Staff Publications

Yang, H., Gao, P., Rajashankar, K. R., and Patel, D. J. (2016) PAM-Dependent Target DNA Recognition and Cleavage by C2c1 CRISPR-Cas Endonuclease. Cell. 167, 1814-1828.e12
Clark, N. E., Katolik, A., Roberts, K. M., Taylor, A. B., Holloway, S. P., Schuermann, J. P., Montemayor, E. J., Stevens, S. W., Fitzpatrick, P. F., Damha, M. J., and P Hart, J. (2016) Metal dependence and branched RNA cocrystal structures of the RNA lariat debranching enzyme Dbr1. Proc Natl Acad Sci U S A. 113, 14727-14732
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
Rechkoblit, O., Gupta, Y. K., Malik, R., Rajashankar, K. R., Johnson, R. E., Prakash, L., Prakash, S., and Aggarwal, A. K. (2016) Structure and mechanism of human PrimPol, a DNA polymerase with primase activity. Sci Adv. 2, e1601317
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
Coloma, J., Jain, R., Rajashankar, K. R., García-Sastre, A., and Aggarwal, A. K. (2016) Structures of NS5 Methyltransferase from Zika Virus. Cell Rep. 16, 3097-102
Uddin, M. Jashim, Crews, B. C., Xu, S., Ghebreselasie, K., Daniel, C. K., Kingsley, P. J., Banerjee, S., and Marnett, L. J. (2016) Antitumor Activity of Cytotoxic Cyclooxygenase-2 Inhibitors. ACS Chem Biol. 11, 3052-3060
Gao, P., Yang, H., Rajashankar, K. R., Huang, Z., and Patel, D. J. (2016) Type V CRISPR-Cas Cpf1 endonuclease employs a unique mechanism for crRNA-mediated target DNA recognition. Cell Res. 26, 901-13
Doamekpor, S. K., Lee, J. - W., Hepowit, N. L., Wu, C., Charenton, C., Leonard, M., Bengtson, M. H., Rajashankar, K. R., Sachs, M. S., Lima, C. D., and Joazeiro, C. A. P. (2016) Structure and function of the yeast listerin (Ltn1) conserved N-terminal domain in binding to stalled 60S ribosomal subunits. Proc Natl Acad Sci U S A. 113, E4151-60
Yao, G., Zhang, S., Mahrhold, S., Lam, K. - H., Stern, D., Bagramyan, K., Perry, K., Kalkum, M., Rummel, A., Dong, M., and Jin, R. (2016) N-linked glycosylation of SV2 is required for binding and uptake of botulinum neurotoxin A. Nat Struct Mol Biol. 23, 656-62
Tabackman, A. A., Frankson, R., Marsan, E. S., Perry, K., and Cole, K. E. (2016) Structure of 'linkerless' hydroxamic acid inhibitor-HDAC8 complex confirms the formation of an isoform-specific subpocket. J Struct Biol. 195, 373-378
Li, H., Hwang, Y., Perry, K., Bushman, F., and Van Duyne, G. D. (2016) Structure and Metal Binding Properties of a Poxvirus Resolvase. J Biol Chem. 291, 11094-104
Yin, Z., Shi, K., Banerjee, S., Pandey, K. K., Bera, S., Grandgenett, D. P., and Aihara, H. (2016) Crystal structure of the Rous sarcoma virus intasome. Nature. 530, 362-6
Chattopadhyay, D., Swingle, M. R., Salter, E. A., Wood, E., D'Arcy, B., Zivanov, C., Abney, K., Musiyenko, A., Rusin, S. F., Kettenbach, A., Yet, L., Schroeder, C. E., Golden, J. E., Dunham, W. H., Gingras, A. - C., Banerjee, S., Forbes, D., Wierzbicki, A., and Honkanen, R. E. (2016) Crystal structures and mutagenesis of PPP-family ser/thr protein phosphatases elucidate the selectivity of cantharidin and novel norcantharidin-based inhibitors of PP5C. Biochem Pharmacol. 109, 14-26
