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Proceedings of the National Academy of Sciences of the United States of America|May 29, 2024
Atomic resolution structure of full-length human insulin fibrilsSaba Suladze, Riddhiman Sarkar, Natalia Rodina, et al.Angewandte Chemie (International Ed. in English)|July 11, 2018
Overcoming Volume Selectivity of Dipolar Recoupling in Biological Solid-State NMR SpectroscopyZdeněk Tošner, Riddhiman Sarkar, Johanna Becker-Baldus, et al.Scientific Reports|January 28, 2017
Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chainsManuel Hora, Martin Carballo-Pacheco, Benedikt Weber, et al.Journal of Molecular Biology|February 4, 2012
Structural properties of EGCG-induced, nontoxic Alzheimer's disease Aβ oligomersJuan Miguel Lopez del Amo, Uwe Fink, Muralidhar Dasari, et al.Journal of Molecular Biology|June 17, 2009
Dimer formation of a stabilized Gbeta1 variant: a structural and energetic analysisStephanie Thoms, Klaas E A Max, Michael Wunderlich, et al.Journal of the American Chemical Society|September 21, 2006
Protein side-chain dynamics observed by solution- and solid-state NMR: comparative analysis of methyl 2H relaxation dataBernd Reif, Yi Xue, Vipin Agarwal, et al.Journal of the American Chemical Society|May 9, 2024
Structural Insights into Seeding Mechanisms of hIAPP Fibril FormationSaba Suladze, Christian Sustay Martinez, Diana C Rodriguez Camargo, et al.Journal of Structural Biology: X|August 4, 2022
SAA fibrils involved in AA amyloidosis are similar in bulk and by single particle reconstitution: A MAS solid-state NMR studyArpita Sundaria, Falk Liberta, Dilan Savran, et al.Nature Communications|February 18, 2018
Physical basis of amyloid fibril polymorphismWilliam Close, Matthias Neumann, Andreas Schmidt, et al.Nature Communications|November 19, 2021
Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensembleMoritz Mühlhofer, Carsten Peters, Thomas Kriehuber, et al.Pageof 15