Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Kevin C Entzminger"'
Autor:
Heather M. Callaway, Kathryn M. Hastie, Sharon L. Schendel, Haoyang Li, Xiaoying Yu, Jeremy Shek, Tierra Buck, Sean Hui, Dan Bedinger, Camille Troup, S. Moses Dennison, Kan Li, Michael D. Alpert, Charles C. Bailey, Sharon Benzeno, Jody L. Bonnevier, Jin-Qiu Chen, Charm Chen, Hyeseon Cho, Peter D. Crompton, Vincent Dussupt, Kevin C. Entzminger, Yassine Ezzyat, Jonathan K. Fleming, Nick Geukens, Amy E. Gilbert, Yongjun Guan, Xiaojian Han, Christopher J. Harvey, Julia M. Hatler, Bryan Howie, Chao Hu, Ailong Huang, Maya Imbrechts, Aishun Jin, Nik Kamachi, Gladys Keitany, Mark Klinger, Jay K. Kolls, Shelly J. Krebs, Tingting Li, Feiyan Luo, Toshiaki Maruyama, Michael A. Meehl, Letzibeth Mendez-Rivera, Andrea Musa, C.J. Okumura, Benjamin E.R. Rubin, Aaron K. Sato, Meiying Shen, Anirudh Singh, Shuyi Song, Joshua Tan, Jeffrey M. Trimarchi, Dhruvkumar P. Upadhyay, Yingming Wang, Lei Yu, Tom Z. Yuan, Erik Yusko, Bjoern Peters, Georgia Tomaras, Erica Ollmann Saphire
Publikováno v:
Cell Reports, Vol 42, Iss 1, Pp 112014- (2023)
Summary: The SARS-CoV-2 Omicron variant of concern (VoC) and its sublineages contain 31–36 mutations in spike and escape neutralization by most therapeutic antibodies. In a pseudovirus neutralization assay, 66 of the nearly 400 candidate therapeuti
Externí odkaz:
https://doaj.org/article/61e61f138daa45d1ba9a2edb473cf0bc
Autor:
Kevin C Entzminger, Jonathan K Fleming, Paul D Entzminger, Lisa Yuko Espinosa, Alex Samadi, Yuko Hiramoto, Shigeru C J Okumura, Toshiaki Maruyama
Publikováno v:
Antibody Therapeutics.
SARS-CoV-2 Omicron variant XBB.1.5 has shown extraordinary immune escape even for fully vaccinated individuals. There are currently no approved antibodies that neutralize this variant, and continued emergence of new variants puts immunocompromised an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6ee6343f72db2fe69605d3bec718efde
https://doi.org/10.1093/abt/tbad006
https://doi.org/10.1093/abt/tbad006
Autor:
Kevin C. Entzminger, Jonathan K. Fleming, Paul D. Entzminger, Lisa Yuko Espinosa, Alex Samadi, Yuko Hiramoto, CJ Okumura, Toshiaki Maruyama
An antibody panel that broadly neutralizes currently circulating Omicron variants was obtained byin vitroaffinity maturation using phage display. Starting from a single parent clone, antibody engineering was performed in iterative stages in real time
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cbfb3a788a22b39396c9c80a216adcdb
https://doi.org/10.1101/2023.01.25.525589
https://doi.org/10.1101/2023.01.25.525589
Autor:
C.J. Okumura, Jose M. M. Caaveiro, Kouhei Tsumoto, Daisuke Kuroda, Makoto Nakakido, Kevin C. Entzminger, Misaki Ishii, Toshiaki Maruyama
Publikováno v:
The Journal of Biological Chemistry
Proteins are modulated by a variety of posttranslational modifications including methylation. Despite its importance, the majority of protein methylation modifications discovered by mass spectrometric analyses are functionally uncharacterized, partly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::529889bf127773dbad3788d11cb98087
http://europepmc.org/articles/PMC7948472
http://europepmc.org/articles/PMC7948472
Autor:
Toshiaki Maruyama, Raiji Kawade, C.J. Okumura, Hiroki Akiba, Kouhei Tsumoto, Kevin C. Entzminger
Publikováno v:
Protein Engineering, Design and Selection. 31:243-247
Rabbit antibodies show unique structural characteristics in that kappa chains have an inter-domain disulfide bond between the variable and constant domains. Here we characterized this disulfide bond from physicochemical viewpoints both in stability a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cb8762e5a4ea4da59f3c46fc6124a9d
https://doi.org/10.1093/protein/gzy008
https://doi.org/10.1093/protein/gzy008
Autor:
Jennifer A. Maynard, Robert J. Pantazes, Costas D. Maranas, R. E. Hughes, Zach P. Frye, Andrew D. Ellington, Kevin C. Entzminger, Ahlam Qerqez, Athéna C. Patterson-Orazem, Raquel L. Lieberman, Jeong Min Hyun
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific Reports
Scientific Reports
Computational antibody engineering efforts to date have focused on improving binding affinities or biophysical characteristics. De novo design of antibodies binding specific epitopes could greatly accelerate discovery of therapeutics as compared to c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9be2a5617b9ab625972e6b30aca25da
http://link.springer.com/article/10.1038/s41598-017-10737-9
http://link.springer.com/article/10.1038/s41598-017-10737-9
Autor:
Jennifer L. Johnson, Raquel L. Lieberman, Kevin C. Entzminger, Jennifer A. Maynard, Jeongmin Hyun
Publikováno v:
Protein Engineering Design and Selection. 28:365-377
Antibody aggregation is frequently mediated by the complementarity determining regions within the variable domains and can significantly decrease purification yields, shorten shelf-life and increase the risk of anti-drug immune responses. Aggregation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e6a0fad3dbaf1880a814bf4300fa593
https://doi.org/10.1093/protein/gzv037
https://doi.org/10.1093/protein/gzv037
Autor:
Jennifer A. Maynard, Thomas M. Truskett, Jennifer L. Johnson, Kevin C. Entzminger, Ivan A. Morales, Sibel Kalyoncu, Avni Jain, David P. Heaner, Jeongmin Hyun, Jennifer C. Pai, Raquel L. Lieberman
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 82:1884-1895
Protein crystallization is dependent upon, and sensitive to, the intermolecular contacts that assist in ordering proteins into a three-dimensional lattice. Here we used protein engineering and mutagenesis to affect the crystallization of single chain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::32f08b6c273470c99e8bbf393f46510c
https://doi.org/10.1002/prot.24542
https://doi.org/10.1002/prot.24542
Publikováno v:
Analytical Biochemistry. 421:640-648
Directed evolution relies on both random and site-directed mutagenesis of individual genes and regulatory elements to create variants with altered activity profiles for engineering applications. Central to these experiments is the construction of lar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7be15265a107e6b2836eba712a0ef551
https://doi.org/10.1016/j.ab.2011.11.009
https://doi.org/10.1016/j.ab.2011.11.009
Autor:
Sibel Kalyoncu, James C. Gumbart, Jennifer A. Maynard, David P. Heaner, Jeongmin Hyun, Jennifer L. Johnson, Aly Sheppard, Ivan A. Morales, Kevin C. Entzminger, Raquel L. Lieberman
Crystallization chaperones are attracting increasing interest as a route to crystal growth and structure elucidation of difficult targets such as membrane proteins. While strategies to date have typically employed protein-specific chaperones, a pepti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cb1d781a734d22ad7bb874edb448426
https://europepmc.org/articles/PMC4388267/
https://europepmc.org/articles/PMC4388267/