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  • (-) Publication Year = 2006 - 2018
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CLASP Suppresses Microtubule Catastrophes through a Single TOG Domain
Aher, A., Kok, M., Sharma, A., Rai, A., Olieric, N., Rodriguez-Garcia, R., … Akhmanova, A. (2018). CLASP Suppresses Microtubule Catastrophes through a Single TOG Domain. Developmental Cell, 46(1), 40-58. https://doi.org/10.1016/j.devcel.2018.05.032
Study of magneto-electric coupling between ultra-thin Fe films and PMN-PT using X-ray magnetic circular dichroism
Avula, S. R. V., Heidler, J., Dreiser, J., Vijayakumar, J., Howald, L., Nolting, F., & Piamonteze, C. (2018). Study of magneto-electric coupling between ultra-thin Fe films and PMN-PT using X-ray magnetic circular dichroism. Journal of Applied Physics, 123(6), 64103. https://doi.org/10.1063/1.5002530
Botulinum neurotoxin diversity from a gene-centered view
Benoit, R. M. (2018). Botulinum neurotoxin diversity from a gene-centered view. Toxins, 10(8), 310 (14 pp.). https://doi.org/10.3390/toxins10080310
Interaction between the <i>Caenorhabditis elegans</i> centriolar protein SAS-5 and microtubules facilitates organelle assembly
Bianchi, S., Rogala, K. B., Dynes, N. J., Hilbert, M., Leidel, S. A., Steinmetz, M. O., … Vakonakis, I. (2018). Interaction between the Caenorhabditis elegans centriolar protein SAS-5 and microtubules facilitates organelle assembly. Molecular Biology of the Cell, 29(6), 722-735. https://doi.org/10.1091/mbc.E17-06-0412
High-affinity ligands of the colchicine domain in tubulin based on a structure-guided design
Bueno, O., ficas, M., Estévez Gallego, J., Martins, S., Prota, A. E., Gago, F., … ficas, M. (2018). High-affinity ligands of the colchicine domain in tubulin based on a structure-guided design. Scientific Reports, 8(1), 4242. https://doi.org/10.1038/s41598-018-22382-x
Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals
Casadei, C. M., Tsai, C. J., Barty, A., Hunter, M. S., Zatsepin, N. A., Padeste, C., … Frank, M. (2018). Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals. IUCrJ, 5(1), 103-117. https://doi.org/10.1107/S2052252517017043
Electron diffraction and three-dimensional crystallography for structural biology
Clabbers, M. T. B., & Abrahams, J. P. (2018). Electron diffraction and three-dimensional crystallography for structural biology. Crystallography Reviews, 24(3), 176-204. https://doi.org/10.1080/0889311X.2018.1446427
Electron diffraction data processing with <i>DIALS</i>
Clabbers, M. T. B., Gruene, T., Parkhurst, J. M., Abrahams, J. P., & Waterman, D. G. (2018). Electron diffraction data processing with DIALS. Acta Crystallographica Section D: Structural Biology, 74(6), 506-518. https://doi.org/10.1107/S2059798318007726
Quinazolinone-Based Anticancer Agents: Synthesis, Antiproliferative SAR, Antitubulin Activity, and Tubulin Co-crystal Structure
Dohle, W., Jourdan, F. L., Menchon, G., Prota, A. E., Foster, P. A., Mannion, P., … Potter, B. V. L. (2018). Quinazolinone-Based Anticancer Agents: Synthesis, Antiproliferative SAR, Antitubulin Activity, and Tubulin Co-crystal Structure. Journal of Medicinal Chemistry, 61(3), 1031-1044. https://doi.org/10.1021/acs.jmedchem.7b01474
Zampanolide binding to tubulin indicates cross-talk of taxane site with colchicine and nucleotide sites
Field, J. J., Pera, B., Estévez Gallego, J., Calvo, E., Rodríguez-Salarichs, J., Sáez-Calvo, G., … Díaz, J. F. (2018). Zampanolide binding to tubulin indicates cross-talk of taxane site with colchicine and nucleotide sites. Journal of Natural Products, 81(3), 494-505. https://doi.org/10.1021/acs.jnatprod.7b00704
Convergent evolution of tertiary structure in rhodopsin visual proteins from vertebrates and box jellyfish
