Search Results - "Swapna, G. V. T."

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    microscale protein NMR sample screening pipeline by Rossi, Paolo, Swapna, G. V. T, Huang, Yuanpeng J, Aramini, James M, Anklin, Clemens, Conover, Kenith, Hamilton, Keith, Xiao, Rong, Acton, Thomas B, Ertekin, Asli, Everett, John K, Montelione, Gaetano T

    Published in Journal of biomolecular NMR (01-01-2010)
    “…As part of efforts to develop improved methods for NMR protein sample preparation and structure determination, the Northeast Structural Genomics Consortium…”
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    Structure of Antibacterial Peptide Microcin J25:  A 21-Residue Lariat Protoknot by Bayro, Marvin J, Mukhopadhyay, Jayanta, Swapna, G. V. T, Huang, Janet Y, Ma, Li-Chung, Sineva, Elena, Dawson, Philip E, Montelione, Gaetano T, Ebright, Richard H

    Published in Journal of the American Chemical Society (15-10-2003)
    “…The antibacterial peptide microcin J25 (MccJ25) inhibits bacterial transcription by binding within, and obstructing, the nucleotide-uptake channel of bacterial…”
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    Minimal Heterochiral de Novo Designed 4Fe–4S Binding Peptide Capable of Robust Electron Transfer by Kim, J. Dongun, Pike, Douglas H, Tyryshkin, Alexei M, Swapna, G. V. T, Raanan, Hagai, Montelione, Gaetano T, Nanda, Vikas, Falkowski, Paul G

    Published in Journal of the American Chemical Society (12-09-2018)
    “…Ambidoxin is a designed, minimal dodecapeptide consisting of alternating L and D amino acids that binds a 4Fe–4S cluster through ligand–metal interactions and…”
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    Structural Basis by Which the N‑Terminal Polypeptide Segment of Rhizopus chinensis Lipase Regulates Its Substrate Binding Affinity by Zhang, Meng, Yu, Xiao-Wei, Xu, Yan, Guo, Rey-Ting, Swapna, G. V. T, Szyperski, Thomas, Hunt, John F, Montelione, Gaetano T

    Published in Biochemistry (Easton) (24-09-2019)
    “…Members of an important group of industrial enzymes, Rhizopus lipases, exhibit valuable hydrolytic features that underlie their biological functions…”
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    Cold-shock induced high-yield protein production in Escherichia coli by Inouye, Masayori, Qing, Guoliang, Ma, Li-Chung, Khorchid, Ahmad, Swapna, G V T, Mal, Tapas K, Takayama, Masanori Mitta, Xia, Bing, Phadtare, Sangita, Ke, Haiping, Acton, Thomas, Montelione, Gaetano T, Ikura, Mitsuhiko

    Published in Nature biotechnology (01-07-2004)
    “…Overexpression of proteins in Escherichia coli at low temperature improves their solubility and stability. Here, we apply the unique features of the cspA gene…”
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    Engineering of a wheat germ expression system to provide compatibility with a high throughput pET-based cloning platform by Zhao, Li, Zhao, Kate Q, Hurst, Robin, Slater, Michael R, Acton, Thomas B, Swapna, G. V. T, Shastry, Ritu, Kornhaber, Gregory J, Montelione, Gaetano T

    “…Wheat germ cell-free methods provide an important approach for the production of eukaryotic proteins. We have developed a protein expression vector for the…”
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    Conserved Surface Features Form the Double-stranded RNA Binding Site of Non-structural Protein 1 (NS1) from Influenza A and B Viruses by Yin, Cuifeng, Khan, Javed A., Swapna, G.V.T., Ertekin, Asli, Krug, Robert M., Tong, Liang, Montelione, Gaetano T.

    Published in The Journal of biological chemistry (13-07-2007)
    “…Influenza A viruses cause a highly contagious respiratory disease in humans and are responsible for periodic widespread epidemics with high mortality rates…”
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    Efficient production of 2H, 13C, 15N-enriched industrial enzyme Rhizopus chinensis lipase with native disulfide bonds by Zhang, Meng, Yu, Xiao-Wei, Swapna, G. V. T, Xiao, Rong, Zheng, Haiyan, Sha, Chong, Xu, Yan, Montelione, Gaetano T

    Published in Microbial cell factories (13-07-2016)
    “…In order to use most modern methods of NMR spectroscopy to study protein structure and dynamics, isotope-enriched protein samples are essential. Especially for…”
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    Segmental isotope labeling of proteins for NMR structural study using a protein S tag for higher expression and solubility by Kobayashi, Hiroshi, Swapna, G. V. T., Wu, Kuen-Phon, Afinogenova, Yuliya, Conover, Kenith, Mao, Binchen, Montelione, Gaetano T., Inouye, Masayori

    Published in Journal of biomolecular NMR (01-04-2012)
    “…A common obstacle to NMR studies of proteins is sample preparation. In many cases, proteins targeted for NMR studies are poorly expressed and/or expressed in…”
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    Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold by Mani, Rajeswari, Vorobiev, Sergey, Swapna, G. V. T., Neely, Helen, Janjua, Haleema, Ciccosanti, Colleen, Xiao, Rong, Acton, Thomas B., Everett, John K., Hunt, John, Montelione, Gaetano T.

    “…The conserved Lipoprotein-17 domain of membrane-associated protein Q9PRA0_UREPA from Ureaplasma parvum was selected for structure determination by the…”
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    Effect of mitochondrial uncouplers niclosamide ethanolamine (NEN) and oxyclozanide on hepatic metastasis of colon cancer by Alasadi, Amer, Chen, Michael, Swapna, G. V. T., Tao, Hanlin, Guo, Jingjing, Collantes, Juan, Fadhil, Noor, Montelione, Gaetano T., Jin, Shengkan

    Published in Cell death & disease (13-02-2018)
    “…Metabolism of cancer cells is characterized by aerobic glycolysis, or the Warburg effect. Aerobic glycolysis reduces pyruvate flux into mitochondria,…”
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    A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins by Aiyer, Sriram, Swapna, G.V.T., Ma, Li-Chung, Liu, Gaohua, Hao, Jingzhou, Chalmers, Gordon, Jacobs, Brian C., Montelione, Gaetano T., Roth, Monica J.

    Published in Structure (London) (05-08-2021)
    “…The extraterminal (ET) domain of BRD3 is conserved among BET proteins (BRD2, BRD3, BRD4), interacting with multiple host and viral protein-protein networks…”
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    Structure Determination of Challenging Protein–Peptide Complexes Combining NMR Chemical Shift Data and Molecular Dynamics Simulations by Mondal, Arup, Swapna, G.V.T., Lopez, Maria M., Klang, Laura, Hao, Jingzhou, Ma, LiChung, Roth, Monica J., Montelione, Gaetano T., Perez, Alberto

    “…Intrinsically disordered regions of proteins often mediate important protein–protein interactions. However, the folding-upon-binding nature of many…”
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