Zobrazeno 1 - 10
of 63
pro vyhledávání: '"Bernhard H, Geierstanger"'
Autor:
Scott A. Hollingsworth, Cameron L. Noland, Karin Vroom, Anasuya Saha, Miranda Sam, Qinshan Gao, Haihong Zhou, David U. Grandy, Sujata Singh, Zhiyun Wen, Christopher Warren, Xiaohong Shirley Ma, Daniel Malashock, Jennifer Galli, Gwenny Go, Michael Eddins, Todd Mayhood, Karthik Sathiyamoorthy, Arthur Fridman, Fahimeh Raoufi, Yacob Gomez-Llorente, Andrea Patridge, Yinyan Tang, Shi-Juan Chen, Marc Bailly, Chengjie Ji, Laura J. Kingsley, Alan C. Cheng, Bernhard H. Geierstanger, Daniel M. Gorman, Lan Zhang, Kalyan Pande
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-15 (2023)
Abstract Coronaviruses have been the causative agent of three epidemics and pandemics in the past two decades, including the ongoing COVID-19 pandemic. A broadly-neutralizing coronavirus therapeutic is desirable not only to prevent and treat COVID-19
Externí odkaz:
https://doaj.org/article/a9d7ab42a9cb4a6cb05bac47eef92301
Autor:
Kalyan Pande, Scott A. Hollingsworth, Miranda Sam, Qinshan Gao, Sujata Singh, Anasuya Saha, Karin Vroom, Xiaohong Shirley Ma, Tres Brazell, Dan Gorman, Shi-Juan Chen, Fahimeh Raoufi, Marc Bailly, David Grandy, Karthik Sathiyamoorthy, Lan Zhang, Rob Thompson, Alan C. Cheng, Laurence Fayadat-Dilman, Bernhard H. Geierstanger, Laura J. Kingsley
Publikováno v:
Frontiers in Immunology, Vol 13 (2022)
The SARS-CoV-2 pandemic and particularly the emerging variants have deepened the need for widely available therapeutic options. We have demonstrated that hexamer-enhancing mutations in the Fc region of anti-SARS-CoV IgG antibodies lead to a noticeabl
Externí odkaz:
https://doaj.org/article/145d782d89b84e8a8997fe9cccda8169
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2012
4'-Phosphopantetheinyl transferases (PPTases) have been employed by researchers as versatile biocatalysts for the site-specific modification of numerous protein targets with structurally diverse molecules. Here we describe the use of these enzymes fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a56c3fd706d9f317dfe651c9033d4265
https://pubmed.ncbi.nlm.nih.gov/31161512
https://pubmed.ncbi.nlm.nih.gov/31161512
Publikováno v:
Methods in Molecular Biology ISBN: 9781493995455
4'-Phosphopantetheinyl transferases (PPTases) have been employed by researchers as versatile biocatalysts for the site-specific modification of numerous protein targets with structurally diverse molecules. Here we describe the use of these enzymes fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0fb52787ae6728603c660ac6c454c18f
https://doi.org/10.1007/978-1-4939-9546-2_13
https://doi.org/10.1007/978-1-4939-9546-2_13
Autor:
Weijia Ou, Susan E. Cellitti, Bernhard H. Geierstanger, Paula Patterson, Xing Wang, Heath E. Klock, Edward Nigoghossian, Ansgar Brock, Hung Tong, Dylan Daniel, Jan Grünewald, Badry Bursulaya, William Mallet, David H. Jones, Tetsuo Uno, Daniel McMullan, Hsien-Po Chiu, Julie Vance, Huanfang Zhou, Scott A. Lesley
Publikováno v:
Bioconjugate Chemistry. 26:2554-2562
Post-translational modification catalyzed by phosphopantetheinyl transferases (PPTases) has previously been used to site-specifically label proteins with structurally diverse molecules. PPTase catalysis results in covalent modification of a serine re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7286bacea55f1489eb11261e6f30abd6
https://doi.org/10.1021/acs.bioconjchem.5b00558
