다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기
Angewandte Chemie. international edition, v.49 no.28, 2010년, pp.4809 - 4812
Kubicek, Karel (Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gö) , Grimm, S. Kaspar (ttingen (Germany)) , Orts, Julien (Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gö) , Sasse, Florenz (ttingen (Germany)) , Carlomagno, Teresa (EMBL, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg (Germany))
AI-Helper
Graphic AbstractBound to be active: The solution structure of tubulin-bound tubulysin A is determined from transferred NOE data (see picture; blue N, red O, yellow S, green C), and this bioactive conformation is compared to the unbound conformation. The binding site on tubulin is examined on the bas...
J. Antibiot. Sasse F. 53 2000
Khalil, Mohamed W., Sasse, Florenz, Lünsdorf, Heinrich, Elnakady, Yasser A., Reichenbach, Hans. Mechanism of Action of Tubulysin, an Antimitotic Peptide from Myxobacteria. Chembiochem : a European journal of chemical biology, vol.7, no.4, 678-683.
Steinmetz, Heinrich, Glaser, Nicole, Herdtweck, Eberhardt, Sasse, Florenz, Reichenbach, Hans, Höfle, Gerhard. Isolation, Crystal and Solution Structure Determination, and Biosynthesis of Tubulysins—Powerful Inhibitors of Tubulin Polymerization from Myxobacteria. Angewandte Chemie, vol.116, no.37, 4996-5000.
Steinmetz, Heinrich, Glaser, Nicole, Herdtweck, Eberhardt, Sasse, Florenz, Reichenbach, Hans, Höfle, Gerhard. Isolation, Crystal and Solution Structure Determination, and Biosynthesis of Tubulysins—Powerful Inhibitors of Tubulin Polymerization from Myxobacteria. Angewandte Chemie. international edition, vol.43, no.37, 4888-4892.
Ravelli, Raimond B.G., Gigant, Benoît, Curmi, Patrick A., Jourdain, Isabelle, Lachkar, Sylvie, Sobel, André, Knossow, Marcel. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature, vol.428, no.6979, 198-202.
Gigant, Benoît, Wang, Chunguang, Ravelli, Raimond B. G., Roussi, Fanny, Steinmetz, Michel O., Curmi, Patrick A., Sobel, André, Knossow, Marcel. Structural basis for the regulation of tubulin by vinblastine. Nature, vol.435, no.7041, 519-522.
Bai, R L, Pettit, G R, Hamel, E. Binding of dolastatin 10 to tubulin at a distinct site for peptide antimitotic agents near the exchangeable nucleotide and vinca alkaloid sites.. The Journal of biological chemistry, vol.265, no.28, 17141-17149.
Bai, Ruoli, Roach, Mary Carmen, Jayaram, Srirangam K., Barkoczy, Jozef, Pettit, George R., Luduen̄a, Richard F., Hamel, Ernest. Differential effects of active isomers, segments, and analogs of dolastatin 10 on ligand interactions with tubulin. Biochemical pharmacology, vol.45, no.7, 1503-1515.
Bai, R., Durso, N. A., Sackett, D. L., Hamel, E.. Interactions of the Sponge-Derived Antimitotic Tripeptide Hemiasterlin with Tubulin: Comparison with Dolastatin 10 and Cryptophycin 1. Biochemistry, vol.38, no.43, 14302-14310.
Nogales, Eva, Wolf, Sharon G., Downing, Kenneth H.. Erratum: Structure of the αβ tubulin dimer by electron crystallography. Nature, vol.393, no.6681, 191-191.
Nettles, James H., Li, Huilin, Cornett, Ben, Krahn, Joseph M., Snyder, James P., Downing, Kenneth H.. The Binding Mode of Epothilone A on &agr;,&bgr;-Tubulin by Electron Crystallography. Science, vol.305, no.5685, 866-869.
Carlomagno, Teresa, Sánchez, Víctor M., Blommers, Marcel J. J., Griesinger, Christian. Derivation of Dihedral Angles from CH–CH Dipolar–Dipolar Cross-Correlated Relaxation Rates: A C–C Torsion Involving a Quaternary Carbon Atom in Epothilone A Bound to Tubulin. Angewandte Chemie, vol.115, no.22, 2619-2621.
Carlomagno, Teresa, Sánchez, Víctor M., Blommers, Marcel J. J., Griesinger, Christian. Derivation of Dihedral Angles from CH–CH Dipolar–Dipolar Cross-Correlated Relaxation Rates: A C–C Torsion Involving a Quaternary Carbon Atom in Epothilone A Bound to Tubulin. Angewandte Chemie. international edition, vol.42, no.22, 2515-2517.
