Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Aaron J. Cantor"'
Publikováno v:
Cantor, AJ; Shah, NH; & Kuriyan, J. (2018). Deep mutational analysis reveals functional trade-offs in the sequences of EGFR autophosphorylation sites. Proceedings of the National Academy of Sciences of the United States of America, 115(31), E7303-E7312. doi: 10.1073/pnas.1803598115. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/7nb1t9db
Proceedings of the National Academy of Sciences of the United States of America, vol 115, iss 31
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, vol 115, iss 31
Proceedings of the National Academy of Sciences of the United States of America
Significance Phosphorylation of tyrosine residues in the cytoplasmic tail of the epidermal growth factor receptor (EGFR) by its kinase domain propagates a rich variety of information downstream of growth factor binding. The amino acid sequences surro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa3a59e4050fcfc0ebc1f9bd1289e528
https://doi.org/10.1073/pnas.1803598115
https://doi.org/10.1073/pnas.1803598115
Autor:
Eric R. Goedken, Mike O'Donnell, Kyle R. Simonetta, Steven N. Seyedin, John Kuriyan, Debora L. Makino, Brian A. Kelch, Aaron J. Cantor, Randall McNally, Steven L. Kazmirski
Publikováno v:
Cell. 137:659-671
SummaryClamp loaders load sliding clamps onto primer-template DNA. The structure of the E. coli clamp loader bound to DNA reveals the formation of an ATP-dependent spiral of ATPase domains that tracks only the template strand, allowing recognition of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdc8432dc4e910c11b76df9ba221f162
https://doi.org/10.1016/j.cell.2009.03.044
https://doi.org/10.1016/j.cell.2009.03.044
Autor:
Arthur R. Salomon, Aaron J. Cantor, Qinqin Ji, Debra A. Cheng, John Kuriyan, Theresa A. Kadlecek, Hanna Sjolin-Goodfellow, Arup K. Chakraborty, Arthur Weiss, Maria P. Frushicheva
Publikováno v:
Science signaling, vol 8, iss 377
Sjölin-Goodfellow, H; Frushicheva, MP; Ji, Q; Cheng, DA; Kadlecek, TA; Cantor, AJ; et al.(2015). The catalytic activity of the kinase ZAP-70 mediates basal signaling and negative feedback of the T cell receptor pathway. Science Signaling, 8(377), ra49. doi: 10.1126/scisignal.2005596. UCSF: Retrieved from: http://www.escholarship.org/uc/item/9rz7n24s
PMC
Sjölin-Goodfellow, H; Frushicheva, MP; Ji, Q; Cheng, DA; Kadlecek, TA; Cantor, AJ; et al.(2015). The catalytic activity of the kinase ZAP-70 mediates basal signaling and negative feedback of the T cell receptor pathway. Science Signaling, 8(377), ra49. doi: 10.1126/scisignal.2005596. UCSF: Retrieved from: http://www.escholarship.org/uc/item/9rz7n24s
PMC
T cell activation by antigens binding to the T cell receptor (TCR) must be properly regulated to ensure normal T cell development and effective immune responses to pathogens and transformed cells while avoiding autoimmunity. The Src family kinase Lck
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6445e5638c26fe8399c2290a7e56201b
https://escholarship.org/uc/item/9rz7n24s
https://escholarship.org/uc/item/9rz7n24s
Autor:
Qi Wang, Rahul Das, Aaron J. Cantor, John Kuriyan, Kathryn Wong, Patricia Grob, Ron Bose, Tiago Barros, Yongjian Huang, Amar Mirza, Natalia Jura, Erika Kovacs, Timothy S. Collier
Publikováno v:
Kovacs, E; Das, R; Wang, Q; Collier, TS; Cantor, A; Huang, Y; et al.(2015). Analysis of the role of the C-terminal tail in the regulation of the epidermal growth factor receptor. Molecular and Cellular Biology, 35(17), 3083-3102. doi: 10.1128/MCB.00248-15. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/5vt7d0ph
Molecular and cellular biology, vol 35, iss 17
Molecular and cellular biology, vol 35, iss 17
© 2015, American Society for Microbiology. The ~230-residue C-terminal tail of the epidermal growth factor receptor (EGFR) is phosphorylated upon activation. We examined whether this phosphorylation is affected by deletions within the tail and wheth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::371318f1699ea4754357121688758041
http://www.escholarship.org/uc/item/5vt7d0ph
http://www.escholarship.org/uc/item/5vt7d0ph
Publikováno v:
Trends in biochemical sciences. 39(10)
The activation of receptor tyrosine kinases in response to extracellular signals is a principal component of metazoan signaling. Structural analysis of the extracellular and intracellular domains of these receptors has shed substantial light on the m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a5fd0802ae4bf9fc013f9b19cdd18a0
https://pubmed.ncbi.nlm.nih.gov/25242369
https://pubmed.ncbi.nlm.nih.gov/25242369
Publikováno v:
BMC Biology
Lorenz, Sonja; Cantor, Aaron J; Rape, Michael; & Kuriyan, John. (2013). Macromolecular juggling by ubiquitylation enzymes. BMC Biology, 11(1), 65. doi: http://dx.doi.org/10.1186/1741-7007-11-65. Retrieved from: http://www.escholarship.org/uc/item/5dm6t06f
Lorenz, Sonja; Cantor, Aaron J; Rape, Michael; & Kuriyan, John. (2013). Macromolecular juggling by ubiquitylation enzymes. BMC Biology, 11(1), 65. doi: http://dx.doi.org/10.1186/1741-7007-11-65. Retrieved from: http://www.escholarship.org/uc/item/5dm6t06f
The posttranslational modification of target proteins with ubiquitin and ubiquitin-like proteins is accomplished by the sequential action of E1, E2, and E3 enzymes. Members of the E1 and E3 enzyme families can undergo particularly large conformationa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f86940527100829d801e53652bf9833a
http://europepmc.org/articles/PMC3748819
http://europepmc.org/articles/PMC3748819