Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Eric W Lake"'
Autor:
Emily F Ruff, Joseph M Muretta, Andrew R Thompson, Eric W Lake, Soreen Cyphers, Steven K Albanese, Sonya M Hanson, Julie M Behr, David D Thomas, John D Chodera, Nicholas M Levinson
Publikováno v:
eLife, Vol 7 (2018)
Many eukaryotic protein kinases are activated by phosphorylation on a specific conserved residue in the regulatory activation loop, a post-translational modification thought to stabilize the active DFG-In state of the catalytic domain. Here we use a
Externí odkaz:
https://doaj.org/article/f6eb943b1d3d40128485f13e5dbe282f
Autor:
Obinna C. Ubah, Eric W. Lake, Gihan S. Gunaratne, Joseph P. Gallant, Marie Fernie, Austin J. Robertson, Jonathan S. Marchant, Tyler D. Bold, Ryan A. Langlois, William E. Matchett, Joshua M. Thiede, Ke Shi, Lulu Yin, Nicholas H. Moeller, Surajit Banerjee, Laura Ferguson, Marina Kovaleva, Andrew J. Porter, Hideki Aihara, Aaron M. LeBeau, Caroline J. Barelle
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Shark antibodies (Variable New Antigen Receptors, VNARs) are the smallest naturally occurring antibody fragments. Here, the authors screen a VNAR phage display library against the SARS-CoV2 receptor binding domain (RBD) and identify VNARs that neutra
Externí odkaz:
https://doaj.org/article/d533a0ef137944a582f18b4def8a849b
Autor:
Abir Majumdar, Damien M. Rasmussen, Erik B. Faber, Andrew R. Thompson, David D. Thomas, Joseph M. Muretta, Emily F. Ruff, Nicholas M. Levinson, Eric W. Lake
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Many drugs trigger changes to the structure of their target receptor upon binding. These conformational effects are thought to be an essential part of molecular recognition but have proven challenging to quantify. Using a high-throughput
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e7e838b277600ebbd4a0d0e15f08a2e
https://doi.org/10.1073/pnas.1811158115
https://doi.org/10.1073/pnas.1811158115
Autor:
Joseph M. Muretta, Steven K. Albanese, Sonya M. Hanson, David D. Thomas, John D. Chodera, Julie M. Behr, Andrew R. Thompson, Nicholas M. Levinson, Soreen Cyphers, Eric W. Lake, Emily F. Ruff
Publikováno v:
eLife
eLife, Vol 7 (2018)
eLife, Vol 7 (2018)
Many eukaryotic protein kinases are activated by phosphorylation on a specific conserved residue in the regulatory activation loop, a post-translational modification thought to stabilize the active DFG-In state of the catalytic domain. Here we use a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fae27425896dbff034463448cee527db
http://europepmc.org/articles/PMC5849412
http://europepmc.org/articles/PMC5849412