Wang, Zhiyong, McPherson, Peter A., Raccor, Brianne S., Balachandran, Raghavan, Zhu, Guangyu, Day, Billy W., Vogt, Andreas, Wipf, Peter. Structure–activity and High-content Imaging Analyses of Novel Tubulysins. Chemical biology & drug design, vol.70, no.2, 75-86.
Patterson, Andrew W., Peltier, Hillary M., Sasse, Florenz, Ellman, Jonathan A.. Design, Synthesis, and Biological Properties of Highly Potent Tubulysin D Analogues. Chemistry : a European journal, vol.13, no.34, 9534-9541.
Sánchez-Pedregal, Víctor M., Reese, Marcel, Meiler, Jens, Blommers, Marcel J. J., Griesinger, Christian, Carlomagno, Teresa. The INPHARMA Method: Protein-Mediated Interligand NOEs for Pharmacophore Mapping. Angewandte Chemie, vol.117, no.27, 4244-4247.
Sánchez-Pedregal, Víctor M., Reese, Marcel, Meiler, Jens, Blommers, Marcel J. J., Griesinger, Christian, Carlomagno, Teresa. The INPHARMA Method: Protein-Mediated Interligand NOEs for Pharmacophore Mapping. Angewandte Chemie. international edition, vol.44, no.27, 4172-4175.
Reese, Marcel, Sánchez-Pedregal, Víctor M., Kubicek, Karel, Meiler, Jens, Blommers, Marcel J. J., Griesinger, Christian, Carlomagno, Teresa. Structural Basis of the Activity of the Microtubule-Stabilizing Agent Epothilone A Studied by NMR Spectroscopy in Solution. Angewandte Chemie, vol.119, no.11, 1896-1900.
Reese, Marcel, Sánchez-Pedregal, Víctor M., Kubicek, Karel, Meiler, Jens, Blommers, Marcel J. J., Griesinger, Christian, Carlomagno, Teresa. Structural Basis of the Activity of the Microtubule-Stabilizing Agent Epothilone A Studied by NMR Spectroscopy in Solution. Angewandte Chemie. international edition, vol.46, no.11, 1864-1868.
Buey, Rubén M, Calvo, Enrique, Barasoain, Isabel, Pineda, Oriol, Edler, Michael C, Matesanz, Ruth, Cerezo, Gemma, Vanderwal, Christopher D, Day, Billy W, Sorensen, Erik J, López, Juan Antonio, Andreu, José Manuel, Hamel, Ernest, Díaz, J Fernando. Cyclostreptin binds covalently to microtubule pores and lumenal taxoid binding sites. Nature chemical biology, vol.3, no.2, 117-125.
Díaz, José Fernando, Barasoain, Isabel, Souto, André A., Amat-Guerri, Francisco, Andreu, José Manuel. Macromolecular Accessibility of Fluorescent Taxoids Bound at a Paclitaxel Binding Site in the Microtubule Surface. The Journal of biological chemistry, vol.280, no.5, 3928-3937.
Cormier, Anthony, Marchand, Matthieu, Ravelli, Raimond B G, Knossow, Marcel, Gigant, Benoît. Structural insight into the inhibition of tubulin by vinca domain peptide ligands. EMBO reports, vol.9, no.11, 1101-1106.
Sánchez-Pedregal, Víctor M., Kubicek, Karel, Meiler, Jens, Lyothier, Isabelle, Paterson, Ian, Carlomagno, Teresa. The Tubulin-Bound Conformation of Discodermolide Derived by NMR Studies in Solution Supports a Common Pharmacophore Model for Epothilone and Discodermolide. Angewandte Chemie, vol.118, no.44, 7548-7554.
Sánchez-Pedregal, Víctor M., Kubicek, Karel, Meiler, Jens, Lyothier, Isabelle, Paterson, Ian, Carlomagno, Teresa. The Tubulin-Bound Conformation of Discodermolide Derived by NMR Studies in Solution Supports a Common Pharmacophore Model for Epothilone and Discodermolide. Angewandte Chemie. international edition, vol.45, no.44, 7388-7394.
Delaglio, Frank, Grzesiek, Stephan, Vuister, GeertenW., Zhu, Guang, Pfeifer, John, Bax, Ad. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. Journal of biomolecular NMR, vol.6, no.3,
Schwieters, Charles D, Kuszewski, John J, Tjandra, Nico, Marius Clore, G. The Xplor-NIH NMR molecular structure determination package. Journal of magnetic resonance, vol.160, no.1, 65-73.
해당 논문의 주제분야에서 활용도가 높은 상위 5개 콘텐츠를 보여줍니다.
더보기 버튼을 클릭하시면 더 많은 관련자료를 살펴볼 수 있습니다.
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
Copyright KISTI. All Rights Reserved.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.