Bing Gong

University of Science and Technology of China

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Yong‐Fei Zheng

University of Science and Technology of China

Huijuan Li

Qilu University of Technology

Zi‐Fu Zhao

University of Science and Technology of China

Li‐Qun Dai

University of Science and Technology of China

Irina Burnina

Adimab (United States)

Heather Lynaugh

Adimab (United States)

Y. F. Zheng

University of Science and Technology of China

Terrance A. Stadheim

Merck & Co., Inc., Rahway, NJ, USA (United States)

Bin Fu

Australian National University

Ren‐Xu Chen

University of Science and Technology of China

Cooperative Institutions

Merck & Co., Inc., Rahway, NJ, USA (United States)

Compass (United States)

Chinese Academy of Sciences

University of Science and Technology of China

Sage Therapeutics (United States)

Dartmouth College

Biolog (United States)

Moffitt Cancer Center

Dartmouth–Hitchcock Medical Center

GlycoScientific (United States)

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CTX-8573, an Innate-Cell Engager Targeting BCMA, is a Highly Potent Multispecific Antibody for the Treatment of Multiple Myeloma

Blood (2019)

Jennifer Watkins-Yoon Wilson Guzman Amanda Oliphant Sara M. Haserlat Alan Leung

10.1182/blood-2019-128749

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Citations (36)

Characterization of N-Linked Glycosylation on Recombinant Glycoproteins Produced in Pichia pastoris Using ESI-MS and MALDI-TOF

Humana Press eBooks (2008)

Bing Gong Michael Cukan Richard Fisher Huijuan Li Terrance A. Stadheim

The production of recombinant therapeutic glycoproteins is an active area of research and drug development. Typically, improvements in therapeutic glycoprotein efficacy have focused on engineering additional N-glycosylation sites into the primary amino acid sequence or attempting to control a particular glycoform profile on a protein through process improvements. Recently, a number of alternative expression systems have appeared that are challenging the dominance of mammalian cell culture. Our laboratory has focused on the re-engineering of the secretory pathway in the yeast Pichia pastoris to perform glycosylation reactions that mimic processing of N-glycans in humans. We have demonstrated that human antibodies with specific human N-glycan structures can be produced in glycoengineered lines of Pichia pastoris and that antibody-mediated effector functions can be optimized by generating specific glycoforms. In this chapter we provide detailed protocols for the analysis of glycosylation on intact glycoproteins by MALDI-TOF and site specific N-glycan occupancy on digested glycoprotein using ESI-MS.

Pichia

N-linked glycosylation

Protein Engineering

10.1007/978-1-59745-022-5_16

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Citations (20)

The effect of supercritical fluids on Nb-Ta fractionation in subduction zones: Geochemical insights from a coesite-bearing eclogite-vein system

Geochimica et Cosmochimica Acta (2022)

Tienan Chen Ren‐Xu Chen Yong‐Fei Zheng Kun Zhou Zhuang-Zhuang Yin

Omphacite

Coesite

Amphibole

10.1016/j.gca.2022.08.013

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Citations (18)

A cost-effective plate-based sample preparation for antibody N-glycan analysis

Journal of Chromatography A (2013)

Irina Burnina Erik Hoyt Heather Lynaugh Huijuan Li Bing Gong

Sample Preparation

Filter paper

10.1016/j.chroma.2013.07.104

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Citations (33)

ChemInform Abstract: A New and Efficient Method for the Resolution of 2,2′‐Dihydroxy‐1,1′‐ binaphthyl.

ChemInform (1991)

Bing Gong W.‐Y. Chen Bin Hu

Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.

10.1002/chin.199121071

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Citations (0)

Regioselective reductions of diacids: aspartic acid to homoserine

The Journal of Organic Chemistry (1990)

Bing Gong David G. Lynn

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTRegioselective reductions of diacids: aspartic acid to homoserineBing Gong and David G. LynnCite this: J. Org. Chem. 1990, 55, 15, 4763–4765Publication Date (Print):July 1, 1990Publication History Published online1 May 2002Published inissue 1 July 1990https://pubs.acs.org/doi/10.1021/jo00302a054https://doi.org/10.1021/jo00302a054research-articleACS PublicationsRequest reuse permissionsArticle Views1021Altmetric-Citations19LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

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10.1021/jo00302a054

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Citations (23)

Rapid Fc glycosylation analysis of Fc fusions with IdeS and liquid chromatography mass spectrometry

mAbs (2013)

Heather Lynaugh Huijuan Li Bing Gong

We developed a rapid method to analyze Fc glycosylation of Fc fusion proteins, especially those with mutated Fc hinge regions. Fc fusion proteins were digested with IdeS, an IgG specific protease with exosites for substrate recognition and cleavage. The resultant fragments were directly analyzed through liquid chromatography mass spectrometry. The structures and relative quantities of Fc glycans were deduced from their masses and intensities. The separated substrate recognition and cleavage property of IdeS makes this method applicable to a broad range of Fc fusion proteins having either standard or non-canonical hinge regions.

Cleavage (geology)

Fragment crystallizable region

N-linked glycosylation

10.4161/mabs.25302

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Citations (40)

Determination of iguratimod in rat plasma by high performance liquid chromatography: method and application

Biomedical Chromatography (2007)

Ting Zhou Li Ding Xiaomin Li Fei Zhang Qian Zhang

Abstract A high‐performance liquid chromatographic method with UV detection has been developed for the determination of iguratimod (T‐614) in rat plasma. Plasma was precipitated with acetonitrile after the addition of the internal standard (IS), N ‐[4‐(2‐formylaminoacetyl)‐5‐methoxy‐2‐phenoxyphenyl]‐methanesulfonamide. The chromatographic separation was achieved on a reversed‐phase C 18 column with the mobile phase acetonitrile–acetic acid aqueous solution, pH 4.5 (40:60, v/v), at a flow rate of 1 mL/min, and the UV detection wavelength was set at 257 nm. The calibration curve was linear over the range 0.10–50.0 µg/mL, and the lower limit of quantification was 0.10 µg/mL. The intra‐ and inter‐day relative standard deviations were all less than 11.5%. The method has been successfully applied to study the pharmacokinetics of iguratimod in rats. A single 10 mg/kg dose of iguratimod was given to the rats by intragastric administration. The mean maximum plasma concentration of iguratimod for the six rats was 14.5 µg/mL, and the mean elimination half‐life of iguratimod was 4.0 h. Copyright © 2007 John Wiley & Sons, Ltd.

Chromatographic Separation

Relative standard deviation

10.1002/bmc.921

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Citations (10)

Geochemical studies of eclogites and marbles from Sujiahe in the western Dabie Mountains

Bin Fu Yan Zheng Yang Xiao Yu LI Bing Gong

Source

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Citations (1)

N-Glycosylamine-mediated isotope labeling for mass spectrometry-based quantitative analysis of N-linked glycans

Analytical and Bioanalytical Chemistry (2013)