Publications

Found 1383 results
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2011
Xia, S., Wang, M., Lee, H. R., Sinha, A., Blaha, G., Christian, T., Wang, J., and Konigsberg, W. (2011) Variation in mutation rates caused by RB69pol fidelity mutants can be rationalized on the basis of their kinetic behavior and crystal structures. J Mol Biol. 406, 558-70
2010
Rosen, M. D., Venkatesan, H., Peltier, H. M., Bembenek, S. D., Kanelakis, K. C., Zhao, L. X., Leonard, B. E., Hocutt, F. M., Wu, X., Palomino, H. L., Brondstetter, T. I., Haugh, P. V., Cagnon, L., Yan, W., Liotta, L. A., Young, A., Mirzadegan, T., Shankley, N. P., Barrett, T. D., and Rabinowitz, M. H. (2010) Benzimidazole-2-pyrazole HIF Prolyl 4-Hydroxylase Inhibitors as Oral Erythropoietin Secretagogues. ACS Med Chem Lett. 1, 526-9
Freeman, M. M., Seaman, M. S., Rits-Volloch, S., Hong, X., Kao, C. - Y., Ho, D. D., and Chen, B. (2010) Crystal structure of HIV-1 primary receptor CD4 in complex with a potent antiviral antibody. Structure. 18, 1632-41
Malakhova, M., D'Angelo, I., Kim, H. - G., Kurinov, I., Bode, A. M., and Dong, Z. (2010) The crystal structure of the active form of the C-terminal kinase domain of mitogen- and stress-activated protein kinase 1. J Mol Biol. 399, 41-52
Malakhova, M., D'Angelo, I., Kim, H. - G., Kurinov, I., Bode, A. M., and Dong, Z. (2010) The crystal structure of the active form of the C-terminal kinase domain of mitogen- and stress-activated protein kinase 1. J Mol Biol. 399, 41-52
Matsuura, H., Kirschner, A. N., Longnecker, R., and Jardetzky, T. S. (2010) Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex. Proc Natl Acad Sci U S A. 107, 22641-6
Arbing, M. A., Kaufmann, M., Phan, T., Chan, S., Cascio, D., and Eisenberg, D. (2010) The crystal structure of the Mycobacterium tuberculosis Rv3019c-Rv3020c ESX complex reveals a domain-swapped heterotetramer. Protein Sci. 19, 1692-703
Arbing, M. A., Handelman, S. K., Kuzin, A. P., Verdon, G., Wang, C., Su, M., Rothenbacher, F. P., Abashidze, M., Liu, M., Hurley, J. M., Xiao, R., Acton, T., Inouye, M., Montelione, G. T., Woychik, N. A., and Hunt, J. F. (2010) Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems. Structure. 18, 996-1010
Day, J. E., Hall, ii, T., Pegg, L. E., Benson, T. E., Hausmann, J., and Kamtekar, S. (2010) Crystallization and preliminary X-ray diffraction analysis of rat autotaxin. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66, 1127-9
Dutta, S., Gullá, S., T Chen, S., Fire, E., Grant, R. A., and Keating, A. E. (2010) Determinants of BH3 binding specificity for Mcl-1 versus Bcl-xL. J Mol Biol. 398, 747-62
Banigan, J. R., Mandal, K., Sawaya, M. R., Thammavongsa, V., Hendrickx, A. P. A., Schneewind, O., Yeates, T. O., and Kent, S. B. H. (2010) Determination of the X-ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography. Protein Sci. 19, 1840-9
Zhang, Y., Zhu, X., Torelli, A. T., Lee, M., Dzikovski, B., Koralewski, R. M., Wang, E., Freed, J., Krebs, C., Ealick, S. E., and Lin, H. (2010) Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. Nature. 465, 891-6
Zhang, Y., Zhu, X., Torelli, A. T., Lee, M., Dzikovski, B., Koralewski, R. M., Wang, E., Freed, J., Krebs, C., Ealick, S. E., and Lin, H. (2010) Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. Nature. 465, 891-6
Scott, D. C., Monda, J. K., Grace, C. R. R., Duda, D. M., Kriwacki, R. W., Kurz, T., and Schulman, B. A. (2010) A dual E3 mechanism for Rub1 ligation to Cdc53. Mol Cell. 39, 784-96
Scott, D. C., Monda, J. K., Grace, C. R. R., Duda, D. M., Kriwacki, R. W., Kurz, T., and Schulman, B. A. (2010) A dual E3 mechanism for Rub1 ligation to Cdc53. Mol Cell. 39, 784-96
Wang, L., Yang, J. Kuk, Kabaleeswaran, V., Rice, A. J., Cruz, A. C., Park, A. Young, Yin, Q., Damko, E., Jang, S. Bok, Raunser, S., Robinson, C. V., Siegel, R. M., Walz, T., and Wu, H. (2010) The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nat Struct Mol Biol. 17, 1324-9
Fuse, S., Tsukamoto, H., Yuan, Y., Wang, T. - S. Andrew, Zhang, Y., Bolla, M., Walker, S., Sliz, P., and Kahne, D. (2010) Functional and structural analysis of a key region of the cell wall inhibitor moenomycin. ACS Chem Biol. 5, 701-11
Mueser, T. C., Griffith, W. P., Kovalevsky, A. Y., Guo, J., Seaver, S., Langan, P., and B Hanson, L. (2010) Hemoglobin redux: combining neutron and X-ray diffraction with mass spectrometry to analyse the quaternary state of oxidized hemoglobins. Acta Crystallogr D Biol Crystallogr. 66, 1249-56
Cotner-Gohara, E., Kim, I. - K., Hammel, M., Tainer, J. A., Tomkinson, A. E., and Ellenberger, T. (2010) Human DNA ligase III recognizes DNA ends by dynamic switching between two DNA-bound states. Biochemistry. 49, 6165-76
Subramanian, R., Wilson-Kubalek, E. M., Arthur, C. P., Bick, M. J., Campbell, E. A., Darst, S. A., Milligan, R. A., and Kapoor, T. M. (2010) Insights into antiparallel microtubule crosslinking by PRC1, a conserved nonmotor microtubule binding protein. Cell. 142, 433-43
Stewart, M. L., Fire, E., Keating, A. E., and Walensky, L. D. (2010) The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer. Nat Chem Biol. 6, 595-601
Fire, E., Gullá, S. V., Grant, R. A., and Keating, A. E. (2010) Mcl-1-Bim complexes accommodate surprising point mutations via minor structural changes. Protein Sci. 19, 507-19
Rechkoblit, O., Kolbanovskiy, A., Malinina, L., Geacintov, N. E., Broyde, S., and Patel, D. J. (2010) Mechanism of error-free and semitargeted mutagenic bypass of an aromatic amine lesion by Y-family polymerase Dpo4. Nat Struct Mol Biol. 17, 379-88
Demirci, H., Murphy, F., Belardinelli, R., Kelley, A. C., Ramakrishnan, V., Gregory, S. T., Dahlberg, A. E., and Jogl, G. (2010) Modification of 16S ribosomal RNA by the KsgA methyltransferase restructures the 30S subunit to optimize ribosome function. RNA. 16, 2319-24
Khare, B., Samal, A., Vengadesan, K., Rajashankar, K. R., Ma, X., I Huang, H., Ton-That, H., and Narayana, S. V. L. (2010) Preliminary crystallographic study of the Streptococcus agalactiae sortases, sortase A and sortase C1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66, 1096-100

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