Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Christine C. Siska"'
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:
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
Autor:
Jon Woodard, Randal R. Ketchem, Vladimir I. Razinkov, Ramil F. Latypov, Joanna L. Scavezze, Douglas D. Banks, Christine C. Siska
Publikováno v:
Journal of Pharmaceutical Sciences. 101:2720-2732
In the present report, two formulation strategies, based on different aggregation models, were compared for their ability to quickly predict which excipients (cosolutes) would minimize the aggregation rate of an immunoglobulin G1 monoclonal antibody
Autor:
Andrei A. Raibekas, Edward J. Bures, Bruce A. Kerwin, Tadahiko Kohno, Ramil F. Latypov, Christine C. Siska
Publikováno v:
Biochemistry. 44:9871-9879
Highly concentrated human recombinant interleukin-1 receptor antagonist (IL-1ra) aggregates at elevated temperature without perturbation in its secondary structure. The protein aggregation can be suppressed depending on the buffer ionic strength and
Publikováno v:
Journal of Bone and Mineral Research. 17:1954-1960
There is a decrease in cancellous bone mass and strength during lactation but these are partially or completely reconstituted in the postlactational period. The purpose of this study was to determine changes in cancellous bone structure and formation
Publikováno v:
Molecular pharmaceutics. 11(10)
Prescreening methods are needed in the biotechnology industry for rapid selection of protein therapeutic candidates and formulations of low aggregation propensity. In recent reports solubility measurements have shown promise as one such method, altho
Autor:
Jennifer R. Litowski, Xiaolin Cao, Christine C. Siska, R. Matthew Fesinmeyer, Stephen R. Brych, Gerd R. Kleemann, Christopher J. Pierini, Zai-Qing Wen
Publikováno v:
Journal of pharmaceutical sciences. 104(2)
We report, for the first time, the identification of fatty acid particles in formulations containing the surfactant polysorbate 20. These fatty acid particles were observed in multiple mAb formulations during their expected shelf life under recommend
Autor:
Ramil F. Latypov, Christopher J. Pierini, Christine C. Siska, Jennifer R. Litowski, Hollis Lau, R. Matthew Fesinmeyer
Publikováno v:
Journal of pharmaceutical sciences. 104(2)
Polysorbate 20 (PS20) is a nonionic surfactant frequently used to stabilize protein biopharmaceuticals. During the development of mAb formulations containing PS20, small clouds of particles were observed in solutions stored in vials. The degree of pa
Autor:
Joanna L. Scavezze, Douglas D. Banks, David M. Hambly, Christine C. Siska, Himanshu S. Gadgil
Publikováno v:
Analytical chemistry. 81(17)
In biopharmaceutical process development, it is desirable to identify sites of covalent degradations to ensure product consistency. One characterization method used for therapeutic immunoglobulin gamma (IgG) 1 antibodies is limited LysC proteolysis f