Publications

Found 77 results
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Journal Article
Hofmann, L., Tsybovsky, Y., Alexander, N. S., Babino, D., Leung, N. Y., Montell, C., Banerjee, S., von Lintig, J., and Palczewski, K. (2016) Structural Insights into the Drosophila melanogaster Retinol Dehydrogenase, a Member of the Short-Chain Dehydrogenase/Reductase Family. Biochemistry. 55, 6545-6557
Shi, K., Oakland, J. T., Kurniawan, F., Moeller, N. H., Banerjee, S., and Aihara, H. (2020) Structural basis of superinfection exclusion by bacteriophage T4 Spackle. Commun Biol. 3, 691
Shi, K., Carpenter, M. A., Banerjee, S., Shaban, N. M., Kurahashi, K., Salamango, D. J., McCann, J. L., Starrett, G. J., Duffy, J. V., Demir, Ö., Amaro, R. E., Harki, D. A., Harris, R. S., and Aihara, H. (2017) Structural basis for targeted DNA cytosine deamination and mutagenesis by APOBEC3A and APOBEC3B. Nat Struct Mol Biol. 24, 131-139
Shi, K., Moeller, N. H., Banerjee, S., McCann, J. L., Carpenter, M. A., Yin, L., Moorthy, R., Orellana, K., Harki, D. A., Harris, R. S., and Aihara, H. (2021) Structural basis for recognition of distinct deaminated DNA lesions by endonuclease Q. Proc Natl Acad Sci U S A. 10.1073/pnas.2021120118
Clarke, O. B., Tomasek, D., Jorge, C. D., Dufrisne, M. Belcher, Kim, M., Banerjee, S., Rajashankar, K. R., Shapiro, L., Hendrickson, W. A., Santos, H., and Mancia, F. (2015) Structural basis for phosphatidylinositol-phosphate biosynthesis. Nat Commun. 6, 8505
Li, J., Ma, X., Banerjee, S., Baruah, S., Schnicker, N. J., Roh, E., Ma, W., Liu, K., Bode, A. M., and Dong, Z. (2020) Structural basis for multifunctional roles of human Ints3 C-terminal domain. J Biol Chem. 10.1074/jbc.RA120.016393
Patra, A., Banerjee, S., Salyard, T. L. Johnson, Malik, C. K., Christov, P. P., Rizzo, C. J., Stone, M. P., and Egli, M. (2015) Structural Basis for Error-Free Bypass of the 5-N-Methylformamidopyrimidine-dG Lesion by Human DNA Polymerase η and Sulfolobus solfataricus P2 Polymerase IV.. J Am Chem Soc. 137, 7011-4
Sciara, G., Clarke, O. B., Tomasek, D., Kloss, B., Tabuso, S., Byfield, R., Cohn, R., Banerjee, S., Rajashankar, K. R., Slavkovic, V., Graziano, J. H., Shapiro, L., and Mancia, F. (2014) Structural basis for catalysis in a CDP-alcohol phosphotransferase. Nat Commun. 5, 4068
Dufrisne, M. Belcher, Jorge, C. D., Timóteo, C. G., Petrou, V. I., Ashraf, K. U., Banerjee, S., Clarke, O. B., Santos, H., and Mancia, F. (2020) Structural and Functional Characterization of Phosphatidylinositol-Phosphate Biosynthesis in Mycobacteria. J Mol Biol. 10.1016/j.jmb.2020.04.028
Brown, K. L., Banerjee, S., Feigley, A., Abe, H., Blackwell, T. S., Pozzi, A., Hudson, B. G., and Zent, R. (2018) Salt-bridge modulates differential calcium-mediated ligand binding to integrin α1- and α2-I domains.. Sci Rep. 8, 2916
Duggan, K. C., Hermanson, D. J., Musee, J., Prusakiewicz, J. J., Scheib, J. L., Carter, B. D., Banerjee, S., Oates, J. A., and Marnett, L. J. (2011) (R)-Profens are substrate-selective inhibitors of endocannabinoid oxygenation by COX-2. Nat Chem Biol. 7, 803-9
Shanmugam, G., Minko, I. G., Banerjee, S., Christov, P. P., Kozekov, I. D., Rizzo, C. J., R Lloyd, S., Egli, M., and Stone, M. P. (2013) Ring-opening of the γ-OH-PdG adduct promotes error-free bypass by the Sulfolobus solfataricus DNA polymerase Dpo4.. Chem Res Toxicol. 26, 1348-60
