Zobrazeno 1 - 10
of 167
pro vyhledávání: '"Benjamin Schuler"'
Autor:
Mark F. Nüesch, Lisa Pietrek, Erik D. Holmstrom, Daniel Nettels, Valentin von Roten, Rafael Kronenberg-Tenga, Ohad Medalia, Gerhard Hummer, Benjamin Schuler
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-11 (2024)
Abstract The conformational dynamics of single-stranded nucleic acids are fundamental for nucleic acid folding and function. However, their elementary chain dynamics have been difficult to resolve experimentally. Here we employ a combination of singl
Externí odkaz:
https://doaj.org/article/57a99000c53543ce8ce1987da9fd0904
Autor:
Andrea Sottini, Alessandro Borgia, Madeleine B. Borgia, Katrine Bugge, Daniel Nettels, Aritra Chowdhury, Pétur O. Heidarsson, Franziska Zosel, Robert B. Best, Birthe B. Kragelund, Benjamin Schuler
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-2 (2023)
Externí odkaz:
https://doaj.org/article/5ea12d9ad73449e59a25cd48ca8dd0ce
Autor:
Lukas S. Stelzl, Lisa M. Pietrek, Andrea Holla, Javier Oroz, Mateusz Sikora, Jürgen Köfinger, Benjamin Schuler, Markus Zweckstetter, Gerhard Hummer
Publikováno v:
JACS Au, Vol 2, Iss 3, Pp 673-686 (2022)
Externí odkaz:
https://doaj.org/article/1ab0d99f678148b7bfcf7450f680de6d
Autor:
Fabian Dingfelder, Iuri Macocco, Stephan Benke, Daniel Nettels, Pietro Faccioli, Benjamin Schuler
Publikováno v:
JACS Au, Vol 1, Iss 8, Pp 1217-1230 (2021)
Externí odkaz:
https://doaj.org/article/20f874893af24ed49f2ac22b6aba0269
Autor:
Jakob C. Stüber, Christian P. Richter, Junel Sotolongo Bellón, Martin Schwill, Iwo König, Benjamin Schuler, Jacob Piehler, Andreas Plückthun
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
Stüber et. al. show that receptor tyrosine kinase signaling can be neutralized through intermolecular, biparatopic bipDARPin crosslinking that locks down the bipDARPin-HER2 complexes. This affects the spatiotemporal organization and dynamics of HER2
Externí odkaz:
https://doaj.org/article/47e73f2b585647239c63400329c551bf
Autor:
Andrea Sottini, Alessandro Borgia, Madeleine B. Borgia, Katrine Bugge, Daniel Nettels, Aritra Chowdhury, Pétur O. Heidarsson, Franziska Zosel, Robert B. Best, Birthe B. Kragelund, Benjamin Schuler
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Abstract Highly charged intrinsically disordered proteins can form complexes with very high affinity in which both binding partners fully retain their disorder and dynamics, exemplified by the positively charged linker histone H1.0 and its chaperone,
Externí odkaz:
https://doaj.org/article/64b405d60211411596d26e2756ae1e36
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
RNA chaperones, such as the hepatitic C virus (HCV) core protein, are proteins that aid in the folding of nucleic acids. Here authors use single‐molecule spectroscopy and simulation to show that the HCV core protein acts as a flexible macromolecula
Externí odkaz:
https://doaj.org/article/289f20cc4cd4465ab566f9409c9f7499
Autor:
Flurin Sturzenegger, Franziska Zosel, Erik D. Holmstrom, Karin J. Buholzer, Dmitrii E. Makarov, Daniel Nettels, Benjamin Schuler
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
How interactions between binding partners form or break is hidden in the transition paths from the encounter to the formation of a stable complex. Here authors use single‐molecule spectroscopy to measure the transition path times for the associatio
Externí odkaz:
https://doaj.org/article/fb0baaec43a44cbeac635378d9bb4a00
Autor:
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 Kapanidis, Harold D Kim, Ted Laurence, Nam Ki Lee, Tae-Hee Lee, Edward A Lemke, Emmanuel Margeat, Jens Michaelis, Xavier Michalet, Sua Myong, Daniel Nettels, Thomas-Otavio Peulen, Evelyn Ploetz, Yair Razvag, Nicole C Robb, Benjamin Schuler, Hamid Soleimaninejad, Chun Tang, Reza Vafabakhsh, Don C Lamb, Claus AM Seidel, Shimon Weiss
Publikováno v:
eLife, Vol 10 (2021)
Single-molecule FRET (smFRET) has become a mainstream technique for studying biomolecular structural dynamics. The rapid and wide adoption of smFRET experiments by an ever-increasing number of groups has generated significant progress in sample prepa
Externí odkaz:
https://doaj.org/article/acccb8f6f1f1430c8cef78416466d619
Autor:
Salvatore Assenza, Alberto Stefano Sassi, Ruth Kellner, Benjamin Schuler, Paolo De Los Rios, Alessandro Barducci
Publikováno v:
eLife, Vol 8 (2019)
Hsp70 molecular chaperones are abundant ATP-dependent nanomachines that actively reshape non-native, misfolded proteins and assist a wide variety of essential cellular processes. Here, we combine complementary theoretical approaches to elucidate the
Externí odkaz:
https://doaj.org/article/5916742e47564e3c8585dd71ebb8e6b0