Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Timothy P. Ikeda"'
Autor:
Rama Balakrishnan, Ellen L. Berg, Christopher C. Butler, Alex M. Clark, Sheryl P. Denker, Isabella Feierberg, Jason Harris, Timothy P. Ikeda, Samantha Jeschonek, Vladimir A. Makarov, Christopher Southan, Dana Vanderwall, Peter Winstanley
Publikováno v:
SLAS Discovery, Vol 29, Iss 8, Pp 100188- (2024)
We present a standardized metadata template for assays used in pharmaceutical drug discovery research, according to the FAIR principles. We also describe the use of an automated tool for annotating assays from a variety of sources, including PubChem,
Externí odkaz:
https://doaj.org/article/8b7a8009037942d7bdea6491991dfffb
Autor:
Neil P. Grimster, Lakshmaiah Gingipalli, Bernard Barlaam, Qibin Su, XiaoLan Zheng, David Watson, Haixia Wang, Iain Simpson, Andy Pike, Amber Balazs, Scott Boiko, Timothy P. Ikeda, Anna C. Impastato, Natalie H. Jones, Sameer Kawatkar, Paul Kemmitt, Scott Lamont, Joe Patel, Jon Read, Ujjal Sarkar, Li Sha, Ronald C. Tomlinson, Haiyun Wang, David M. Wilson, Troy E. Zehnder, Lianghe Wang, Peng Wang, Frederick W. Goldberg, Wenlin Shao, Stephen Fawell, Hannah Dry, James E. Dowling, Scott D. Edmondson
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 30:127433
Spleen tyrosine kinase (SYK) is a non-receptor cytosolic kinase. Due to its pivotal role in B cell receptor and Fc-receptor signaling, inhibition of SYK has been targeted in a variety of disease areas. Herein, we report the optimization of a series o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::300ccf0156daf617e8afd1d69c45160f
https://doi.org/10.1016/j.bmcl.2020.127433
https://doi.org/10.1016/j.bmcl.2020.127433
Publikováno v:
Journal of Biological Chemistry. 271:19124-19128
Isocitrate dehydrogenase (IDH) of Escherichia coli is regulated by a bifunctional protein, IDH kinase/phosphatase. In addition to the kinase and phosphatase activities, this protein catalyzes an intrinsic ATPase reaction. The initial velocity kinetic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::07b6326d7bc67831fd7ea7345b6f7b73
https://doi.org/10.1074/jbc.271.32.19124
https://doi.org/10.1074/jbc.271.32.19124
In many bacteria, accumulation of K+ at high external osmolalities is accompanied by accumulation of glutamate. To determine whether there is an obligatory relationship between glutamate and K+ pools, we studied mutant strains of Salmonella typhimuri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7571599c5f29b738ccaace1be17d5a5a
https://europepmc.org/articles/PMC39057/
https://europepmc.org/articles/PMC39057/
Publikováno v:
Journal of molecular biology. 259(4)
Assimilation of nitrogen requires the synthesis of only two central intermediates, glutamate and glutamine, from which other compounds derive nitrogen by secondary transfers. We measured the internal pool sizes of glutamate and glutamine in Salmonell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70e9747039f5879dfd95d5e1c6ab2891
https://pubmed.ncbi.nlm.nih.gov/8683567
https://pubmed.ncbi.nlm.nih.gov/8683567
Publikováno v:
Journal of Biological Chemistry. 264:13775-13779
In Escherichia coli, the reversible phosphorylation of isocitrate dehydrogenase (IDH) is catalyzed by a bifunctional protein: IDH kinase/phosphatase. Although both IDH kinase and IDH phosphatase require ATP, the amino acid sequence of IDH kinase/phos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0321556cd68a56a1b88656a348d9396c
https://doi.org/10.1016/s0021-9258(18)80068-0
https://doi.org/10.1016/s0021-9258(18)80068-0
Publikováno v:
Biochimie. 71(9-10)
In Escherichia coli , isocitrate dehydrogenase (IDH) is regulated by phosphorylation. This phosphorylation cycle is catalyzed by an unusual, bifunctional protein: IDH kinase/phosphatase. IDH kinase/phosphatase is expressed from a single gene, aceK ,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb242a91ddbc2fbc9a0af9ceed6532c8
https://pubmed.ncbi.nlm.nih.gov/2557093
https://pubmed.ncbi.nlm.nih.gov/2557093