Zobrazeno 1 - 10
of 51
pro vyhledávání: '"Ansgar, Brock"'
Autor:
Catherine A. Sabatos-Peyton, James Nevin, Ansgar Brock, John D. Venable, Dewar J. Tan, Nasim Kassam, Fangmin Xu, John Taraszka, Luke Wesemann, Thomas Pertel, Nandini Acharya, Max Klapholz, Yassaman Etminan, Xiaomo Jiang, Yu-Hwa Huang, Richard S. Blumberg, Vijay K. Kuchroo, Ana C. Anderson
Publikováno v:
OncoImmunology, Vol 7, Iss 2 (2018)
Both in vivo data in preclinical cancer models and in vitro data with T cells from patients with advanced cancer support a role for Tim-3 blockade in promoting effective anti-tumor immunity. Consequently, there is considerable interest in the clinica
Externí odkaz:
https://doaj.org/article/3c144a1874ea4d4292b8f6ab85913507
Autor:
John D Venable, Ajay A Vashisht, Shima Rayatpisheh, James P Lajiness, Dean P Phillips, Ansgar Brock
Proximity dependent labeling using engineered enzymes has been used extensively to identify protein-protein interactions, and map protein complexes in-vitro and in-vivo. Here, we extend the use of engineered promiscuous biotin ligases to the identifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::11521c45e325bcdb46153b2a8649dbe5
https://doi.org/10.1101/2022.09.26.509259
https://doi.org/10.1101/2022.09.26.509259
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
Autor:
Michael J. Chalmers, Ioannis Karageorgos, John D. Venable, James A. Carroll, Arun Chandramohan, Kasper D. Rand, John D. Lambris, Alfonso Espada, Sheng Li, Jennifer Zhang, Ansgar Brock, George M. Bou-Assaf, Sasidhar N. Nirudodhi, Ratnesh Pandey, Mohammed A. Al-Naqshabandi, Eduardo Harguindey, Patrick L. Wintrode, Kyle Anderson, Daniel Deredge, Ulrike Leurs, Tyler S. Hageman, Jeffrey W. Hudgens, Justin B. Sperry, Benjamin T. Walters, Hui-Min Zhang, Sarah Urata, Xiaojun Lu, Caitlin Steckler, Ganesh S. Anand, Guodong Chen, David D. Weis, Jason C. Rouse, Malvina Papanastasiou, Richard Y.-C. Huang, In-Hee Park, Elyssia S. Gallagher
Publikováno v:
J Res Natl Inst Stand Technol
The spreadsheet file reported herein provides centroid data, descriptive of deuterium uptake, for the FabFragment of NISTmAb (PDB: 5K8A) reference material, as measured by the bottom-up hydrogen-deuterium exchange mass spectrometry (HDX-MS) method. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23a7327699cde634290e4ee6dba251cc
https://pubmed.ncbi.nlm.nih.gov/34877153
https://pubmed.ncbi.nlm.nih.gov/34877153
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:
Tyler S. Hageman, Ulrike Leurs, John D. Lambris, Michael J. Chalmers, Ratnesh Pandey, Malvina Papanastasiou, James J. Filliben, Ioannis Karageorgos, Jeffrey W. Hudgens, Guodong Chen, Sarah Urata, Xiaojun Lu, Arun Chandramohan, Sheng Li, George M. Bou-Assaf, Mohammed A. Al-Naqshabandi, Alfonso Espada, Daniel Deredge, Ganesh S. Anand, Ansgar Brock, Sasidhar N. Nirudodhi, Caitlin Steckler, Patrick L. Wintrode, Eduardo Harguindey, Justin B. Sperry, Jennifer Zhang, Kyle Anderson, Kasper D. Rand, David D. Weis, Jason C. Rouse, James A. Carroll, Benjamin T. Walters, John D. Venable, Elyssia S. Gallagher, Hui-Min Zhang, Richard Y.-C. Huang, In-Hee Park
Publikováno v:
Hudgens, J W, Gallagher, E S, Karageorgos, I, Anderson, K W, Filliben, J J, Huang, R Y-C, Chen, G, Bou-Assaf, G M, Espada, A, Chalmers, M J, Harguindey, E, Zhang, H-M, Walters, B T, Zhang, J, Venable, J D, Steckler, C, Park, I, Brock, A, Lu, X, Pandey, R K, Chandramohan, A, Anand, G S, Nirudodhi, S N, Sperry, J B, Rouse, J C, Carroll, J A, Rand, K D, Leurs, U, Weis, D D, Al-Naqshabandi, M A, Hageman, T S, Deredge, D, Wintrode, P L, Papanastasiou, M, Lambris, J D, Li, S & Urata, S 2019, ' Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab fragment of NISTmAb ', Analytical Chemistry, vol. 91, no. 11, pp. 7336-7345 . https://doi.org/10.1021/acs.analchem.9b01100
Anal Chem
Anal Chem
Hydrogen-deuterium exchange mass spectrometry (HDX-MS) is an established, powerful tool for investigating protein-ligand interactions, protein folding, and protein dynamics. However, HDX-MS is still an emergent tool for quality control of biopharmace
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5296a6097f668348bab5767e63adbfa6
https://curis.ku.dk/portal/da/publications/interlaboratory-comparison-of-hydrogendeuterium-exchange-mass-spectrometry-measurements-of-the-fab-fragment-of-nistmab(681700fb-de3a-485d-8fe7-fe3921794d20).html
https://curis.ku.dk/portal/da/publications/interlaboratory-comparison-of-hydrogendeuterium-exchange-mass-spectrometry-measurements-of-the-fab-fragment-of-nistmab(681700fb-de3a-485d-8fe7-fe3921794d20).html
Autor:
Advait Nagle, Ben G. Wen, Srinivasa P. S. Rao, Monique Stinson, Glenn C. Federe, Richard Glynne, Yin H. Lai, Ianne C. Rivera, Ansgar Brock, Michael Shapiro, Hazel X. Y. Koh, John D. Venable, Jaime Ballard, J. Robert Gillespie, Badry Bursulaya, Glen Spraggon, Xianzhong Liu, Mu-Yun Gao, Vince Yeh, Tove Tuntland, Fang Liang, S. Whitney Barnes, Todd Groessl, Shilpi Khare, Elmarie Myburgh, Agnes Biggart, Lauren C. Davis, Jocelyn Tan, Pranab Mishra, Frantisek Supek, Casey J. N. Mathison, Valentina Molteni, Jeremy C. Mottram, Frederick S. Buckner, John R. Walker
Publikováno v:
Nature
Chagas disease, leishmaniasis and sleeping sickness affect 20 million people worldwide and lead to more than 50,000 deaths annually1. The diseases are caused by infection with the kinetoplastid parasites Trypanosoma cruzi, Leishmania spp. and Trypano
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24bc027b1d63c94a64adf691d28ee40c
http://europepmc.org/articles/PMC5161665
http://europepmc.org/articles/PMC5161665
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
Publikováno v:
Journal of the American Society for Mass Spectrometry. 24:642-645
An algorithm for retention time alignment of mass shifted hydrogen-deuterium exchange (HDX) data based on an iterative distance minimization procedure is described. The algorithm performs pairwise comparisons in an iterative fashion between a list of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::194b4377589dd47306edbd275c7dece5
https://doi.org/10.1007/s13361-012-0566-9
https://doi.org/10.1007/s13361-012-0566-9