Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Eric S, Day"'
Autor:
Matthew G. Romei, Brandon Leonard, Zachary B. Katz, Daniel Le, Yanli Yang, Eric S. Day, Christopher W. Koo, Preeti Sharma, Jack Bevers III, Ingrid Kim, Huiguang Dai, Farzam Farahi, May Lin, Andrey S. Shaw, Gerald Nakamura, Jonathan T. Sockolosky, Greg A. Lazar
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract The ability to leverage antibodies to agonize disease relevant biological pathways has tremendous potential for clinical investigation. Yet while antibodies have been successful as antagonists, immune mediators, and targeting agents, they ar
Externí odkaz:
https://doaj.org/article/17d263c9cfc746cea0b227c5efde646d
Autor:
Elena Ferri, Adrien Le Thomas, Heidi Ackerly Wallweber, Eric S. Day, Benjamin T. Walters, Susan E. Kaufman, Marie-Gabrielle Braun, Kevin R. Clark, Maureen H. Beresini, Kyle Mortara, Yung-Chia A. Chen, Breanna Canter, Wilson Phung, Peter S. Liu, Alfred Lammens, Avi Ashkenazi, Joachim Rudolph, Weiru Wang
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
The RNase activity of Inositol-Requiring Enzyme 1 (IRE1) can be allosterically regulated by ATP-competitive inhibitors of the IRE1 kinase domain. Here, the authors identify ATP-competitive IRE1 RNase activators with improved selectivity and cellular
Externí odkaz:
https://doaj.org/article/b949b998bea04b119070c87d6eced201
Autor:
Breanna Canter, Benjamin T. Walters, Alfred Lammens, Peter Liu, Avi Ashkenazi, Wilson Phung, Weiru Wang, Kevin R Clark, Adrien Le Thomas, Joachim Rudolph, Heidi J.A. Wallweber, Elena Ferri, Eric S. Day, Kyle Mortara, Maureen Beresini, Marie-Gabrielle Braun, Yung-Chia A. Chen, Susan Kaufman
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Nature Communications
Nature Communications
Inositol-Requiring Enzyme 1 (IRE1) is an essential component of the Unfolded Protein Response. IRE1 spans the endoplasmic reticulum membrane, comprising a sensory lumenal domain, and tandem kinase and endoribonuclease (RNase) cytoplasmic domains. Exc
Autor:
George M. Bou-Assaf, Ivan L. Budyak, Michael Brenowitz, Eric S. Day, David Hayes, John Hill, Ranajoy Majumdar, Paola Ringhieri, Peter Schuck, Jasper C. Lin
Publikováno v:
J Pharm Sci
Analytical ultracentrifugation (AUC) is a critical analytical tool supporting the development and manufacture of protein therapeutics. AUC is routinely used as an assay orthogonal to size exclusion chromatography for aggregate quantitation. This arti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e43b967f463b00c953dcfcd1b5533d9
https://europepmc.org/articles/PMC9232890/
https://europepmc.org/articles/PMC9232890/
Autor:
Thierry Nivaggioli, Shalini Burra, Laetitia Comps-Agrar, Karthikan Rajagopal, Eric S. Day, Joyce Chan, Debby P. Chang
Publikováno v:
Journal of pharmaceutical sciences. 110(2)
The port delivery system with ranibizumab (PDS) is an investigational long-acting drug delivery system for the continuous release of ranibizumab, an anti-VEGF biologic, in the vitreous humor. The efficacy of the PDS implant relies on the maintenance
Autor:
Oliver B. Stauch, Robert Ovadia, Eric S. Day, Benson Gikanga, Yuh-Fun Maa, Devon Roshan Eisner
Publikováno v:
PDA Journal of Pharmaceutical Science and Technology. 71:172-188
Subvisible particle formation in monoclonal antibody drug product resulting from mixing and filling operations represents a significant processing risk that can lead to filter fouling and thereby lead to process delays or failures. Several previous s
Autor:
Napoleone Ferrara, Mehraban Khosraviani, Barthélemy Demeule, Eric S. Day, Steven J. Shire, Sandeep Yadav, Germaine Fuh, Lanlan Yu, Jun Liu, Jihong Yang, Eric Wakshull, Xiangdan Wang
Publikováno v:
Molecular pharmaceutics, vol 11, iss 10
The objectives of this study were to evaluate the relative binding and potencies of three inhibitors of vascular endothelial growth factor A (VEGF), used to treat neovascular age-related macular degeneration, and assess their relevance in the context
Autor:
Pascal Schneider, Laure Willen, Eric S. Day, Dennis Krushinskie, Timothy S. Zheng, Mai Perroud, Hernan Cuervo, Kathy Strauch, Maria Pellegrini
Publikováno v:
The FEBS journal
FEBS Journal, vol. 280, no. 8, pp. 1818-1829
FEBS Journal, vol. 280, no. 8, pp. 1818-1829
TWEAK (TNF homologue with weak apoptosis-inducing activity) and Fn14 (fibroblast growth factor-inducible protein 14) are members of the tumor necrosis factor (TNF) ligand and receptor super-families. Having observed that Xenopus Fn14 cross-reacts wit
Autor:
John E. Schiel, Darryl L. Davis, Oleg V. Borisov, Trina Formolo, Mellisa Ly, Michaella Levy, Lisa Kilpatrick, Scott Lute, Karen Phinney, Lisa Marzilli, Kurt Brorson, Michael Boyne, Darryl Davis, John Schiel, Melissa Alvarez, James A. Carroll, Paul W. Brown, Wenzhou Li, James L. Kerwin, Andrew Mahan, Sabrina A. Benchaar, Justin M. Prien, Henning Stöckmann, Simone Albrecht, Silvia M. Martin, Matthew Varatta, Marsha Furtado, Stephen Hosselet, Meiyao Wang, Pauline M. Rudd, David A. Michels, Anna Y. Ip, Thomas M. Dillon, Brittany Chavez, Ken M. Prentice, Lowell J. Brady, Karen J. Miller, Yatin Gokarn, Sanjeev Agarwal, Kelly Arthur, Alexander Bepperling, Eric S. Day, Dana Filoti, Daniel G. Greene, David Hayes, Rachel Kroe-Barrett, Thomas Laue, Jasper Lin, Brian McGarry, Vladimir Razinkov, Sanjaya Singh, Rosalynn Taing, Sathyadevi Venkataramani, William Weiss, Danlin Yang, Isidro E. Zarraga, Dorina Saro, Audrey Baker, Robert Hepler, Stacey Spencer, Rick Bruce, Steven LaBrenz, Mark Chiu, Steven E. Lang, Dean C. Ripple, Linda O. Narhi, Kesh Prakash, Weibin Che
Autor:
Kathleen Wortham, Ellen Garber, Eric S. Day, Laure Wille, You Li, Sandy Cho, Rebecca Kelly, Yen-Ming Hsu, Lihe Su, Ingrid B.J.K. Joseph, Lisa Berquist, Jennifer S. Michaelson, Aldo Amatucci, Pascal Schneider, Michael Parr, Linda C. Burkly
Publikováno v:
mAbs. 3:362-375
TNF-like weak inducer of apoptosis (TWEAK), a tumor necrosis factor (TNF) family ligand with pleiotropic cellular functions, was originally described as capable of inducing tumor cell death in vitro. TWEAK functions by binding its receptor, Fn14, whi