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Krochmal, D., Roman, C., Lewicka, A., Shao, Y., and Piccirilli, J. A. (2024) Structural basis for promiscuity in ligand recognition by yjdF riboswitch. Cell Discov. 10, 37
Krochmal, D., Shao, Y., Li, N. - S., DasGupta, S., Shelke, S. A., Koirala, D., and Piccirilli, J. A. (2022) Structural basis for substrate binding and catalysis by a self-alkylating ribozyme. Nat Chem Biol. 10.1038/s41589-021-00950-z
Krishnan, V., Dwivedi, P., Kim, B. J., Samal, A., Macon, K., Ma, X., Mishra, A., Doran, K. S., Ton-That, H., and Narayana, S. V. L. (2013) Structure of Streptococcus agalactiae tip pilin GBS104: a model for GBS pili assembly and host interactions. Acta Crystallogr D Biol Crystallogr. 69, 1073-89
Krishnamurthy, H., and Gouaux, E. (2012) X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature. 481, 469-74
Krauthammer, M., Kong, Y., Ha, B. Hak, Evans, P., Bacchiocchi, A., McCusker, J. P., Cheng, E., Davis, M. J., Goh, G., Choi, M., Ariyan, S., Narayan, D., Dutton-Regester, K., Capatana, A., Holman, E. C., Bosenberg, M., Sznol, M., Kluger, H. M., Brash, D. E., Stern, D. F., Materin, M. A., Lo, R. S., Mane, S., Ma, S., Kidd, K. K., Hayward, N. K., Lifton, R. P., Schlessinger, J., Boggon, T. J., and Halaban, R. (2012) Exome sequencing identifies recurrent somatic RAC1 mutations in melanoma. Nat Genet. 44, 1006-14
Kozono, S., Lin, Y. - M., Seo, H. - S., Pinch, B., Lian, X., Qiu, C., Herbert, M. K., Chen, C. - H., Tan, L., Gao, Z. Jeff, Massefski, W., Doctor, Z. M., Jackson, B. P., Chen, Y., Dhe-Paganon, S., Lu, K. Ping, and Zhou, X. Zhen (2018) Arsenic targets Pin1 and cooperates with retinoic acid to inhibit cancer-driving pathways and tumor-initiating cells. Nat Commun. 9, 3069
Kozlov, G., Mattijssen, S., Jiang, J., Nyandwi, S., Sprules, T., Iben, J. R., Coon, S. L., Gaidamakov, S., Noronha, A. M., Wilds, C. J., Maraia, R. J., and Gehring, K. (2022) Structural basis of 3'-end poly(A) RNA recognition by LARP1. Nucleic Acids Res. 10.1093/nar/gkac696
Kovalevsky, A. Y., S Fisher, Z., Seaver, S., Mustyakimov, M., Sukumar, N., Langan, P., Mueser, T. C., and B Hanson, L. (2010) Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66, 474-7
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
Kourinov, I., Capel, M., Banerjee, S., Murphy, F., Neau, D., Perry, K., Rajashankar, K., Schuermann, J., Sukumar, N., and Ealick, S. E. (2014) NE-CAT Crystallography Beamlines for Challenging Structural Biology Research. 23rd International Union of Crystallography (IuCr) and General Assembly, August 5-12, 2014
Kourinov, I., Capel, M., Banerjee, S., A. Lynch, E., Murphy, F., Neau, D., Perry, K., Rajashankar, K., Salbego, C., Schuermann, J., Sukumar, N., Withrow, J., and Ealick, S. (2017) Northeastern Collaborative Access Team (NE-CAT) Crystallography Beam Lines for Challenging Structural Biology Research. 2017 Annual Meeting of the American Crystallographic Association, May 26-30, 2017
Kourinov, I., Capel, M., Banerjee, S., A. Lynch, E., Murphy, F., Neau, D., Perry, K., Rajashankar, K., Salbego, C., Schuermann, J., Sukumar, N., Withrow, J., and Ealick, S. (2018) NE-CAT: Crystallography Beamlines for Challenging Structural Biology Research. 2018 Annual Meeting of the American Crystallographic Association, July 20-24, 2018
