Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Kayo Umetani"'
Autor:
Yoshiji Hantani, Kiyosei Iio, Rie Hantani, Kayo Umetani, Toshihiro Sato, Tracy Young, Katelyn Connell, Sam Kintz, Joshua Salafsky
Publikováno v:
FEBS Open Bio, Vol 8, Iss 9, Pp 1412-1423 (2018)
Many clinically approved protein kinase inhibitors stabilize an inactive conformation of their kinase target. Such inhibitors are generally highly selective compared to active conformation inhibitors, and consequently, general methods to identify inh
Externí odkaz:
https://doaj.org/article/8d0437040b1b4dbdb797c18f711baa16
Autor:
Tomohisa Yamamoto, Toshiki Urashima, Kumiko Ayukawa, Fuminori Tokunaga, Daisuke Oikawa, Yuji Hori, Masahiro Tamaru, Tomomi Kinoshita, Kayo Umetani, Ken Katsuya
Publikováno v:
SLAS Discovery. 23:1018-1029
The nuclear factor κB (NF-κB) pathway is critical for regulating immune and inflammatory responses, and uncontrolled NF-κB activation is closely associated with various inflammatory diseases and malignant tumors. The Met1-linked linear ubiquitin c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b50a2fb899c78a722ef857333734299
https://doi.org/10.1177/2472555218793066
https://doi.org/10.1177/2472555218793066
Autor:
Tracy A. Young, Toshihiro Sato, Sam Kintz, Kayo Umetani, Kiyosei Iio, Rie Hantani, Joshua Salafsky, Yoshiji Hantani, Katelyn Connell
Publikováno v:
FEBS Open Bio
Many clinically approved protein kinase inhibitors stabilize an inactive conformation of their kinase target. Such inhibitors are generally highly selective compared to active conformation inhibitors, and consequently, general methods to identify inh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7635a31bde6e39756a249e1ddbc85cf7
https://doi.org/10.1002/2211-5463.12489
https://doi.org/10.1002/2211-5463.12489
Publikováno v:
SLAS discovery : advancing life sciences RD. 24(8)
Interleukin-2-inducible T-cell kinase (ITK) plays an important role in T-cell signaling and is considered a promising drug target. As the ATP binding sites of protein kinases are highly conserved, the design of selective kinase inhibitors remains a c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbcb51755cfe1e29d74a9a8126925cf3
https://pubmed.ncbi.nlm.nih.gov/31247148
https://pubmed.ncbi.nlm.nih.gov/31247148