Cong Chen
Peking Union Medical College
7 Papers
22 Citations
Cong Chen is an academic researcher from Peking Union Medical College. The author has contributed to research in topics: Antibody & Virus. The author has an hindex of 4, co-authored 7 publications.
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Papers
Human Neutralizing Monoclonal Antibody Inhibition of Middle East Respiratory Syndrome Coronavirus Replication in the Common Marmoset
Zhe Chen,Linlin Bao,Cong Chen,Tingting Zou,Ying Xue,Fengdi Li,Qi Lv,Songzhi Gu,Xiaopan Gao,Sheng Cui,Jianmin Wang,Chuan Qin,Qi Jin +12 more
TL;DR: A human monoclonal antibody, MCA1, directly targeting the receptor-binding domain of Middle East respiratory syndrome coronavirus (MERS-CoV) S glycoprotein, was isolated from a human survivor and completely inhibited viral replication in common marmosets.
Identification of a Novel Serum Biomarker for Tuberculosis Infection in Chinese HIV Patients by iTRAQ-Based Quantitative Proteomics.
TL;DR: ENG demonstrated the diagnostic efficacy and presented a novel molecular biomarker for TB in HIV-infected Chinese patients, which provided new insight into the challenges in the diagnosis and effective management of patients with HIV-TB.
Structural Insight into a Human Neutralizing Antibody against Influenza Virus H7N9.
TL;DR: The crystal structure of the HNIgGA6/HA1 complex provided new insight into the protective immune response to H7n9 virus in humans, as well as possibilities for the development of effective H7N9 pandemic vaccines and antiviral molecules.
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Broad neutralizing activity of a human monoclonal antibody against H7N9 strains from 2013 to 2017.
TL;DR: A previously characterized human monoclonal antibody, HNIgGA6, obtained by isolating rearranged heavy-chain and light-chain genes from patients who had recovered from H7N9 infections is described and represents a potential alternative treatment for H 7N9 interventions.
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Structural characterization of glycinamide-RNase-transformylase T from Mycobacterium tuberculosis
TL;DR: The crystal structure of MtbPurT is determined, which shows an “open” conformation, which results in a broader ATP-binding pocket and thus might facilitate the entry and exit of the cofactor, and would provide a possible opportunity for anti-TB drug development.
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