https://doi.org/10.1021/acs.bioconjchem.5b00558
Autor:
Grace H. Pham, Weijia Ou, Badry Bursulaya, Michael DiDonato, Ananda Herath, Yunho Jin, Xueshi Hao, Jon Loren, Glen Spraggon, Ansgar Brock, Tetsuo Uno, Bernhard H. Geierstanger, Susan E. Cellitti
Publikováno v:
Chembiochem : a European journal of chemical biology. 19(8)
Activated esters are widely used to label proteins at lysine side chains and N termini. These reagents are useful for labeling virtually any protein, but robust reactivity toward primary amines generally precludes site-selective modification. In a un
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb61def8cf23e49b760bbe64e924ae39
https://pubmed.ncbi.nlm.nih.gov/29388367
https://pubmed.ncbi.nlm.nih.gov/29388367
Autor:
Jan Grünewald, Weijia Ou, Huanfang Zhou, Tetsuo Uno, Xing Wang, Heath E. Klock, Eric C. Peters, Jessica Read, Ansgar Brock, Julie Vance, Jin Yunho, Yongqin Wan, Bernhard H. Geierstanger
Publikováno v:
Bioconjugate chemistry. 28(7)
Phosphopantetheine transferases (PPTases) can be used to efficiently prepare site-specific antibody-drug conjugates (ADCs) by enzymatically coupling coenzyme A (CoA)-linker payloads to 11-12 amino acid peptide substrates inserted into antibodies. Her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63bd99ba14848ee5878640e2a238e6d3
https://pubmed.ncbi.nlm.nih.gov/28590752
https://pubmed.ncbi.nlm.nih.gov/28590752
Autor:
Varun Gauba, Weijia Ou, Badry Bursulaya, Vanessa Gorney, Richard A. Lerner, Bernhard H. Geierstanger, Peter G. Schultz, Teresa Ramirez-Montagut, Lisa Deaton, Mingchao Kang, Christian Schmedt, Jan Grünewald
Publikováno v:
Proceedings of the National Academy of Sciences. 108:12821-12826
The site-specific incorporation of the unnatural amino acid p -nitrophenylalanine (pNO 2 Phe) into autologous proteins overcomes self-tolerance and induces a long-lasting polyclonal IgG antibody response. To determine the molecular mechanism by which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e2e9931776242b0bd8ae37546b75a91
https://doi.org/10.1073/pnas.1110042108
https://doi.org/10.1073/pnas.1110042108
Autor:
Jan Grünewald, Qian Fan, David H. Jones, Ansgar Brock, Linda Okach, Scott A. Lesley, Tiffany Crossgrove, Lisa Quinn, Weijia Ou, Hsien-Po Chiu, Tetsuo Uno, Susan E. Cellitti, Bernhard H. Geierstanger, Paula Patterson, Xueshi Hao
Publikováno v:
Proceedings of the National Academy of Sciences. 108:10437-10442
Pyrroline-carboxy-lysine (Pcl) is a demethylated form of pyrrolysine that is generated by the pyrrolysine biosynthetic enzymes when the growth media is supplemented with D-ornithine . Pcl is readily incorporated by the unmodified pyrrolysyl-tRNA/tRNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01ae8f126a25b2c8d6300ff5801c6d8c
https://doi.org/10.1073/pnas.1105197108
https://doi.org/10.1073/pnas.1105197108
Autor:
Deborah C. Tahmassebi, Bernhard H. Geierstanger, Shannen L. Cravens, Tammy J. Dwyer, Alyssa C. Navapanich
Publikováno v:
Journal of the American Chemical Society. 132:17588-17598
The solution structures of two different DNA duplexes (one containing a G-T mismatched base pair and the other a non-hydrogen-bonding G-F pair, where F is difluorotoluene) in complex with the peptide antibiotic actinomycin D (ActD) are presented. Usi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb37cdba591288611c1bdc15e569b7e6
https://doi.org/10.1021/ja107575f
https://doi.org/10.1021/ja107575f