Publications
2025
37. B. Hobbs, N. Limmer, G. Clenshaw, F. Ossa, and Theodoros K. Karamanos. Accurate conformational ensembles of mixed folded proteins from NMR-guided simulations. biorxiv preprint biorchiv 10.1101/2025.11.21.689726
36. Grimaldi, A., Stofella, M., Hobbs, B., Karamanos, T. K., & Paci, E. (2025). Amide Hydrogen Deuterium Exchange in Isotopically Mixed Waters. arXiv preprint arXiv:2510.24860.
35. B. Hobbs, N. Limmer, F. Ossa, E. Knüpling, S. Lenton, V. Foderà, A. P. Kalverda, and Theodoros K. Karamanos. A low-complexity linker as a driver of intra-and intermolecular interactions in DNAJB chaperones. Nature Communications 16, no. 1 (2025): 5070
2024
34. E Cawood, E Baker, T Edwards, D Woolfson*, T Karamanos*, A Wilson*. Understanding β-strand mediated protein–protein interactions: tuning binding behaviour of intrinsically disordered sequences by backbone modification. Chemical Science, 15, 10237-10245
33. BJ Lane, Y Ma, N Yan, B Wang, K Ackermann, TK Karamanos, BE Bode, Christos Pliotas
Monitoring the Conformational Ensemble and Lipid Environment of a Mechanosensitive Channel Under Cyclodextrin-Induced Membrane Tension. Structure, 32, 6, 739-750
32. TK Karamanos*, S Matthews*. Biomolecular NMR in the AI-assisted structural biology era: Old tricks and new opportunities. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 140949
31. E Cawood, E Baker, T Edwards, D Woolfson*, T Karamanos*, A Wilson*. Peptidomimetic inhibitors of β-strand mediated protein-protein interactions: tuning binding affinity of intrinsically disordered sequences by covalent backbone modification. Chemrxiv
30. TK Karamanos*. Chasing long‐range evolutionary couplings in the AlphaFold era.
Biopolymers 114 (3), e23530 (on the cover)
2023
29. EE Cawood, GM Clore, TK Karamanos* Microsecond backbone motions modulate the oligomerization of the Dnajb6 chaperone. . Angewandte Chemie 134 (20), e202116403
28. R Maya-Martinez, Y Xu, N Guthertz, M Walko, TK Karamanos, F Sobott, et al., Dimers of D76N-β2-microglobulin display potent antiamyloid aggregation activity. Journal of Biological Chemistry 298 (12)
27. V Tugarinov, Y Okuno, F Torricella, TK Karamanos, GM Clore. A “Steady-State” Relaxation Dispersion Nuclear Magnetic Resonance Experiment for Studies of Chemical Exchange in Degenerate 1H Transitions of Methyl Groups. The Journal of Physical Chemistry Letters 13, 11271-11279
26. B Schiffrin, JM Machin, TK Karamanos, A Zhuravleva, DJ Brockwell, et al. Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding. Communications Biology 5 (1), 560
25. TK Karamanos*, GM Clore*. Large chaperone complexes through the lens of nuclear magnetic resonance spectroscopy. Annual review of biophysics 51, 223-246
24. TK Karamanos*, AP Kalverda, SE Radford*. Generating ensembles of dynamic misfolding proteins.
Frontiers in Neuroscience 16, 881534
2022
23. SE Radford*, TK Karamanos*. Finding the sweet spot for chaperone activity Nature Chemistry 13 (5), 397-399
22. EE Cawood, T.K Karamanos, AJ Wilson, SE Radford. Visualising and trapping transient oligomers in
amyloid assembly pathways. Biophysical Chemistry 268, 106505 (2021) (on the cover)
2021
21. E Cawood, N Guthertz, J Ebo, T Karamanos, SE Radford FRS, A Wilson. Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules. J. Am. Chem. Soc 142 (49), 20845-20854
20. A. N. Calabrese, B.Schiffrin, M.A Watson, T. K. Karamanos, M. Walko, J.R Humes, J. E Horne, P. White, A.J Wilson, A.C Kalli, R. Tuma, A.E Ashcroft, D.J Brockwell, S.E Radford. Inter-domain dynamics in the chaperone SurA and multi-site binding to its unfolded outer membrane protein clients. Nat. Comms, 11(1), 1-16 (2020)
19. V Tugarinov, TK Karamanos, GM Clore. Optimized selection of slow-relaxing 13C transitions in methyl groups of proteins: application to relaxation dispersion. Journal of Biomolecular NMR, 1-8 (2020)
