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Min Shen

Researcher at Amgen

Publications -  6
Citations -  824

Min Shen is an academic researcher from Amgen. The author has contributed to research in topics: Endoplasmic reticulum & Secretory pathway. The author has an hindex of 5, co-authored 6 publications receiving 738 citations. Previous affiliations of Min Shen include Protein Sciences.

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Enhancing Antibody Fc Heterodimer Formation through Electrostatic Steering Effects: APPLICATIONS TO BISPECIFIC MOLECULES AND MONOVALENT IgG

TL;DR: This work modified the CH3 domain interface of the antibody Fc region with selected mutations so that the engineered Fc proteins preferentially form heterodimers, demonstrating the feasibility of robust production of novel Fc-based heterodimeric molecules.
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Interleukin-36 (IL-36) ligands require processing for full agonist (IL-36α, IL-36β, and IL-36γ) or antagonist (IL-36Ra) activity.

TL;DR: It is demonstrated that IL-36Ra antagonist activity is dependent upon removal of its N-terminal methionine, and the mechanism of action is directly analogous to that of IL-1Ra, which suggests that protease(s) that activate IL- 36 cytokines could be excellent drug targets for psoriasis.
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A novel antibody engineering strategy for making monovalent bispecific heterodimeric IgG antibodies by electrostatic steering mechanism.

TL;DR: The engineered heterodimeric IgG molecules maintain the overall IgG structure with correct LC-HC pairings, bind to two different antigens with comparable affinity when compared with their parental antibodies, and retain the functionality of parental antibodies in biological assays.
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In Vivo Crystallization of Human IgG in the Endoplasmic Reticulum of Engineered Chinese Hamster Ovary (CHO) Cells

TL;DR: It is shown that the ER-to-Golgi transport steps became rate-limiting in cells with high secretory activity, and the efficiency of IgG protein synthesis and oxidative folding exceeded the capacity of ER export machinery.
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Modulation of in vivo IgG crystallization in the secretory pathway by heavy chain isotype class switching and N-linked glycosylation

TL;DR: An IgG's in vivo crystal morphology and crystallization propensity can be modulated by the properties genetically and biochemically encoded in the HC constant region, and alterations to the constant domain-encoded properties revealed their modulatory roles in CB-inducing propensities and CB morphology.