Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Brett T. Staahl"'
Autor:
Arik Shams, Sean A. Higgins, Christof Fellmann, Thomas G. Laughlin, Benjamin L. Oakes, Rachel Lew, Shin Kim, Maria Lukarska, Madeline Arnold, Brett T. Staahl, Jennifer A. Doudna, David F. Savage
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Proteins evolve through the modular rearrangement of domains. Here the authors introduce MISER, a minimization by iterative size-exclusion and recombination method to make all possible deletions of a protein, uncovering functions for Cas9 domains inv
Externí odkaz:
https://doaj.org/article/f92b1a4bf0574fe9b95344d8bcec8e40
Autor:
Marco J. Lobba, Christof Fellmann, Alan M. Marmelstein, Johnathan C. Maza, Elijah N. Kissman, Stephanie A. Robinson, Brett T. Staahl, Cole Urnes, Rachel J. Lew, Casey S. Mogilevsky, Jennifer A. Doudna, Matthew B. Francis
Publikováno v:
ACS Central Science, Vol 6, Iss 9, Pp 1564-1571 (2020)
Externí odkaz:
https://doaj.org/article/717bb74132f54986ad0e5c0d11e24c37
Autor:
Lucas B. Harrington, David Paez-Espino, Brett T. Staahl, Janice S. Chen, Enbo Ma, Nikos C. Kyrpides, Jennifer A. Doudna
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-8 (2017)
While current CRISPR-Cas9 tools have revolutionized genome editing, they are not suitable for applications at elevated temperatures. Here, the authors characterize GeoCas9 from Geobacillus stearothermophilus, which is active up to 70°C and is stable
Externí odkaz:
https://doaj.org/article/5515b76d1431477696220e607e0ddca5
Autor:
Rachel J. Lew, Christof Fellmann, Thomas G. Laughlin, Arik Shams, Benjamin L. Oakes, Maria Lukarska, David F. Savage, Jennifer A. Doudna, Brett T. Staahl, Shin Kim, Sean Higgins, Madeline L. Arnold
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Nature Communications
Nature Communications
Proteins evolve through the modular rearrangement of elements known as domains. Extant, multidomain proteins are hypothesized to be the result of domain accretion, but there has been limited experimental validation of this idea. Here, we introduce a
Autor:
Matthew B. Francis, Alan M. Marmelstein, Brett T. Staahl, Johnathan C. Maza, Stephanie A. Robinson, Elijah N Kissman, Marco J. Lobba, Casey S. Mogilevsky, Rachel J. Lew, Jennifer A. Doudna, Christof Fellmann, Cole Urnes
Publikováno v:
ACS Central Science, Vol 6, Iss 9, Pp 1564-1571 (2020)
ACS Central Science
ACS Central Science
The synthesis of protein–protein and protein–peptide conjugates is an important capability for producing vaccines, immunotherapeutics, and targeted delivery agents. Herein we show that the enzyme tyrosinase is capable of oxidizing exposed tyrosin
Publikováno v:
eLife, Vol 3 (2014)
The CRISPR/Cas9 system is a robust genome editing technology that works in human cells, animals and plants based on the RNA-programmed DNA cleaving activity of the Cas9 enzyme. Building on previous work (Jinek et al., 2013), we show here that new gen
Externí odkaz:
https://doaj.org/article/827b3586ab1e43eba0b9099d5b77271b
Autor:
Eva Nogales, Hannah Spinner, Jonathan Chuck, Basem Al-Shayeb, Natalia Orlova, Enbo Ma, Jun-Jie Liu, Gavin J. Knott, Jennifer A. Doudna, John J Desmarais, Brett T. Staahl, Katherine Baney, Alexander J. Wagner, Julian Brötzmann, Dan Tan, Lucas B. Harrington, Benjamin L. Oakes, Kian Taylor
Publikováno v:
Nature
The RNA-guided CRISPR-associated (Cas) proteins Cas9 and Cas12a provide adaptive immunity against invading nucleic acids, and function as powerful tools for genome editing in a wide range of organisms. Here we reveal the underlying mechanisms of a th
Autor:
David F. Savage, Benjamin L. Oakes, Rachel J. Lew, Christof Fellmann, Madeline L. Arnold, Maria Lukarska, Brett T. Staahl, Sean Higgins, Jennifer A. Doudna, Arik Shams, Thomas J. Laughlin
Proteins evolve through the modular rearrangement of elements known as domains. It is hypothesized that extant, multidomain proteins are the result of domain accretion, but there has been limited experimental validation of this idea. Here, we introdu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f1f66e6e83764defec213e57cff04e32
https://doi.org/10.1101/2020.10.19.344077
https://doi.org/10.1101/2020.10.19.344077
Autor:
Hongjie Li, Mark A. Gillespie, Maria C. Marchetto, Hirotaka Shoji, Gerald R. Crabtree, Zohar Shipony, Erik L. Miller, Lu Wang, Seung Tae Baek, Liqun Luo, Laura Elias, Cynthia Moncada, Wendy Wenderski, Andrey Krokhotin, Esther Y. Son, Jessica J. Walsh, Fred H. Gage, Tipu Sultan, Valentina Stanley, Shereen G. Ghosh, Jeffrey A. Ranish, Tsuyoshi Miyakawa, Renee D. George, Brett T. Staahl, Maha S. Zaki, Dillon Y. Chen, Joseph G. Gleeson, Sara B. Linker, Robert C. Malenka
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 117, iss 18
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
Significance Autism is a complex neurodevelopmental disorder whose causative mechanisms are unclear. Taking advantage of a unique cohort with recessively inherited autism, we identified six families with biallelic mutation of the neuronal-specific su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94cdae66df1cbf408e3b12b6df577943
https://escholarship.org/uc/item/65w0b3xr
https://escholarship.org/uc/item/65w0b3xr
Autor:
Marco J. Lobba, Stephanie A. Robinson, Elijah N Kissman, Casey S. Mogilevsky, Brett T. Staahl, Johnathan C. Maza, Christof Fellmann, Cole Urnes, Rachel J. Lew, Matthew B. Francis, Jennifer A. Doudna, Alan M. Marmelstein
Chimeric protein-protein conjugates provide platforms for immunotherapy, targeted drug delivery, and vaccine development. However, many desirable constructs cannot be produced through direct expression, and the targeted coupling of two proteins is ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b179ca12313dbe33d5439dde5220813
https://doi.org/10.26434/chemrxiv.9941948.v2
https://doi.org/10.26434/chemrxiv.9941948.v2