Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Taia S. Wu"'
Autor:
David Mavor, Kyle A. Barlow, Daniel Asarnow, Yuliya Birman, Derek Britain, Weilin Chen, Evan M. Green, Lillian R. Kenner, Bruk Mensa, Leanna S. Morinishi, Charlotte A. Nelson, Erin M. Poss, Pooja Suresh, Ruilin Tian, Taylor Arhar, Beatrice E. Ary, David P. Bauer, Ian D. Bergman, Rachel M. Brunetti, Cynthia M. Chio, Shizhong A. Dai, Miles S. Dickinson, Susanna K. Elledge, Cole V. M. Helsell, Nathan L. Hendel, Emily Kang, Nadja Kern, Matvei S. Khoroshkin, Lisa L. Kirkemo, Greyson R. Lewis, Kevin Lou, Wesley M. Marin, Alison M. Maxwell, Peter F. McTigue, Douglas Myers-Turnbull, Tamas L. Nagy, Andrew M. Natale, Keely Oltion, Sergei Pourmal, Gabriel K. Reder, Nicholas J. Rettko, Peter J. Rohweder, Daniel M. C Schwarz, Sophia K. Tan, Paul V. Thomas, Ryan W. Tibble, Jason P. Town, Mary K. Tsai, Fatima S. Ugur, Douglas R. Wassarman, Alexander M. Wolff, Taia S. Wu, Derek Bogdanoff, Jennifer Li, Kurt S. Thorn, Shane O'Conchúir, Danielle L. Swaney, Eric D. Chow, Hiten D. Madhani, Sy Redding, Daniel N. Bolon, Tanja Kortemme, Joseph L. DeRisi, Martin Kampmann, James S. Fraser
Publikováno v:
Biology Open, Vol 7, Iss 7 (2018)
Although the primary protein sequence of ubiquitin (Ub) is extremely stable over evolutionary time, it is highly tolerant to mutation during selection experiments performed in the laboratory. We have proposed that this discrepancy results from the di
Externí odkaz:
https://doaj.org/article/120375a9425d4b15800ba82e59af4543
Autor:
Zun Zar Chi Naing, Maru Jaime-Garza, Taia S. Wu, Laurel S Estes, Martin Kampmann, Eric D. Chow, Taylor B. Cavazos, Miriam A. Goldman, Yessica K. Gomez, William F. DeGrado, Stephanie A. Wankowicz, Matthew C. Johnson, Christa Caggiano, Christina A. Stephens, Bryan Faust, Daniel Barrero, Lakshmi E. Miller-Vedam, Elizabeth E. McCarthy, Kyle E. Lopez, Sy Redding, Jenna Pellegrino, Elissa A Fink, Wren Saylor, Alison M Maxwell, Hayarpi Torosyan, Jared Lumpe, Robert W. Newberry, George C. Hartoularos, Daniel M. C. Schwarz, Calla Martyn, Laura M. Gunsalus, Jack Strickland, Maureen Pittman, Taylor Arhar, Andrew F. Kung, Daniel R. Wong, Garrett Wong, Nishith R. Reddy, Matthew G. Jones, Aji Palar, Erik J. Navarro, Nick Hoppe, M. Grace Gordon, Douglas R. Wassarman, Jean Costello, Adam Catching
Publikováno v:
ACS Chem Biol
ACS chemical biology, vol 15, iss 8
ACS chemical biology, vol 15, iss 8
Protein conformations are shaped by cellular environments, but how environmental changes alter the conformational landscapes of specific proteins in vivo remains largely uncharacterized, in part due to the challenge of probing protein structures in l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8292e5bf8e0f1174d79b4faba3fc334b
Autor:
Delaney Osborn, Taia S. Wu, Jennifer N. Rauch, Oleta T. Johnson, Leah N. Makley, Jason E. Gestwicki, Heather A. Carlson, Phani Ghanakota, Tomasz Cierpicki
Publikováno v:
Bioorg Med Chem
Destabilizing mutations in small heat shock proteins (sHsps) are linked to multiple diseases; however, sHsps are conformationally dynamic, lack enzymatic function and have no endogenous chemical ligands. These factors render sHsps as classically “u
Autor:
