Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Karla Camacho Soto"'
Autor:
Christopher K. Prier, Karla Camacho Soto, Jacob H. Forstater, Nadine Kuhl, Jeffrey T. Kuethe, Wai Ling Cheung-Lee, Michael J. Di Maso, Claire M. Eberle, Shane T. Grosser, Hsing-I Ho, Erik Hoyt, Anne Maguire, Kevin M. Maloney, Amanda Makarewicz, Jonathan P. McMullen, Jeffrey C. Moore, Grant S. Murphy, Karthik Narsimhan, Weilan Pan, Nelo R. Rivera, Anumita Saha-Shah, David A. Thaisrivongs, Deeptak Verma, Adeya Wyatt, Daniel Zewge
Publikováno v:
ACS Catalysis. :7707-7714
Enzymes are capable of unique and selective transformations that can enable sustainable chemical production. While many industrial processes have been developed using free enzymes in aqueous solutions, immobilizing enzymes on a solid support can offe
Publikováno v:
Journal of the American Chemical Society. 136:17078-17086
Protein kinases phosphorylate client proteins, while protein phosphatases catalyze their dephosphorylation and thereby in concert exert reversible control over numerous signal transduction pathways. We have recently reported the design and validation
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1248
Protein kinases are implicated in diverse signaling cascades and have been targeted with small molecules that typically bind the conserved ATP-binding active site. These inhibitors are often promiscuous and target multiple protein kinases, which has
Publikováno v:
Peptide Libraries ISBN: 9781493920198
Protein kinases are implicated in diverse signaling cascades and have been targeted with small molecules that typically bind the conserved ATP-binding active site. These inhibitors are often promiscuous and target multiple protein kinases, which has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a6c78b953fce3891db7a439a528bffc4
https://doi.org/10.1007/978-1-4939-2020-4_7
https://doi.org/10.1007/978-1-4939-2020-4_7
Publikováno v:
Journal of the American Chemical Society. 136(10)
The activity of protein kinases are naturally gated by a variety of physiochemical inputs, such as phosphorylation, metal ions, and small molecules. In order to design protein kinases that can be gated by user-defined inputs, we describe a sequence d
We have previously reported that 8-phenyl-2'-deoxyguanosine derivatives (8PhGs) are able to extract metal cations from an aqueous phase into an organic phase. Herein, we report on the ability of 8PhGs to transport metal cations across a bulk lipophil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66fd112f92ec662faf6e2ea47fd5c994
https://kar.kent.ac.uk/45235/1/nihms224307.pdf
https://kar.kent.ac.uk/45235/1/nihms224307.pdf