N. Zhong

发表

Identification of structure-activity relationships from screening a structurally compact DNA-encoded chemical library.

Jonathan Hall, S. Gräslund, T. Ekblad, 2015, Angewandte Chemie.

Assessment of a method to characterize antibody selectivity and specificity for use in immunoprecipitation

Jeffrey R. Whiteaker, Ben C. Collins, Jacob J. Kennedy, 2015, Nature Methods.

C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer

C. Jin, Z. Rao, Z. Lou, 2009, Protein science : a publication of the Protein Society.

Discovery of a chemical probe for the L3MBTL3 methyl-lysine reader domain

A. Emili, J. Greenblatt, Xi-Ping Huang, 2012, Nature chemical biology.

Letter to the Editor: 1H, 13C, and 15N resonance assignments of the N-terminal domain of the SARS CoV nucleocapsid protein

C. Jin, N. Zhong, B. Xia, 2005, Journal of biomolecular NMR.

Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site.

C. Jin, J. Jacquot, N. Rouhier, 2006, Biochemistry.

Tankyrase 1 Inhibitors with Drug-like Properties Identified by Screening a DNA-Encoded Chemical Library.

Jonathan Hall, S. Gräslund, T. Ekblad, 2015, Journal of medicinal chemistry.

Optimizing Production of Antigens and Fabs in the Context of Generating Recombinant Antibodies to Human Proteins

J. Greenblatt, A. Koide, S. Koide, 2015, PloS one.

Histone recognition by human malignant brain tumor domains.

C. Arrowsmith, Shili Duan, N. Zhong, 2012, Journal of molecular biology.

A High Through-put Platform for Recombinant Antibodies to Folded Proteins*

Shohei Koide, Franco J. Vizeacoumar, Nan Zhong, 2015, Molecular & Cellular Proteomics.

The structure-activity relationships of L3MBTL3 inhibitors: flexibility of the dimer interface.

S. Frye, W. Janzen, C. Arrowsmith, 2013, MedChemComm.

Foldon unfolding mediates the interconversion between Mpro-C monomer and 3D domain-swapped dimer

C. Jin, Peng Zou, N. Zhong, 2012, Proceedings of the National Academy of Sciences.

Without Its N-Finger, the Main Protease of Severe Acute Respiratory Syndrome Coronavirus Can Form a Novel Dimer through Its C-Terminal Domain

C. Jin, Peng Zou, N. Zhong, 2008, Journal of Virology.

Without its N-Finger , SARS-CoV Main Protease 1 can Form a Novel Dimer through its C-Terminal Domain 2 3

C. Jin, Peng Zou, N. Zhong, 2008 .

Cyclophilin A (CyPA) Induces Chemotaxis Independent of Its Peptidylprolyl Cis-Trans Isomerase Activity

N. Zhong, Zhi-Nan Chen, Jian-Li Jiang, 2011, The Journal of Biological Chemistry.

Three-dimensional domain swapping as a mechanism to lock the active conformation in a super-active octamer of SARS-CoV main protease

C. Jin, Z. Lou, N. Zhong, 2010, Protein & Cell.

Crystal structure of the nucleotide-binding domain of Ras-related GTP-binding protein C

C. Bountra, C. Arrowsmith, J. Weigelt, 2010 .

Structure Based Affinity Maturation and Characterizing of SARS-CoV Antibody CR3022 against SARS-CoV-2 by Computational and Experimental Approaches

N. Zhong, Rongfeng Chen, Xiaohui Yuan, 2022, Viruses.

Without Its N-Finger, the Main Protease of Severe Acute Respiratory Syndrome Coronavirus Can Form a Novel Dimer through Its C-Terminal Domain

C. Jin, Peng Zou, N. Zhong, 2008, Journal of Virology.