Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Steven C. Bremmer"'
Autor:
Laurie L. Parker, Christie L. Eissler, Harry Charbonneau, Juan S. Martinez, Mark C. Hall, Steven C. Bremmer
Publikováno v:
Analytical Biochemistry. 418:267-275
The majority of eukaryotic proteins are phosphorylated in vivo and phosphorylation may be the most common regulatory post-translational modification. Many proteins are phosphorylated at numerous sites, often by multiple kinases, which may have differ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::006aaef8f0abd096d4c7937877a9c05d
https://doi.org/10.1016/j.ab.2011.07.015
https://doi.org/10.1016/j.ab.2011.07.015
Autor:
Dah-Eun Jeong, Anton Iliuk, Mark C. Hall, James T. Henderson, Harry Charbonneau, Eunyoung Choi, Steven C. Bremmer
Publikováno v:
Journal of Biological Chemistry. 283:10396-10407
The anaphase-promoting complex (APC) regulates the eukaryotic cell cycle by targeting specific proteins for proteasomal degradation. Its activity must be strictly controlled to ensure proper cell cycle progression. The co-activator proteins Cdc20 and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07170666c8b5fed728970055e1f8d786
https://doi.org/10.1074/jbc.m710011200
https://doi.org/10.1074/jbc.m710011200
Publikováno v:
Chemical communications (Cambridge, England). 50(14)
A generalizable method for detecting protease activity via gelation is described. A recognition sequence is used to target the protease of interest while a second protease is used to remove the residual residues from the gelator scaffold. Using this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6446d3873d675df2f014b9dc47b36e0
https://pubmed.ncbi.nlm.nih.gov/24394494
https://pubmed.ncbi.nlm.nih.gov/24394494
A modular system for detecting protease activity via enzyme-triggered gel formation is described. Protease-specific recognition sequences are utilized to achieve enzyme specificity. Artificial blood clotting is demonstrated by activating endogenous t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7a05e2241d19139bf96f84eb6feeb61
https://europepmc.org/articles/PMC3376645/
https://europepmc.org/articles/PMC3376645/
Autor:
Laurie L. Parker, Juan S. Martinez, Hana Hall, Harry Charbonneau, Sandra Rossie, Steven C. Bremmer, Mark C. Hall, Thomas H. Hinrichsen, Christie L. Eissler
Publikováno v:
The Journal of biological chemistry. 287(3)
Mitotic cell division is controlled by cyclin-dependent kinases (Cdks), which phosphorylate hundreds of protein substrates responsible for executing the division program. Cdk inactivation and reversal of Cdk-catalyzed phosphorylation are universal re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82cd9aab77db2f74fc3d69b99d1dafc5
https://pubmed.ncbi.nlm.nih.gov/22247558
https://pubmed.ncbi.nlm.nih.gov/22247558