Košutić, M., Neuner, S., Ren, A., Flür, S., Wunderlich, C., Mairhofer, E., Vušurović, N., Seikowski, J., Breuker, K., Höbartner, C., Patel, D. J., Kreutz, C., and Micura, R. (2015) A Mini-Twister Variant and Impact of Residues/Cations on the Phosphodiester Cleavage of this Ribozyme Class. Angew Chem Int Ed Engl. 54, 15128-15133
Kosciuk, T., Price, I. R., Zhang, X., Zhu, C., Johnson, K. N., Zhang, S., Halaby, S. L., Komaniecki, G. P., Yang, M., DeHart, C. J., Thomas, P. M., Kelleher, N. L., J Fromme, C., and Lin, H. (2020) NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle. Nat Commun. 11, 1067
Korman, T. P., Sahachartsiri, B., Charbonneau, D. M., Huang, G. L., Beauregard, M., and Bowie, J. U. (2013) Dieselzymes: development of a stable and methanol tolerant lipase for biodiesel production by directed evolution. Biotechnol Biofuels. 6, 70
Korasick, D. A., Singh, H., Pemberton, T. A., Luo, M., Dhatwalia, R., and Tanner, J. J. (2017) Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J. 10.1111/febs.14165
Korasick, D. A., Končitíková, R., Kopečná, M., Hájková, E., Vigouroux, A., Moréra, S., Becker, D. F., Šebela, M., Tanner, J. J., and Kopečný, D. (2019) Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants. J Mol Biol. 431, 576-592
Korasick, D. A., Owuocha, L. F., Kandoth, P. K., Tanner, J. J., Mitchum, M. G., and Beamer, L. J. (2023) Structural and functional analysis of two SHMT8 variants associated with soybean cyst nematode resistance. FEBS J. 10.1111/febs.16971
Kono, A., Chou, T. - H., Radhakrishnan, A., Bolla, J. Reddy, Sankar, K., Shome, S., Su, C. - C., Jernigan, R. L., Robinson, C. V., Yu, E. W., and Spalding, M. H. (2020) Structure and Function of LCI1: A plasma membrane CO channel in the Chlamydomonas CO concentrating mechanism. Plant J. 10.1111/tpj.14745
Kono, M., Ochida, A., Oda, T., Imada, T., Banno, Y., Taya, N., Masada, S., Kawamoto, T., Yonemori, K., Nara, Y., Fukase, Y., Yukawa, T., Tokuhara, H., Skene, R., Sang, B. - C., Hoffman, I. D., Snell, G. P., Uga, K., Shibata, A., Igaki, K., Nakamura, Y., Nakagawa, H., Tsuchimori, N., Yamasaki, M., Shirai, J., and Yamamoto, S. (2018) Discovery of [cis-3-({(5 R)-5-[(7-Fluoro-1,1-dimethyl-2,3-dihydro-1H-inden-5-yl)carbamoyl]-2-methoxy-7,8-dihydro-1,6-naphthyridin-6(5H)-yl}carbonyl)cyclobutyl]acetic Acid (TAK-828F) as a Potent Selective and Orally Available Novel Retinoic Acid Receptor-R. J Med Chem. 10.1021/acs.jmedchem.8b00061
Kolyadko, V. N., Layzer, J. M., Perry, K., Sullenger, B. A., and Krishnaswamy, S. (2024) An RNA aptamer exploits exosite-dependent allostery to achieve specific inhibition of coagulation factor IXa. Proc Natl Acad Sci U S A. 121, e2401136121
Kolli, N., and Garman, S. C. (2014) Proteolytic activation of human cathepsin A. J Biol Chem. 289, 11592-600
Kolesiński, P., McGowan, M., Botteaux, A., Smeesters, P. R., and Ghosh, P. (2024) Conservation of C4BP-binding sequence patterns in Streptococcus pyogenes M and Enn proteins. J Biol Chem. 300, 107478
Köksal, M., Hu, H., Coates, R. M., Peters, R. J., and Christianson, D. W. (2011) Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase. Nat Chem Biol. 7, 431-3
Koirala, D., Lewicka, A., Koldobskaya, Y., Huang, H., and Piccirilli, J. A. (2019) Synthetic Antibody Binding to a Preorganized RNA Domain of Hepatitis C Virus Internal Ribosome Entry Site Inhibits Translation. ACS Chem Biol. 10.1021/acschembio.9b00785

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