Search Results - "Chumsae, Chris"

Ranking the Susceptibility of Disulfide Bonds in Human IgG1 Antibodies by Reduction, Differential Alkylation, and LC−MS Analysis by Liu, Hongcheng, Chumsae, Chris, Gaza-Bulseco, Georgeen, Hurkmans, Karen, Radziejewski, Czeslaw H

“…One of the basic structural features of human IgG1 is the arrangement of the disulfide bond structure, 4 inter chain disulfide bonds in the hinge region and 12…”
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Comparison of methionine oxidation in thermal stability and chemically stressed samples of a fully human monoclonal antibody by Chumsae, Chris, Gaza-Bulseco, Georgeen, Sun, Joanne, Liu, Hongcheng

“…Methionine (Met) oxidation is a major degradation pathway of protein therapeutics. Met oxidation of a fully human recombinant monoclonal antibody was…”
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Effect of methionine oxidation of a recombinant monoclonal antibody on the binding affinity to protein A and protein G by Gaza-Bulseco, Georgeen, Faldu, Sagar, Hurkmans, Karen, Chumsae, Chris, Liu, Hongcheng

“…Oxidation of methionine (Met) residues is one of the most common protein degradation pathways. Two Met residues, Met256 and Met432, of a recombinant fully…”
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PULSE SPR: A High Throughput Method to Evaluate the Domain Stability of Antibodies by Zhou, Li, Zhang, Jun, DiGiammarino, Enrico, Kavishwar, Amol, Yan, Bo, Chumsae, Chris, Ihnat, Peter M, Powers, David, Harlan, John, Stine, William Blaine

“…Downstream purification of therapeutic antibodies requires candidates to be stable under various stress conditions, such as low pH. Current approaches to…”
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Characterization of lower molecular weight artifact bands of recombinant monoclonal IgG1 antibodies on non-reducing SDS-PAGE by Liu, Hongcheng, Gaza-Bulseco, Georgeen, Chumsae, Chris, Newby-Kew, Abigail

“…SDS-PAGE under non-reducing conditions is one of the most commonly used techniques for recombinant monoclonal antibody purity and stability indicating assay…”
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Characterization of the glycosylation state of a recombinant monoclonal antibody using weak cation exchange chromatography and mass spectrometry by Gaza-Bulseco, Georgeen, Bulseco, Ashley, Chumsae, Chris, Liu, Hongcheng

“…Recombinant monoclonal antibody heterogeneity is inherent due to various enzymatic and non-enzymatic modifications. In this study, a recombinant humanized…”
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Expression of antibodies using single open reading frame (sORF) vector design: Demonstration of manufacturing feasibility by Gion, Wendy R., Davis-Taber, Rachel A., Regier, Dean A., Fung, Emma, Medina, Limary, Santora, Ling C., Bose, Sahana, Ivanov, Alexander V., Perilli-Palmer, Barbara A., Chumsae, Chris M., Matuck, Joseph G., Kunes, Yune Z., Carson, Gerald R.

“…Efficient production of large quantities of therapeutic antibodies is becoming a major goal of the pharmaceutical industry. We developed a proprietary…”
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Heterogeneity of monoclonal antibodies by Liu, Hongcheng, Gaza-Bulseco, Georgeen, Faldu, Dinesh, Chumsae, Chris, Sun, Joanne

“…Heterogeneity of monoclonal antibodies is common due to the various modifications introduced over the lifespan of the molecules from the point of synthesis to…”
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Comparison of the in vitro and in vivo stability of a succinimide intermediate observed on a therapeutic IgG1 molecule by Ouellette, David, Chumsae, Chris, Clabbers, Anca, Radziejewski, Czeslaw, Correia, Ivan

“…Deamidation of asparagine residues, a post-translational modification observed in proteins, is a common degradation pathway in monoclonal antibodies (mAbs)…”
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Arginine Modifications by Methylglyoxal: Discovery in a Recombinant Monoclonal Antibody and Contribution to Acidic Species by Chumsae, Chris, Gifford, Kathreen, Lian, Wei, Liu, Hongcheng, Radziejewski, Czeslaw H, Zhou, Zhaohui Sunny

