Pubblicazioni Peer reviewed articles (15) FRET-based dynamic structural biology: Challenges, perspectives and an appeal for open-science practices Autori: Eitan Lerner, Anders Barth, Jelle Hendrix, Benjamin Ambrose, Victoria Birkedal, Scott C Blanchard, Richard Börner, Hoi Sung Chung, Thorben Cordes, Timothy D Craggs, Ashok A Deniz, Jiajie Diao, Jingyi Fei, Ruben L Gonzalez, Irina V Gopich, Taekjip Ha, Christian A Hanke, Gilad Haran, Nikos S Hatzakis, Sungchul Hohng, Seok-Cheol Hong, Thorsten Hugel, Antonino Ingargiola, Chirlmin Joo, Achillefs N Ka Pubblicato in: eLife, Issue 10, 2021, ISSN 2050-084X Editore: eLife Sciences Publications DOI: 10.7554/elife.60416 Synthesis and Evaluation of Novel Ring‐Strained Noncanonical Amino Acids for Residue‐Specific Bioorthogonal Reactions in Living Cells Autori: Christopher D. Reinkemeier, Christine Koehler, Paul F. Sauter, Nataliia V. Shymanska, Cecile Echalier, Anna Rutkowska, David W. Will, Carsten Schultz, Edward A. Lemke Pubblicato in: Chemistry – A European Journal, Issue 27/19, 2021, Page(s) 6094-6099, ISSN 0947-6539 Editore: John Wiley & Sons Ltd. DOI: 10.1002/chem.202100322 Multifunctionality of F-rich nucleoporins Autori: Nike Heinß, Mikhail Sushkin, Miao Yu, Edward A. Lemke Pubblicato in: Biochemical Society Transactions, Issue 48/6, 2020, Page(s) 2603-2614, ISSN 0300-5127 Editore: Portland Press, Ltd. DOI: 10.1042/bst20200357 Floppy but not sloppy: Interaction mechanism of FG-nucleoporins and nuclear transport receptors Autori: Iker Valle Aramburu, Edward A. Lemke Pubblicato in: Seminars in Cell & Developmental Biology, Issue 68, 2017, Page(s) 34-41, ISSN 1084-9521 Editore: Academic Press DOI: 10.1016/j.semcdb.2017.06.026 Beyond the Transport Function of Import Receptors: What’s All the FUS about? Autori: Sofya Mikhaleva, Edward A. Lemke Pubblicato in: Cell, Issue 173/3, 2018, Page(s) 549-553, ISSN 0092-8674 Editore: Cell Press DOI: 10.1016/j.cell.2018.04.002 Two Differential Binding Mechanisms of FG-Nucleoporins and Nuclear Transport Receptors Autori: Piau Siong Tan, Iker Valle Aramburu, Davide Mercadante, Swati Tyagi, Aritra Chowdhury, Daniel Spitz, Sarah L. Shammas, Frauke Gräter, Edward A. Lemke Pubblicato in: Cell Reports, Issue 22/13, 2018, Page(s) 3660-3671, ISSN 2211-1247 Editore: Cell Press DOI: 10.1016/j.celrep.2018.03.022 Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study Autori: Björn Hellenkamp, Sonja Schmid, Olga Doroshenko, Oleg Opanasyuk, Ralf Kühnemuth, Soheila Rezaei Adariani, Benjamin Ambrose, Mikayel Aznauryan, Anders Barth, Victoria Birkedal, Mark E. Bowen, Hongtao Chen, Thorben Cordes, Tobias Eilert, Carel Fijen, Christian Gebhardt, Markus Götz, Giorgos Gouridis, Enrico Gratton, Taekjip Ha, Pengyu Hao, Christian A. Hanke, Andreas Hartmann, Jelle Hendrix, Lass Pubblicato in: Nature Methods, Issue 15/9, 2018, Page(s) 669-676, ISSN 1548-7091 Editore: Nature Publishing Group DOI: 10.1038/s41592-018-0085-0 Mechanism-Dependent Modulation of Ultrafast Interfacial Water Dynamics in