Zobrazeno 1 - 10
of 68
pro vyhledávání: '"Bruce A. Kerwin"'
Publikováno v:
Journal of Pharmaceutical Sciences
An early-phase development shipping study was designed to interrogate the stability of liquid formulations under normal shipping conditions. Parcel shipments were made between Seattle, WA, and Indianapolis, IN, during 2018-2019. Each parcel contained
Autor:
Jeffrey J. James, Alison J. Gillespie, Yuko Ogata, J. Alaina Floyd, Jeremy M. Shaver, Nancy S. Nightlinger, Richard S. Rogers, Unjy Park, Bruce A. Kerwin
Publikováno v:
Journal of Pharmaceutical Sciences
Formulation screening for biotherapeutics can cover a vast array of excipients and stress conditions. These studies consume quantities of limited material and, with higher concentrated therapeutics, more material is needed. Here, we evaluate the use
Autor:
Chelsey Bennett, Mcclure Megan J, Georgia D. Tomaras, Michael S. Seaman, Clark Rutilio H, Randal R. Ketchem, J. Alaina Floyd, Kelly E. Seaton, Christine C. Siska, Yan Brodsky, Jeremy M. Shaver, Bryan T. Mayer, Nicole L. Yates, Bruce A. Kerwin, Alison J. Gillespie
Publikováno v:
Journal of Pharmaceutical Sciences
The broadly neutralizing anti-HIV antibody, 10-1074, is a highly somatically hypermutated IgG1 being developed for prophylaxis in sub-Saharan Africa. A series of algorithms were applied to identify potentially destabilizing residues in the framework
Autor:
Amimeur Tileli, Clark Rutilio H, Josh Smith, Danielle Van Citters, Bruce A. Kerwin, Jeremy M. Shaver, Randal R. Ketchem, Christine C. Siska, Smidt Pauline S, Megan Sprague, Dean Pettit, J. Alex Taylor
We demonstrate the use of a Generative Adversarial Network (GAN), trained from a set of over 400,000 light and heavy chain human antibody sequences, to learn the rules of human antibody formation. The resulting model surpasses common in silico techni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c13fde634263f9f22e3613107036384e
Publikováno v:
Development of Biopharmaceutical Drug-Device Products ISBN: 9783030314149
Multi-attribute method (MAM) is a mass spectrometry (MS)-based method that is used to directly characterize and monitor many product quality attributes and impurities on biotherapeutics. MAM utilizes high-resolution/accurate mass MS data. These data
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e5f818da71e97be6a564daa6f2aec193
https://doi.org/10.1007/978-3-030-31415-6_9
https://doi.org/10.1007/978-3-030-31415-6_9
Autor:
Robin Curtis, Steven Blake, Wei Qi, Gregory V. Barnett, Vladimir I. Razinkov, Bruce A. Kerwin, Christopher J. Roberts
Publikováno v:
The Journal of Physical Chemistry B. 120:3318-3330
Preferential interactions of proteins with water and osmolytes play a major role in controlling the thermodynamics of protein solutions. While changes in protein stability and shifts in phase behavior are often reported with the addition of osmolytes
Autor:
Christopher J. Roberts, Bruce A. Kerwin, Gregory V. Barnett, Alexander Hillsley, Vladimir I. Razinkov
Publikováno v:
Journal of Pharmaceutical Sciences. 105:1066-1073
Controlling and predicting unwanted degradation, such as non-native aggregation, is a long-standing challenge for mAbs and other protein-based products. mAb aggregation rates are typically sensitive to temperature, pH, and the addition of excipients.
Autor:
Thomas M. Laue, Bruce A. Kerwin, Paul Butler, Christopher J. Roberts, Tatiana Perevozchikova, Andrea H. Woodka, Gregory V. Barnett, Vladimir I. Razinkov
Publikováno v:
The Journal of Physical Chemistry B. 119:5793-5804
Non-native protein aggregation is common in the biopharmaceutical industry and potentially jeopardizes product shelf life, therapeutic efficacy, and patient safety. The present article focuses on the relationship(s) among protein-protein interactions
Autor:
David B. Volkin, C. Russell Middaugh, Feng He, Prem S. Thapa, Christine S. Siska, Sangeeta B. Joshi, Paul S. Bullock, Houman Bashiri, Nigel Pheasey, Bruce A. Kerwin, Ozan S. Kumru
Publikováno v:
Journal of Pharmaceutical Sciences. 104:485-494
The structural integrity and conformational stability of a genetically modified live, oncolytic herpes simplex virus (o-HSV) were investigated across a wide pH (5.5-8.0) and temperature (10°C–87.5°C) range. A combination of circular dichroism, in
Autor:
Christopher E. Woods, Shradha Mishra, Randal R. Ketchem, Feng He, Bruce A. Kerwin, Jeremy D. Schmit
Publikováno v:
The Journal of Physical Chemistry B. 118:5044-5049
Antibody solutions are typically much more viscous than solutions of globular proteins at equivalent volume fraction. Here we propose that this is due to molecular entanglements that are caused by the elongated shape and intrinsic flexibility of anti