GVT Swapna
Affiliations: | 1990- | Biochemistry | Rutgers - Robert Wood Johnson Medical School |
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Parents
Sign in to add mentor| Gaetano T. Montelione | research scientist | 1990- | Rutgers - Robert Wood Johnson Medical School |
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Publications
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| Woltz R, Schweibenz B, Tsutakawa SE, et al. (2024) The NS1 protein of influenza B virus binds 5'-triphosphorylated dsRNA to suppress RIG-I activation and the host antiviral response. Biorxiv : the Preprint Server For Biology |
| Mondal A, Singh B, Felkner RH, et al. (2024) Sifting Through the Noise: A Computational Pipeline for Accurate Prioritization of Protein-Protein Binding Candidates in High-Throughput Protein Libraries. Biorxiv : the Preprint Server For Biology |
| Mondal A, Swapna GVT, Lopez MM, et al. (2023) Structure Determination of Challenging Protein-Peptide Complexes Combining NMR Chemical Shift Data and Molecular Dynamics Simulations. Journal of Chemical Information and Modeling |
| 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 |
| Colman DR, Labesse G, Swapna GVT, et al. (2022) Structural evolution of the ancient enzyme, dissimilatory sulfite reductase. Proteins |
| 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 |
| Aiyer S, Swapna GVT, Ma LC, et al. (2021) A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins. Structure (London, England : 1993) |
| Sala D, Huang YJ, Cole CA, et al. (2019) Protein Structure Prediction Assisted with Sparse NMR Data in CASP13. Proteins |
| Zhang M, Yu X, Xu Y, et al. (2019) The Structural Basis by Which the N-terminal Polypeptide Segment of Rhizopus chinensis Lipase Regulates Its Substrate Binding Affinity. Biochemistry |
| Rosario-Cruz Z, Eletsky A, Daigham NS, et al. (2019) The operon protects from copper toxicity: CopL is an extracellular membrane-associated copper-binding protein. The Journal of Biological Chemistry |