Intrinsically Disordered Protein Complexes Autori: Aritra Chowdhury, Sergey A. Kovalenko, Iker Valle Aramburu, Piau Siong Tan, Nikolaus P. Ernsting, Edward A. Lemke Pubblicato in: Angewandte Chemie International Edition, Issue 58/14, 2019, Page(s) 4720-4724, ISSN 1433-7851 Editore: John Wiley & Sons Ltd. DOI: 10.1002/anie.201813354 Designer membraneless organelles enable codon reassignment of selected mRNAs in eukaryotes Autori: Christopher D. Reinkemeier, Gemma Estrada Girona, Edward A. Lemke Pubblicato in: Science, Issue 363/6434, 2019, Page(s) eaaw2644, ISSN 0036-8075 Editore: American Association for the Advancement of Science DOI: 10.1126/science.aaw2644 Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water” Autori: Gustavo Fuertes, Niccolo Banterle, Kiersten M. Ruff, Aritra Chowdhury, Rohit V. Pappu, Dmitri I. Svergun, Edward A. Lemke Pubblicato in: Science, Issue 361/6405, 2018, Page(s) eaau8230, ISSN 0036-8075 Editore: American Association for the Advancement of Science DOI: 10.1126/science.aau8230 Debugging Eukaryotic Genetic Code Expansion for Site-Specific Click-PAINT Super-Resolution Microscopy Autori: Ivana Nikić, Gemma Estrada Girona, Jun Hee Kang, Giulia Paci, Sofya Mikhaleva, Christine Koehler, Nataliia V. Shymanska, Camilla Ventura Santos, Daniel Spitz, Edward A. Lemke Pubblicato in: Angewandte Chemie International Edition, Issue 55/52, 2016, Page(s) 16172-16176, ISSN 1433-7851 Editore: John Wiley & Sons Ltd. DOI: 10.1002/anie.201608284 Nanoscale devices for linkerless long-term single-molecule observation Autori: Niccolò Banterle, Edward A Lemke Pubblicato in: Current Opinion in Biotechnology, Issue 39, 2016, Page(s) 105-112, ISSN 0958-1669 Editore: Elsevier BV DOI: 10.1016/j.copbio.2016.02.013 The Multiple Faces of Disordered Nucleoporins Autori: Edward A. Lemke Pubblicato in: Journal of Molecular Biology, Issue 428/10, 2016, Page(s) 2011-2024, ISSN 0022-2836 Editore: Academic Press DOI: 10.1016/j.jmb.2016.01.002 The liquid state of FG-nucleoporins mimics permeability barrier properties of nuclear pore complexes Autori: Giorgia Celetti, Giulia Paci, Joana Caria, Virginia VanDelinder, George Bachand, Edward A. Lemke Pubblicato in: The Journal of Cell Biology, Issue 219/1, 2020, ISSN 0021-9525 Editore: Rockefeller University Press DOI: 10.1083/jcb.201907157 Inducible Genetic Code Expansion in Eukaryotes Autori: Christine Koehler, Gemma Estrada Girona, Christopher D. Reinkemeier, Edward A. Lemke Pubblicato in: ChemBioChem, Issue 21/22, 2020, Page(s) 3216-3219, ISSN 1439-4227 Editore: John Wiley & Sons Ltd. DOI: 10.1002/cbic.202000338 Book chapters (1) Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRET Autori: Piau Siong Tan, Edward A. Lemke Pubblicato in: Intrinsically Disordered Proteins, Issue 611, 2018, Page(s) 327-346, ISBN 9780-128156490 Editore: Elsevier DOI: 10.1016/bs.mie.2018.08.034 È in corso la ricerca di dati su OpenAIRE... Si è verificato un errore durante la ricerca dei dati su OpenAIRE Nessun risultato disponibile
