of Scientific Instruments. 92:033705
High-speed atomic force microscopy (HS-AFM) has enabled observing protein molecules during their functional activity at rates of 1-12.5 frames per second (fps), depending on the imaging conditions, sample height, and fragility. To meet the increasing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b256fc350d6473e24bdc1895149db944
https://doi.org/10.1063/5.0032948
https://doi.org/10.1063/5.0032948
Publikováno v:
The Proceedings of Conference of Kanto Branch. :10A12
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::84c742166527fb61e58b71318d402b4d
https://doi.org/10.1299/jsmekanto.2021.27.10a12
https://doi.org/10.1299/jsmekanto.2021.27.10a12
Publikováno v:
Ultramicroscopy. 160:182-196
High-speed atomic force microscopy (HS-AFM) has been established and used, which can visualize biomolecules in dynamic action at high spatiotemporal resolution without disturbing their function. Various studies conducted in the past few years have de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93b630a06265e4fa61a9628be6e4b302
https://doi.org/10.1016/j.ultramic.2015.10.017
https://doi.org/10.1016/j.ultramic.2015.10.017
Publikováno v:
Molecular cell. 77(2)
The signal recognition particle (SRP), responsible for co-translational protein targeting and delivery to cellular membranes, depends on the native long-hairpin fold of its RNA to confer functionality. Since RNA initiates folding during its synthesis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39059bd170eb3ca286f72b9b6c7320fc
https://pubmed.ncbi.nlm.nih.gov/31706702
https://pubmed.ncbi.nlm.nih.gov/31706702