Yuanpeng J. Huang, Ph.D.

Affiliations: 
2001 Rutgers University, New Brunswick, New Brunswick, NJ, United States 
Area:
Biochemistry, Computer Science, Biomedical Engineering
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"Yuanpeng Huang"
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Gaetano T. Montelione grad student 2001 RPI
 (Automated determination of protein structures from NMR data by iterative analysis of self -consistent contact patterns.)
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Publications

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Li EH, Spaman L, Tejero R, et al. (2023) Blind Assessment of Monomeric AlphaFold2 Protein Structure Models with Experimental NMR Data. Biorxiv : the Preprint Server For Biology
Fraga KJ, Huang YJ, Ramelot TA, et al. (2022) SpecDB: A relational database for archiving biomolecular NMR spectral data. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 342: 107268
Tejero R, Huang YJ, Ramelot TA, et al. (2022) AlphaFold Models of Small Proteins Rival the Accuracy of Solution NMR Structures. Frontiers in Molecular Biosciences. 9: 877000
Huang YJ, Zhang N, Bersch B, et al. (2021) Assessment of Prediction Methods for Protein Structures Determined by NMR in CASP14: Impact of AlphaFold2. Proteins
Sala D, Huang YJ, Cole CA, et al. (2019) Protein Structure Prediction Assisted with Sparse NMR Data in CASP13. Proteins
Ozgul S, von Daake S, Kakehi S, et al. (2019) An ELISA-Based Screening Platform for Ligand-Receptor Discovery. Methods in Enzymology. 615: 453-475
Huang YJ, Brock KP, Ishida Y, et al. (2019) Combining Evolutionary Covariance and NMR Data for Protein Structure Determination. Methods in Enzymology. 614: 363-392
Huang YJ, Brock KP, Sander C, et al. (2018) A Hybrid Approach for Protein Structure Determination Combining Sparse NMR with Evolutionary Coupling Sequence Data. Advances in Experimental Medicine and Biology. 1105: 153-169
Aramini JM, Vorobiev SM, Tuberty LM, et al. (2015) The RAS-Binding Domain of Human BRAF Protein Serine/Threonine Kinase Exhibits Allosteric Conformational Changes upon Binding HRAS. Structure (London, England : 1993). 23: 1382-93
Tang Y, Huang YJ, Hopf TA, et al. (2015) Protein structure determination by combining sparse NMR data with evolutionary couplings. Nature Methods
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