Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Jan Grünewald"'
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:
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
Protein interaction surface mapping using MS is widely applied but comparatively resource-intensive. Here, a workflow adaptation for use of isotope-coded tandem mass tags for the purpose is reported. The key benefit of improved throughput derived fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09ac873887c94194544e55964a8b7991
https://europepmc.org/articles/PMC4535432/
https://europepmc.org/articles/PMC4535432/
Publikováno v:
Anti-Infective Agents in Medicinal Chemistry. 5:227-243
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3248df897ff90e3f74f49fa520b55dc7
https://doi.org/10.2174/187152106777697835
https://doi.org/10.2174/187152106777697835
Publikováno v:
Journal of the American Chemical Society. 127:9571-9580
Streptogramin B antibiotics are cyclic peptide natural products produced by Streptomyces species. In combination with the synergistic group A component, they are "last line of defense" antimicrobial agents against multiresistant cocci. The racemizati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c5cde37d43fa57c721085b21014f6eb
https://doi.org/10.1021/ja051254t
https://doi.org/10.1021/ja051254t
Synthesis and Derivatization of Daptomycin: A Chemoenzymatic Route to Acidic Lipopeptide Antibiotics
Publikováno v:
Journal of the American Chemical Society. 126:17025-17031
Daptomycin is a branched cyclic nonribosomally assembled acidic lipopeptide, which is the first clinically approved antibiotic of this class. Here we show that the recombinant cyclization domain of the Streptomyces coelicolor calcium-dependent antibi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bca9680cea2f41b78c3981dddd32c9e
https://doi.org/10.1021/ja045455t
https://doi.org/10.1021/ja045455t