Browse by Basel Contributors ID
2022Kolloff, Christopher and Mazur, Adam and Marzinek, Jan K. and Bond, Peter J. and Olsson, Simon and Hiller, Sebastian. (2022) Motional clustering in supra-τ; c; conformational exchange influences NOE cross-relaxation rate. Journal of Magnetic Resonance, 338. p. 107196. 2021Gray, Declan A. and White, Joshua B. R. and Oluwole, Abraham O. and Rath, Parthasarathi and Glenwright, Amy J. and Mazur, Adam and Zahn, Michael and Baslé, Arnaud and Morland, Carl and Evans, Sasha L. and Cartmell, Alan and Robinson, Carol V. and Hiller, Sebastian and Ranson, Neil A. and Bolam, David N. and van den Berg, Bert. (2021) Insights into SusCD-mediated glycan import by a prominent gut symbiont. Nature Communications, 12 (1). p. 44. 2020Burmann, Björn M. and Gerez, Juan A. and Matečko-Burmann, Irena and Campioni, Silvia and Kumari, Pratibha and Ghosh, Dhiman and Mazur, Adam and Aspholm, Emelie E. and Šulskis, Darius and Wawrzyniuk, Magdalena and Bock, Thomas and Schmidt, Alexander and Rüdiger, Stefan G. D. and Riek, Roland and Hiller, Sebastian. (2020) Regulation of α-synuclein by chaperones in mammalian cells. Nature, 577. pp. 127-132. 2019Mazur, Adam and Broz, Petr and Hiller, Sebastian. (2019) An integrative protocol for the structure determination of the mouse ASC-PYD filament. In: Methods in Enzymology, 625. New York, pp. 205-222. 2017Benning, Friederike M. C. and Sakiyama, Yusuke and Mazur, Adam and Bukhari, Habib S. T. and Lim, Roderick Y. H. and Maier, Timm. (2017) High-Speed Atomic Force Microscopy Visualization of the Dynamics of the Multienzyme Fatty Acid Synthase. ACS Nano, 11 (11). pp. 10852-10859. Morgado, Leonor and Burmann, Björn M. and Sharpe, Timothy and Mazur, Adam and Hiller, Sebastian. (2017) The dynamic dimer structure of the chaperone Trigger Factor. Nature Communications, 8. p. 1992. 2016Leung, Hoi Tik Alvin and Bignucolo, Olivier and Aregger, Regula and Dames, Sonja A. and Mazur, Adam and Bernèche, Simon and Grzesiek, Stephan. (2016) A Rigorous and Efficient Method To Reweight Very Large Conformational Ensembles Using Average Experimental Data and To Determine Their Relative Information Content. Journal of chemical theory and computation, 12 (1). pp. 383-394. Reinders, Alberto and Hee, Chee-Seng and Ozaki, Shogo and Mazur, Adam and Boehm, Alex and Schirmer, Tilman and Jenal, Urs. (2016) Expression and Genetic Activation of Cyclic Di-GMP-Specific Phosphodiesterases in Escherichia coli. Journal of Bacteriology, 198 (3). pp. 448-462. Stanger, Frédéric V. and Burmann, Björn M. and Harms, Alexander and Aragão, Hugo and Mazur, Adam and Sharpe, Timothy and Dehio, Christoph and Hiller, Sebastian and Schirmer, Tilman. (2016) Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification. Proceedings of the National Academy of Sciences of the United States of America, 113 (5). E529-E537. Sakiyama, Yusuke and Mazur, Adam and Kapinos, Larisa E. and Lim, Roderick Y. H.. (2016) Spatiotemporal dynamics of the nuclear pore complex transport barrier resolved by high-speed atomic force microscopy. Nature Nanotechnology (11). pp. 719-723. Ravotti, Francesco and Sborgi, Lorenzo and Cadalbert, Riccardo and Huber, Matthias and Mazur, Adam and Broz, Petr and Hiller, Sebastian and Meier, Beat H. and Böckmann, Anja. (2016) Sequence-specific solid-state NMR assignments of the mouse ASC PYRIN domain in its filament form. Biomolecular NMR Assignments, 10 (1). pp. 107-115. He, Lichun and Sharpe, Timothy and Mazur, Adam and Hiller, Sebastian. (2016) A molecular mechanism of chaperone–client recognition. Science Advances, 2 (11). e1601625. 2015Sborgi, Lorenzo and Ravotti, Francesco and Dandey, Venkata Prasad and Dick, Mathias S. and Mazur, Adam and Reckel, Sina and Chami, Mohamed and Scherer, Sebastian and Huber, Matthias and Böckmann, Anja and Egelman, Edward H. and Stahlberg, Henning and Broz, Petr and Meier, Beat H. and Hiller, Sebastian. (2015) Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy. Proceedings of the National Academy of Sciences of the United States of America, 112 (43). pp. 13237-13242. |