Lim, D. Young, Shin, S. Ho, Lee, M. - H., Malakhova, M., Kurinov, I., Wu, Q., Xu, J., Jiang, Y., Dong, Z., Liu, K., Lee, K. Yeong, Bae, K. Beom, Choi, B. Young, Deng, Y., Bode, A., and Dong, Z. (2016) A natural small molecule, catechol, induces c-Myc degradation by directly targeting ERK2 in lung cancer. Oncotarget. 7, 35001-14
Gorelik, M., Orlicky, S., Sartori, M. A., Tang, X., Marcon, E., Kurinov, I., Greenblatt, J. F., Tyers, M., Moffat, J., Sicheri, F., and Sidhu, S. S. (2016) Inhibition of SCF ubiquitin ligases by engineered ubiquitin variants that target the Cul1 binding site on the Skp1-F-box interface. Proc Natl Acad Sci U S A. 113, 3527-32
Dhindwal, S., Gomez-Gil, L., Neau, D. B., Pham, T. Thanh My, Sylvestre, M., Eltis, L. D., Bolin, J. T., and Kumar, P. (2016) Structural Basis of the Enhanced Pollutant-Degrading Capabilities of an Engineered Biphenyl Dioxygenase. J Bacteriol. 198, 1499-512
Meyer, P. A., Socias, S., Key, J., Ransey, E., Tjon, E. C., Buschiazzo, A., Lei, M., Botka, C., Withrow, J., Neau, D., Rajashankar, K., Anderson, K. S., Baxter, R. H., Blacklow, S. C., Boggon, T. J., Bonvin, A. M. J. J., Borek, D., Brett, T. J., Caflisch, A., Chang, C. - I., Chazin, W. J., Corbett, K. D., Cosgrove, M. S., Crosson, S., Dhe-Paganon, S., Di Cera, E., Drennan, C. L., Eck, M. J., Eichman, B. F., Fan, Q. R., Ferré-D'Amaré, A. R., J Fromme, C., K Garcia, C., Gaudet, R., Gong, P., Harrison, S. C., Heldwein, E. E., Jia, Z., Keenan, R. J., Kruse, A. C., Kvansakul, M., McLellan, J. S., Modis, Y., Nam, Y., Otwinowski, Z., Pai, E. F., Pereira, P. José Barb, Petosa, C., Raman, C. S., Rapoport, T. A., Roll-Mecak, A., Rosen, M. K., Rudenko, G., Schlessinger, J., Schwartz, T. U., Shamoo, Y., Sondermann, H., Tao, Y. J., Tolia, N. H., Tsodikov, O. V., Westover, K. D., Wu, H., Foster, I., Fraser, J. S., Maia, F. R. N. C., Gonen, T., Kirchhausen, T., Diederichs, K., Crosas, M., and Sliz, P. (2016) Data publication with the structural biology data grid supports live analysis. Nat Commun. 7, 10882
Hayes, R. P., Xiao, Y., Ding, F., van Erp, P. B. G., Rajashankar, K., Bailey, S., Wiedenheft, B., and Ke, A. (2016) Structural basis for promiscuous PAM recognition in type I-E Cascade from E. coli. Nature. 530, 499-503
Petrou, V. I., Herrera, C. M., Schultz, K. M., Clarke, O. B., Vendome, J., Tomasek, D., Banerjee, S., Rajashankar, K. R., Dufrisne, M. Belcher, Kloss, B., Kloppmann, E., Rost, B., Klug, C. S., M Trent, S., Shapiro, L., and Mancia, F. (2016) Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation. Science. 351, 608-12
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
Silvers, M. A., Pakhomova, S., Neau, D. B., Silvers, W. C., Anzalone, N., Taylor, C. M., and Waldrop, G. L. (2016) Crystal Structure of Carboxyltransferase from Staphylococcus aureus Bound to the Antibacterial Agent Moiramide B. Biochemistry. 55, 4666-74
Geng, Y., Mosyak, L., Kurinov, I., Zuo, H., Sturchler, E., Cheng, T. Cheung, Subramanyam, P., Brown, A. P., Brennan, S. C., Mun, H. - C., Bush, M., Chen, Y., Nguyen, T. X., Cao, B., Chang, D. D., Quick, M., Conigrave, A. D., Colecraft, H. M., McDonald, P., and Fan, Q. R. (2016) Structural mechanism of ligand activation in human calcium-sensing receptor. Elife. 10.7554/eLife.13662