Danielle L. Swaney, Alexander M. Wolff, Tamas L. Nagy, Douglas Myers-Turnbull, Douglas R. Wassarman, Kyle A. Barlow, Paul V. Thomas, Rachel M. Brunetti, Derek Britain, Kevin Lou, Sy Redding, Wesley M. Marin, Mary K. Tsai, Kurt S. Thorn, Ryan W. Tibble, Lillian R. Kenner, Daniel M. C. Schwarz, Charlotte A. Nelson, Bruk Mensa, Fatima S. Ugur, Derek Bogdanoff, Taia S. Wu, E. Kang, Nicholas J. Rettko, Leanna S. Morinishi, Peter F. McTigue, Martin Kampmann, Gabriel K. Reder, Eric D. Chow, Alison M Maxwell, Jason Town, James S. Fraser, Andrew M. Natale, David P. Bauer, Cole Helsell, Joseph L. DeRisi, Yuliya Birman, Pooja Suresh, Evan M. Green, Ruilin Tian, Jennifer Y. Li, Sergei Pourmal, Weilin Chen, Hiten D. Madhani, Daniel N. Bolon, Miles Sasha Dickinson, Shane O’Conchúir, Keely Oltion, Daniel Asarnow, Peter J. Rohweder, Susanna K. Elledge, David Mavor, Erin M. Poss, Matvei S. Khoroshkin, Beatrice Ary, Ian D. Bergman, Nadja Kern, Taylor Arhar, Lisa L. Kirkemo, Tanja Kortemme, Sophia K. Tan, Shizhong Dai, Greyson R. Lewis, Nathan L. Hendel, Cynthia M. Chio
Publikováno v:
Biology Open
Biology open, vol 7, iss 7
Biology Open, Vol 7, Iss 7 (2018)
Mavor, D; Barlow, KA; Asarnow, D; Birman, Y; Britain, D; Chen, W; et al.(2018). Extending chemical perturbations of the ubiquitin fitness landscape in a classroom setting reveals new constraints on sequence tolerance. BIOLOGY OPEN, 7(7). doi: 10.1242/bio.036103. UCSF: Retrieved from: http://www.escholarship.org/uc/item/2hz894gr
Biology open, vol 7, iss 7
Biology Open, Vol 7, Iss 7 (2018)
Mavor, D; Barlow, KA; Asarnow, D; Birman, Y; Britain, D; Chen, W; et al.(2018). Extending chemical perturbations of the ubiquitin fitness landscape in a classroom setting reveals new constraints on sequence tolerance. BIOLOGY OPEN, 7(7). doi: 10.1242/bio.036103. UCSF: Retrieved from: http://www.escholarship.org/uc/item/2hz894gr
Although the primary protein sequence of ubiquitin (Ub) is extremely stable over evolutionary time, it is highly tolerant to mutation during selection experiments performed in the laboratory. We have proposed that this discrepancy results from the di
Autor:
Aaron M. Leconte, Charlotte E. Morrissey, Colin M. Rathbun, Gabriela V. Ochoa, Marya Y. Ornelas, Taia S. Wu, Jennifer A. Prescher, Mira D. Liu, Elliot A. Warner, Caitlyn W. Fick, Brendan S. Zhang, William B. Porterfield
Publikováno v:
Biochemistry, vol 57, iss 5
Directed evolution has proven to be an invaluable tool for protein engineering; however, there is still a need for developing new approaches to continue to improve the efficiency and efficacy of these methods. Here, we demonstrate a new method for li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d41731eaed5b93ba06d6a41e3fff94f5
https://europepmc.org/articles/PMC6192264/
https://europepmc.org/articles/PMC6192264/
Autor:
Chelsea G. Gordon, Frederick M. Tomlin, Taia S. Wu, Yisu Han, Carolyn R. Bertozzi, Ellen M. Sletten
Publikováno v:
Bioorganicmedicinal chemistry. 26(19)
The quadricyclane (QC) ligation is a bioorthogonal reaction between a quadricyclane moiety and a nickel bis(dithiolene) derivative. Here we show that a QC amino acid can be incorporated into a protein site-specifically using the pyrrolysine-based gen