“…Heterogeneity is common among protein therapeutics. For example, the so-called acidic species (charge variants) are typically observed when recombinant…”
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Analysis of Reduced Monoclonal Antibodies Using Size Exclusion Chromatography Coupled with Mass Spectrometry by Liu, Hongcheng, Gaza-Bulseco, Georgeen, Chumsae, Chris

“…Size-exclusion chromatography (SEC) has been widely used to detect antibody aggregates, monomer, and fragments. SEC coupled to mass spectrometry has been…”
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Discovery of a Chemical Modification by Citric Acid in a Recombinant Monoclonal Antibody by Chumsae, Chris, Zhou, Liqiang Lisa, Shen, Yang, Wohlgemuth, Jessica, Fung, Emma, Burton, Randall, Radziejewski, Czeslaw, Zhou, Zhaohui Sunny

“…Recombinant therapeutic monoclonal antibodies exhibit a high degree of heterogeneity that can arise from various post-translational modifications. The…”
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Detection of Alkynes via Click Chemistry with a Brominated Coumarin Azide by Simultaneous Fluorescence and Isotopic Signatures in Mass Spectrometry by Yang, Lihua, Chumsae, Chris, Kaplan, Jenifer B, Moulton, Kevin Ryan, Wang, Dongdong, Lee, David H, Zhou, Zhaohui Sunny

“…Alkynes are a key component of click chemistry and used for a wide variety of applications including bioconjugation, selective tagging of protein…”
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Identification and Localization of Unpaired Cysteine Residues in Monoclonal Antibodies by Fluorescence Labeling and Mass Spectrometry by Chumsae, Chris, Gaza-Bulseco, Georgeen, Liu, Hongcheng

“…Each human IgG1 antibody contains a total of thirty-two cysteine residues. In theory, all of them are involved in disulfide bonds, and no free sulfhydryl…”
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When Good Intentions Go Awry: Modification of a Recombinant Monoclonal Antibody in Chemically Defined Cell Culture by Xylosone, an Oxidative Product of Ascorbic Acid by Chumsae, Chris, Hossler, Patrick, Raharimampionona, Haly, Zhou, Yu, McDermott, Sean, Racicot, Chris, Radziejewski, Czeslaw, Zhou, Zhaohui Sunny

“…With the advent of new initiatives to develop chemically defined media, cell culture scientists screen many additives to improve cell growth and productivity…”
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Structural effect of deglycosylation and methionine oxidation on a recombinant monoclonal antibody by Liu, Hongcheng, Gaza-Bulseco, Georgeen, Xiang, Tao, Chumsae, Chris

“…Methionine (Met) is one of the most susceptible amino acids to oxidation. Met256 (CH2-Met15.1) and Met432 (CH3-Met107) of a recombinant humanized monoclonal…”
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Quantitation of a recombinant monoclonal antibody in monkey serum by liquid chromatography–mass spectrometry by Liu, Hongcheng, Manuilov, Anton V., Chumsae, Chris, Babineau, Michelle L., Tarcsa, Edit