Szulik, M. W., Pallan, P. S., Nocek, B., Voehler, M., Banerjee, S., Brooks, S., Joachimiak, A., Egli, M., Eichman, B. F., and Stone, M. P. (2015) Differential stabilities and sequence-dependent base pair opening dynamics of Watson-Crick base pairs with 5-hydroxymethylcytosine, 5-formylcytosine, or 5-carboxylcytosine. Biochemistry. 54, 1294-305
Schormann, N., Banerjee, S., Ricciardi, R., and Chattopadhyay, D. (2015) Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase. BMC Struct Biol. 15, 10
Ren, A., Wang, X. C., Kellenberger, C. A., Rajashankar, K. R., Jones, R. A., Hammond, M. C., and Patel, D. J. (2015) Structural basis for molecular discrimination by a 3',3'-cGAMP sensing riboswitch. Cell Rep. 11, 1-12
Ren, A., Rajashankar, K. R., and Patel, D. J. (2015) Global RNA Fold and Molecular Recognition for a pfl Riboswitch Bound to ZMP, a Master Regulator of One-Carbon Metabolism. Structure. 23, 1375-1381
Mir, A., Chen, J., Robinson, K., Lendy, E., Goodman, J., Neau, D., and Golden, B. L. (2015) Two Divalent Metal Ions and Conformational Changes Play Roles in the Hammerhead Ribozyme Cleavage Reaction. Biochemistry. 54, 6369-81
Murphy, M. W., Lee, J. K., Rojo, S., Gearhart, M. D., Kurahashi, K., Banerjee, S., Loeuille, G. - A., Bashamboo, A., McElreavey, K., Zarkower, D., Aihara, H., and Bardwell, V. J. (2015) An ancient protein-DNA interaction underlying metazoan sex determination. Nat Struct Mol Biol. 22, 442-51
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
Kudalkar, S. N., Nikas, S. P., Kingsley, P. J., Xu, S., Galligan, J. J., Rouzer, C. A., Banerjee, S., Ji, L., Eno, M. R., Makriyannis, A., and Marnett, L. J. (2015) 13-Methylarachidonic acid is a positive allosteric modulator of endocannabinoid oxygenation by cyclooxygenase. J Biol Chem. 290, 7897-909
Lee, K., Lam, K. - H., Kruel, A. - M., Mahrhold, S., Perry, K., Cheng, L. W., Rummel, A., and Jin, R. (2015) Inhibiting oral intoxication of botulinum neurotoxin A complex by carbohydrate receptor mimics. Toxicon. 107, 43-9
Lye, M. F., Sharma, M., Omari, K. El, Filman, D. J., Schuermann, J. P., Hogle, J. M., and Coen, D. M. (2015) Unexpected features and mechanism of heterodimer formation of a herpesvirus nuclear egress complex. EMBO J. 34, 2937-52
Matarlo, J. S., Evans, C. E., Sharma, I., Lavaud, L. J., Ngo, S. C., Shek, R., Rajashankar, K. R., French, J. B., Tan, D. S., and Tonge, P. J. (2015) Mechanism of MenE inhibition by acyl-adenylate analogues and discovery of novel antibacterial agents. Biochemistry. 54, 6514-6524
Harris, G. G., Lombardi, P. M., Pemberton, T. A., Matsui, T., Weiss, T. M., Cole, K. E., Köksal, M., Murphy, F. V., L Vedula, S., Chou, W. K. W., Cane, D. E., and Christianson, D. W. (2015) Structural Studies of Geosmin Synthase, a Bifunctional Sesquiterpene Synthase with αα Domain Architecture That Catalyzes a Unique Cyclization-Fragmentation Reaction Sequence.. Biochemistry. 54, 7142-55

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