| Year |
Citation |
Score |
| 2021 |
Radford SE, Karamanos TK. Finding the sweet spot for chaperone activity. Nature Chemistry. 13: 397-399. PMID 33931750 DOI: 10.1038/s41557-021-00691-5 |
0.381 |
|
| 2020 |
Cawood EE, Guthertz N, Ebo JS, Karamanos TK, Radford SE, Wilson AJ. Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules. Journal of the American Chemical Society. PMID 33253560 DOI: 10.1021/jacs.0c10629 |
0.638 |
|
| 2020 |
Cawood EE, Karamanos TK, Wilson AJ, Radford SE. Visualizing and trapping transient oligomers in amyloid assembly pathways. Biophysical Chemistry. 268: 106505. PMID 33220582 DOI: 10.1016/j.bpc.2020.106505 |
0.602 |
|
| 2020 |
Karamanos TK, Tugarinov V, Clore GM. 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. PMID 33199640 DOI: 10.1073/pnas.2020306117 |
0.431 |
|
| 2020 |
Calabrese AN, Schiffrin B, Watson M, Karamanos TK, Walko M, Humes JR, Horne JE, White P, Wilson AJ, Kalli AC, Tuma R, Ashcroft AE, Brockwell DJ, Radford SE. Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients. Nature Communications. 11: 2155. PMID 32358557 DOI: 10.1038/S41467-020-15702-1 |
0.585 |
|
| 2019 |
Karamanos TK, Tugarinov V, Clore GM. 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. PMID 31591220 DOI: 10.1073/pnas.1914999116 |
0.409 |
|
| 2019 |
Karamanos TK, Jackson MP, Calabrese AN, Goodchild SC, Cawood EE, Thompson GS, Kalverda AP, Hewitt EW, Radford SE. Structural mapping of oligomeric intermediates in an amyloid assembly pathway. Elife. 8. PMID 31552823 DOI: 10.7554/eLife.46574 |
0.627 |
|
| 2019 |
Benseny-Cases N, Karamanos TK, Hoop CL, Baum J, Radford SE. Extracellular matrix components modulate different stages in β2-microglobulin amyloid formation. The Journal of Biological Chemistry. PMID 30996004 DOI: 10.1074/Jbc.Ra119.008300 |
0.606 |
|
| 2018 |
Iadanza MG, Silvers R, Boardman J, Smith HI, Karamanos TK, Debelouchina GT, Su Y, Griffin RG, Ranson NA, Radford SE. The structure of a β-microglobulin fibril suggests a molecular basis for its amyloid polymorphism. Nature Communications. 9: 4517. PMID 30375379 DOI: 10.1038/s41467-018-06761-6 |
0.648 |
|
| 2018 |
Doherty CPA, Young LM, Karamanos TK, Smith HI, Jackson MP, Radford SE, Brockwell DJ. A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides. Protein Science : a Publication of the Protein Society. PMID 29417650 DOI: 10.1002/pro.3386 |
0.665 |
|
| 2018 |
Knight PD, Karamanos TK, Radford SE, Ashcroft AE. Identification of a novel site of interaction between ataxin-3 and the amyloid aggregation inhibitor polyglutamine binding peptide 1. European Journal of Mass Spectrometry (Chichester, England). 24: 129-140. PMID 29334808 DOI: 10.1177/1469066717729298 |
0.603 |
|
| 2018 |
Iadanza MG, Silvers R, Boardman J, Smith HI, Karamanos TK, Debelouchina GT, Su Y, Griffin RG, Ranson NA, Radford SE. The structure of a beta2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism. Nature Communications. 9: 4517-4517. DOI: 10.2210/Pdb6Gk3/Pdb |
0.646 |
|
| 2016 |
Dobson CL, Devine PW, Phillips JJ, Higazi DR, Lloyd C, Popovic B, Arnold J, Buchanan A, Lewis A, Goodman J, van der Walle CF, Thornton P, Vinall L, Lowne D, Aagaard A, ... ... Karamanos TK, et al. Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo. Scientific Reports. 6: 38644. PMID 27995962 DOI: 10.1038/Srep38644 |
0.464 |
|
| 2016 |
Karamanos TK, Pashley CL, Kalverda AP, Thompson GS, Mayzel M, Orekhov VY, Radford SE. A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity. Journal of the American Chemical Society. PMID 27117876 DOI: 10.1021/jacs.6b02464 |
0.599 |
|
| 2015 |
Karamanos TK, Kalverda AP, Thompson GS, Radford SE. Mechanisms of amyloid formation revealed by solution NMR. Progress in Nuclear Magnetic Resonance Spectroscopy. 88: 86-104. PMID 26282197 DOI: 10.1016/j.pnmrs.2015.05.002 |
0.622 |
|
| 2015 |
Tipping KW, Karamanos TK, Jakhria T, Iadanza MG, Goodchild SC, Tuma R, Ranson NA, Hewitt EW, Radford SE. pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers. Proceedings of the National Academy of Sciences of the United States of America. 112: 5691-6. PMID 25902516 DOI: 10.1073/Pnas.1423174112 |
0.575 |
|
| 2014 |
Louros NN, Petronikolou N, Karamanos T, Cordopatis P, Iconomidou VA, Hamodrakas SJ. Structural studies of "aggregation-prone" peptide-analogues of teleostean egg chorion ZPB proteins. Biopolymers. 102: 427-36. PMID 25229478 DOI: 10.1002/bip.22563 |
0.384 |
|
| 2014 |
Sarell CJ, Karamanos TK, White SJ, Bunka DH, Kalverda AP, Thompson GS, Barker AM, Stockley PG, Radford SE. Distinguishing closely related amyloid precursors using an RNA aptamer. The Journal of Biological Chemistry. 289: 26859-71. PMID 25100729 DOI: 10.1074/jbc.M114.595066 |
0.59 |
|
| 2014 |
Karamanos TK, Kalverda AP, Thompson GS, Radford SE. Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly. Molecular Cell. 55: 214-26. PMID 24981172 DOI: 10.1016/j.molcel.2014.05.026 |
0.617 |
|
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