Found 68 results
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Journal Article
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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., 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
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
Li, N., Shi, K., Rao, T., Banerjee, S., and Aihara, H. (2020) Structural insights into the promiscuous DNA binding and broad substrate selectivity of fowlpox virus resolvase. Sci Rep. 10, 393
Sui, X., Weitz, A. C., Farquhar, E. R., Badiee, M., Banerjee, S., von Lintig, J., Tochtrop, G. P., Palczewski, K., Hendrich, M. P., and Kiser, P. D. (2017) Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center. Biochemistry. 56, 2836-2852
Ayres, C. A., Schormann, N., Senkovich, O., Fry, A., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2014) Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface. Acta Crystallogr F Struct Biol Commun. 70, 1333-9