“…A method including protein A purification, limited Lys-C digestion, and mass spectrometry analysis was used in the study to quantify a recombinant monoclonal…”
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New Peak Detection Performance Metrics from the MAM Consortium Interlaboratory Study by Mouchahoir, Trina, Schiel, John E, Rogers, Rich, Heckert, Alan, Place, Benjamin J, Ammerman, Aaron, Li, Xiaoxiao, Robinson, Tom, Schmidt, Brian, Chumsae, Chris M, Li, Xinbi, Manuilov, Anton V, Yan, Bo, Staples, Gregory O, Ren, Da, Veach, Alexander J, Wang, Dongdong, Yared, Wael, Sosic, Zoran, Wang, Yan, Zang, Li, Leone, Anthony M, Liu, Peiran, Ludwig, Richard, Tao, Li, Wu, Wei, Cansizoglu, Ahmet, Hanneman, Andrew, Adams, Greg W, Perdivara, Irina, Walker, Hunter, Wilson, Margo, Brandenburg, Arnd, DeGraan-Weber, Nick, Gotta, Stefano, Shambaugh, Joe, Alvarez, Melissa, Yu, X. Christopher, Cao, Li, Shao, Chun, Mahan, Andrew, Nanda, Hirsh, Nields, Kristen, Nightlinger, Nancy, Barysz, Helena Maria, Jahn, Michael, Niu, Ben, Wang, Jihong, Leo, Gabriella, Sepe, Nunzio, Liu, Yan-Hui, Patel, Bhumit A, Richardson, Douglas, Wang, Yi, Tizabi, Daniela, Borisov, Oleg V, Lu, Yali, Maynard, Ernest L, Gruhler, Albrecht, Haselmann, Kim F, Krogh, Thomas N, Sönksen, Carsten P, Letarte, Simon, Shen, Sean, Boggio, Kristin, Johnson, Keith, Ni, Wenqin, Patel, Himakshi, Ripley, David, Rouse, Jason C, Zhang, Ying, Daniels, Carly, Dawdy, Andrew, Friese, Olga, Powers, Thomas W, Sperry, Justin B, Woods, Josh, Carlson, Eric, Sen, K. Ilker, Skilton, St John, Busch, Michelle, Lund, Anders, Stapels, Martha, Guo, Xu, Heidelberger, Sibylle, Kaluarachchi, Harini, McCarthy, Sean, Kim, John, Zhen, Jing, Zhou, Ying, Rogstad, Sarah, Wang, Xiaoshi, Fang, Jing, Chen, Weibin, Yu, Ying Qing, Hoogerheide, John G, Scott, Rebecca, Yuan, Hua

“…The Multi-Attribute Method (MAM) Consortium was initially formed as a venue to harmonize best practices, share experiences, and generate innovative…”
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Global intercompany assessment of ICIEF platform comparability for the characterization of therapeutic proteins by Madren, Seth, McElroy, Will, Schultz‐Kuszak, Kristin, Boumajny, Boris, Shu, Yao, Sautter, Sabine, Zhao, Helen C., Schadock‐Hewitt, Abby, Chumsae, Chris, Ball, Nancy, Zhang, Xiaoying, Rish, Kimberly, Zhang, Shukui, Wurm, Christine, Cai, Sumin, Bauer, Scott P., Stella, Cinzia, Zheng, Laura, Roper, Brian, Michels, David A., Wu, Gang, Kocjan, Bostjan, Birk, Matej, Erdmann, Simon Erik, He, Xiaoping, Whittaker, Brad, Song, Yvonne, Barrett, Hannah, Strozyk, Kevin, Jing, Ye, Huang, Long, Mhatre, Vishal, McLean, Paul, Yu, Tiantian, Yang, Huijuan, Mattila, Minna

“…An international team spanning 19 sites across 18 biopharmaceutical and in vitro diagnostics companies in the United States, Europe, and China, along with one…”
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Back Cover: Global intercompany assessment of ICIEF platform comparability for the characterization of therapeutic proteins by Madren, Seth, McElroy, Will, Schultz‐Kuszak, Kristin, Boumajny, Boris, Shu, Yao, Sautter, Sabine, Zhao, Helen C., Schadock‐Hewitt, Abby, Chumsae, Chris, Ball, Nancy, Zhang, Xiaoying, Rish, Kimberly, Zhang, Shukui, Wurm, Christine, Cai, Sumin, Bauer, Scott P., Stella, Cinzia, Zheng, Laura, Roper, Brian, Michels, David A., Wu, Gang, Kocjan, Bostjan, Birk, Matej, Erdmann, Simon Erik, He, Xiaoping, Whittaker, Brad, Song, Yvonne, Barrett, Hannah, Strozyk, Kevin, Jing, Ye, Huang, Long, Mhatre, Vishal, McLean, Paul, Yu, Tiantian, Yang, Huijuan, Mattila, Minna

“…DOI: 10.1002/elps.202100348 The back cover picture shows the iCE3 and Maurice instruments used to demonstrate the comparability of the instruments for…”
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