Gerrard, E., Mutt, E., Nagata, T., Koyanagi, M., Flock, T., Lesca, E., … Lucas, R. J. (2018). Convergent evolution of tertiary structure in rhodopsin visual proteins from vertebrates and box jellyfish. Proceedings of the National Academy of Sciences of the United States of America PNAS, 115(24), 6201-6206. https://doi.org/10.1073/pnas.1721333115
Expression and purification of the mammalian translocator protein for structural studies
Graeber, E., & Korkhov, V. M. (2018). Expression and purification of the mammalian translocator protein for structural studies. PLoS One, 13(6), 198832. https://doi.org/10.1371/journal.pone.0198832
Characterization at the Level of Individual Crystals: Single-Crystal MFI Type Zeolite Grains
Gruene, T., Li, T., van Genderen, E., Pinar, A. B., & van Bokhoven, J. A. (2018). Characterization at the Level of Individual Crystals: Single-Crystal MFI Type Zeolite Grains. Chemistry: A European Journal, 24(10), 2384-2388. https://doi.org/10.1002/chem.201704213
Frontispiece: Characterization at the Level of Individual Crystals: Single-Crystal MFI Type Zeolite Grains
Gruene, T., Li, T., van Genderen, E., Pinar, A. B., & van Bokhoven, J. A. (2018). Frontispiece: Characterization at the Level of Individual Crystals: Single-Crystal MFI Type Zeolite Grains. Chemistry: A European Journal, 24, 2384. https://doi.org/10.1002/chem.201881065
Rapid Structure Determination of Microcrystalline Molecular Compounds Using Electron Diffraction
Gruene, T., Wennmacher, J. T. C., Zaubitzer, C., Holstein, J. J., Heidler, J., Fecteau-Lefebvre, A., … Pantelic, R. (2018). Rapid Structure Determination of Microcrystalline Molecular Compounds Using Electron Diffraction. Angewandte Chemie International Edition, 57(50), 16313-16317. https://doi.org/10.1002/anie.201811318
OMNY – a tOMography Nano crYo stage
Holler, M., Raabe, J., Diaz, A., Guizar-Sicairos, M., Wepf, R., Odstrcil, M., … Bunk, O. (2018). OMNY – a tOMography Nano crYo stage. Review of Scientific Instruments, 89(4), 043706 (13 pp.). https://doi.org/10.1063/1.5020247
Enzyme catalysis captured using multiple structures from one crystal at varying temperatures
Horrell, S., Kekilli, D., Sen, K., Owen, R. L., Dworkowski, F. S. N., Antonyuk, S. V., … Hough, M. A. (2018). Enzyme catalysis captured using multiple structures from one crystal at varying temperatures. IUCrJ, 5, 283-292. https://doi.org/10.1107/S205225251800386X
In situ serial crystallography for rapid de novo membrane protein structure determination.
Huang, C. Y., Olieric, V., Howe, N., Warshamanage, R., Weinert, T., Panepucci, E., … Wang, M. (2018). In situ serial crystallography for rapid de novo membrane protein structure determination. Communications Biology, 1, 124 (8 pp.). https://doi.org/10.1038/S42003-018-0123-6
Resonant Ptychographic Tomography Facilitates Three-Dimensional Quantitative Colocalization of Catalyst Components and Chemical Elements
Ihli, J., Diaz, A., Shu, Y., Guizar-Sicairos, M., Holler, M., Wakonig, K., … Menzel, A. (2018). Resonant Ptychographic Tomography Facilitates Three-Dimensional Quantitative Colocalization of Catalyst Components and Chemical Elements. Journal of Physical Chemistry C, 122(40), 22920-22929. https://doi.org/10.1021/acs.jpcc.8b05624
Development of smart optical gels with highly magnetically responsive bicelles
Isabettini, S., Stucki, S., Massabni, S., Baumgartner, M. E., Reckey, P. Q., Kohlbrecher, J., … Kuster, S. (2018). Development of smart optical gels with highly magnetically responsive bicelles. ACS Applied Materials and Interfaces, 10(10), 8926-8936. https://doi.org/10.1021/acsami.7b17134
 

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