18. V. Tugarinov, TK Karamanos, GM Clore. Magic-Angle-Pulse Driven Separation of Degenerate 1H Transitions in Methyl Groups of Proteins: Application to Studies of Methyl Axis Dynamics. ChemPhysChem 21, 1-6 (2020)
17. T.K Karamanos, V. Tugarinov, G.M Clore. Determining Methyl Side-Chain Conformations in a CS-Rosetta Model Using Methyl 1H-13C Residual Dipolar Couplings. J. Biomol. NMR, 74(2), 111-118, (2020)
16. V. Tugarinov, T.K Karamanos, A.Ceccon, G.M Clore. Optimized NMR Experiments for the Isolation of I=1/2 Manifold Transitions in Methyl Groups of Proteins. ChemPhysChem, 21, 23 (2020)
15. T.K Karamanos, V. Tugarinov, G.M Clore. An S/T motif controls reversible oligomerization of the Hsp40 chaperone DNAJB6b, through subtle reorganization of a β-sheet backbone. PNAS 117 (48), 30441-30450
2020
14. N Benseny-Cases, T.K Karamanos, C.L Hoop, J. Baum, S.E Radford. Extracellular Matrix Components Modulate Different Stages in β2-microglobulin amyloid formation J. Biol. Chem, 294 (24), 9392-9401, (2019)
13. T.K Karamanos, M.P. Jackson, G.S Thompson, A.N Calabrese, E.E Cawood, E.W Hewitt, A.P Kalverda, S. E. Radford. Structural Mapping of Oligomeric Intermediates in an Amyloid Assembly Pathway Elife, 8, e46574, (2019)
12. T.K Karamanos, V. Tugarinov, G.M Clore. Unravelling the Structure and Dynamics of the Human DNAJB6b Chaperone Reveals Insights into Hsp40 Mediated Proteostasis. Proc. Nat. Acad. Sci. 116 (43), 21529-21538, (2019)
2019
11. M.G. Iadanza, R. Silvers, J. Boardman, H.I. Smith, T.K. Karamanos, G. Debelouchina, Y. Su, R.G. Griffin, N.A. Ranson and S.E. Radford. The structure of a β2-microglobulin fibril suggests a molecular basis for amyloid polymorphism. Nature Coms, 9 (1), 4517, (2018)
10. E.M Martin, M.P Jackson, M. Gamerdinger, K. Gense, T.K Karamanos, J.R Humes, E. Deuerling, A.E Ashcroft, S.E Radford. Conformational flexibility within the nascent polypeptide–associated complex enables its interactions with structurally diverse client proteins. J. Biol. Chem., 293 (22), 8554-8568, (2018)
9. C.P.A Doherty, L.M Young, T.K Karamanos, H.I Smith, M.P Jackson, S.E Radford, D.J Brockwell. A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides. Protein Sci, 27 (7), 1205-1217, (2018)
8. P. Knight, T.K. Karamanos, S.E. Radford, A.E. Ashcroft. Identification of a novel site of interaction between ataxin-3 and the amyloid aggregation inhibitor polyglutamine binding protein 1. Europ. J. Mass Spec, 24(1), 129-140, (2018)
2018
7. T.K Karamanos, C.Pashley, A.P Kalverda, G.S Thompson, M. Mayzel, V. Orekhov, S.E Radford. A population shift between sparsely populated folding intermediates determines amyloigenicity. JACS 138 (19), 6271-6280 (2016)
6. Dobson et al., . Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo. Sci. Rep. 6, 38644 (2016)
2016
5. T.K Karamanos*, A.P Kalverda, G.S Thompson, S.E Radford*. Mechanisms of amyloid formation revealed by solution NMR. Progr. Nucl. Magn. Res. Spec. 88-89, 86-104 (2015)
*Corresponding authors
4. W.K Tipping, T.K Karamanos , T. Jakhria, G.M Iadanza, G.S Goodchild, R. Tuma, N.A Ranson, E.R Hewitt, S.E Radford. pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers. PNAS 112, 5691-5696 (2015)
2015
3. T.K Karamanos, A.P Kalverda, G.S Thompson, S.E Radford. Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly. Mol. Cell 55, 214-226 (2014)
Highlighted as exceptional in F1000, featured in two press releases
2. N.N Louros, N.Petronikolou, T.K Karamanos, P. Cordopatis, V.A Iconomidou, S.J Hamodrakas. Structural studies of 'aggregation-prone' peptide analogues of teleostean egg chorion ZPB proteins. Biopolymers 102, 427-436 (2014)
1. C.J Sarell, T.K Karamanos, S.J White, D.J Bunka, A.P Kalverda, G.S Thompson, A.M Barker, P.G Stockley, S.E Radford. Distinguishing closely-related amyloid precursors using an RNA aptamer. J. Biol. Chem. 289, 26859-26871 (2014)