Theo Karamanos
Affiliations: | 2009-2013 | University of Leeds, Leeds, England, United Kingdom |
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Radford SE, Karamanos TK. (2021) Finding the sweet spot for chaperone activity. Nature Chemistry. 13: 397-399 |
Cawood EE, Guthertz N, Ebo JS, et al. (2020) Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules. Journal of the American Chemical Society |
Cawood EE, Karamanos TK, Wilson AJ, et al. (2020) Visualizing and trapping transient oligomers in amyloid assembly pathways. Biophysical Chemistry. 268: 106505 |
Karamanos TK, Tugarinov V, Clore GM. (2020) An S/T motif controls reversible oligomerization of the Hsp40 chaperone DNAJB6b through subtle reorganization of a β sheet backbone. Proceedings of the National Academy of Sciences of the United States of America. 117: 30441-30450 |
Calabrese AN, Schiffrin B, Watson M, et al. (2020) Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients. Nature Communications. 11: 2155 |
Karamanos TK, Tugarinov V, Clore GM. (2019) Unraveling the structure and dynamics of the human DNAJB6b chaperone by NMR reveals insights into Hsp40-mediated proteostasis. Proceedings of the National Academy of Sciences of the United States of America. 116: 21529-21538 |
Karamanos TK, Jackson MP, Calabrese AN, et al. (2019) Structural mapping of oligomeric intermediates in an amyloid assembly pathway. Elife. 8 |
Benseny-Cases N, Karamanos TK, Hoop CL, et al. (2019) Extracellular matrix components modulate different stages in β2-microglobulin amyloid formation. The Journal of Biological Chemistry |
Iadanza MG, Silvers R, Boardman J, et al. (2018) The structure of a β-microglobulin fibril suggests a molecular basis for its amyloid polymorphism. Nature Communications. 9: 4517 |
Doherty CPA, Young LM, Karamanos TK, et al. (2018) A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides. Protein Science : a Publication of the Protein Society |