Schormann, N., Zhukovskaya, N., Bedwell, G., Nuth, M., Gillilan, R., Prevelige, P. E., Ricciardi, R. P., Banerjee, S., and Chattopadhyay, D. (2016) Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases. Protein Sci. 25, 2113-2131
Gulati, S., Jastrzebska, B., Banerjee, S., Placeres, Á. L., Miszta, P., Gao, S., Gunderson, K., Tochtrop, G. P., Filipek, S., Katayama, K., Kiser, P. D., Mogi, M., Stewart, P. L., and Palczewski, K. (2017) Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism. Proc Natl Acad Sci U S A. 114, E2608-E2615
Xu, S., Hermanson, D. J., Banerjee, S., Ghebreselasie, K., Clayton, G. M., R Garavito, M., and Marnett, L. J. (2014) Oxicams bind in a novel mode to the cyclooxygenase active site via a two-water-mediated H-bonding Network. J Biol Chem. 289, 6799-808
Schormann, N., Hayden, K. L., Lee, P., Banerjee, S., and Chattopadhyay, D. (2019) An overview of structure, function, and regulation of pyruvate kinases. Protein Sci. 10.1002/pro.3691
Ketkar, A., Zafar, M. K., Banerjee, S., Marquez, V. E., Egli, M., and Eoff, R. L. (2012) A nucleotide-analogue-induced gain of function corrects the error-prone nature of human DNA polymerase iota. J Am Chem Soc. 134, 10698-705
Kourinov, I., Capel, M., Banerjee, S., Murphy, F., Neau, D., Perry, K., Rajashankar, K., Schuermann, J., Sukumar, N., and Ealick, S. (2018) Northeastern Collaborative Access Team (NE-CAT) crystallography beamlines for challenging structural biology research. Acta Crystallographica Section A Foundations and Advances. 74, a97-a97
Neumann, W., Xu, S., Sárosi, M. B., Scholz, M. S., Crews, B. C., Ghebreselasie, K., Banerjee, S., Marnett, L. J., and Hey-Hawkins, E. (2016) nido-Dicarbaborate Induces Potent and Selective Inhibition of Cyclooxygenase-2. ChemMedChem. 11, 175-8
Silvaroli, J. A., Plau, J., Adams, C. H., Banerjee, S., Widjaja-Adhi, M. Airanthi K., Blaner, W. S., and Golczak, M. (2021) Molecular basis for the interaction of cellular retinol-binding protein 2 (CRBP2) with non-retinoid ligands. J Lipid Res. 10.1016/j.jlr.2021.100054
Ubah, O. C., Lake, E. W., Gunaratne, G. S., Gallant, J. P., Fernie, M., Robertson, A. J., Marchant, J. S., Bold, T. D., Langlois, R. A., Matchett, W. E., Thiede, J. M., Shi, K., Yin, L., Moeller, N. H., Banerjee, S., Ferguson, L., Kovaleva, M., Porter, A. J., Aihara, H., LeBeau, A. M., and Barelle, C. J. (2021) Mechanisms of SARS-CoV-2 neutralization by shark variable new antigen receptors elucidated through X-ray crystallography. Nat Commun. 12, 7325
Silvaroli, J. A., Arne, J. M., Chelstowska, S., Kiser, P. D., Banerjee, S., and Golczak, M. (2016) Ligand Binding Induces Conformational Changes in Human Cellular Retinol-binding Protein 1 (CRBP1) Revealed by Atomic Resolution Crystal Structures. J Biol Chem. 291, 8528-40
Ketkar, A., Zafar, M. K., Maddukuri, L., Yamanaka, K., Banerjee, S., Egli, M., Choi, J. - Y., R Lloyd, S., and Eoff, R. L. (2013) Leukotriene biosynthesis inhibitor MK886 impedes DNA polymerase activity. Chem Res Toxicol. 26, 221-32
Uddin, M. Jashim, Xu, S., Crews, B. C., Aleem, A. M., Ghebreselasie, K., Banerjee, S., and Marnett, L. J. (2020) Harmaline Analogs as Substrate-Selective Cyclooxygenase-2 Inhibitors. ACS Med Chem Lett. 11, 1881-1885
Chae, P. Seok, Rana, R. R., Gotfryd, K., Rasmussen, S. G. F., Kruse, A. C., Cho, K. Ho, Capaldi, S., Carlsson, E., Kobilka, B., Loland, C. J., Gether, U., Banerjee, S., Byrne, B., Lee, J. K., and Gellman, S. H. (2013) Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study. Chem Commun (Camb). 49, 2287-9

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