Zobrazeno 1 - 10
of 90
pro vyhledávání: '"Atsushi, Yoshimori"'
Autor:
Kazuhiro Abe, Mami Ozako, Miki Inukai, Yoe Matsuyuki, Shinnosuke Kitayama, Chisato Kanai, Chiaki Nagai, Chai C. Gopalasingam, Christoph Gerle, Hideki Shigematsu, Nariyoshi Umekubo, Satoshi Yokoshima, Atsushi Yoshimori
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-14 (2023)
Abstract Existing drugs often suffer in their effectiveness due to detrimental side effects, low binding affinity or pharmacokinetic problems. This may be overcome by the development of distinct compounds. Here, we exploit the rich structural basis o
Externí odkaz:
https://doaj.org/article/cece4c3a0c2549c0b39e71717c9e426c
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-8 (2022)
Abstract New matrix metalloproteinase 1 (MMP-1) inhibitors were predicted using the structure–activity relationship (SAR) transfer method based on a series of analogues of kinesin-like protein 11 (KIF11) inhibitors. Compounds 5–7 predicted to be
Externí odkaz:
https://doaj.org/article/e3d1a7b258214a2e91f62651ec92278c
Autor:
Yasunobu Asawa, Saki Hatsuzawa, Atsushi Yoshimori, Kentaro Yamada, Akira Katoh, Hiroyuki Kouji, Hiroyuki Nakamura
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
Abstract A total of 42 trisubstituted carboranes categorised into five scaffolds were systematically designed and synthesized by exploiting the different reactivities of the twelve vertices of o-, m-, and p-carboranes to cover all directions in chemi
Externí odkaz:
https://doaj.org/article/5bfb1398b2014dceb687354cb4b37d37
Autor:
Hajime Takashima, Atsushi Yoshimori, Eiji Honda, Tomonori Taguri, Jun Ozawa, Masaji Kasai, Satoshi Shuto, Dai Takehara
Publikováno v:
ACS Omega, Vol 6, Iss 40, Pp 26601-26612 (2021)
Externí odkaz:
https://doaj.org/article/2f136a2a8e164a58908361d488e302f5
Autor:
Atsushi Yoshimori, Jürgen Bajorath
Publikováno v:
Future Science OA, Vol 8, Iss 7 (2022)
Externí odkaz:
https://doaj.org/article/5d41444c9d224f739792c403f518d3fc
Autor:
Atsushi Yoshimori, Jürgen Bajorath
Publikováno v:
Biomolecules, Vol 13, Iss 5, p 833 (2023)
In drug design, the prediction of new active compounds from protein sequence data has only been attempted in a few studies thus far. This prediction task is principally challenging because global protein sequence similarity has strong evolutional and
Externí odkaz:
https://doaj.org/article/aa2502292dd54a878a334fbc79eaf0a8
Autor:
Atsushi Yoshimori, Jürgen Bajorath
Publikováno v:
Artificial Intelligence in the Life Sciences, Vol 1, Iss , Pp 100015- (2021)
The Structure-Activity Relationship (SAR) Matrix (SARM) method systematically extracts structurally related compound series from any source and organizes these series in a unique data structure formed by matrices similar to R-group tables from medici
Externí odkaz:
https://doaj.org/article/ea2b97980c1d44638a7c008d98534de3
Autor:
Kumiko Tsuihiji, Eiji Honda, Kanehisa Kojoh, Shizue Katoh, Tomonori Taguri, Atsushi Yoshimori, Hajime Takashima
Publikováno v:
Pharmaceuticals, Vol 15, Iss 12, p 1506 (2022)
Currently, various pharmaceutical modalities are being developed rapidly. Targeting protein–protein interactions (PPIs) is an important objective in such development. Cyclic peptides, because they have good specificity and activity, have been attra
Externí odkaz:
https://doaj.org/article/08221a0e1c484e92919013e466985320
Publikováno v:
ACS Omega, Vol 4, Iss 4, Pp 7061-7069 (2019)
Externí odkaz:
https://doaj.org/article/c73d657ff244460d888952ff67a4d136
Autor:
Kohei, Umedera, Atsushi, Yoshimori, Hengwei, Chen, Hiroyuki, Kouji, Hiroyuki, Nakamura, Jürgen, Bajorath
Publikováno v:
Journal of Computer-Aided Molecular Design. 37:107-115
Mimicking bioactive conformations of peptide segments involved in the formation of protein-protein interfaces with small molecules is thought to represent a promising strategy for the design of protein-protein interaction (PPI) inhibitors. For compou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d7b51f18530530f2cdef786faec9fdd
https://doi.org/10.1007/s10822-022-00493-y
https://doi.org/10.1007/s10822-022-00493-y