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For: Falsig J, Nilsson KP, Knowles TP, Aguzzi A. Chemical and biophysical insights into the propagation of prion strains. HFSP J 2008;2:332-41. [PMID: 19436493 DOI: 10.2976/1.2990786] [Cited by in Crossref: 25] [Cited by in F6Publishing: 22] [Article Influence: 1.8] [Reference Citation Analysis]
Number Citing Articles
1 Dear AJ, Michaels TCT, Knowles TPJ, Mahadevan L. Feedback control of protein aggregation. J Chem Phys 2021;155:064102. [PMID: 34391352 DOI: 10.1063/5.0055925] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
2 Friesen M, Meyer-Luehmann M. Aβ Seeding as a Tool to Study Cerebral Amyloidosis and Associated Pathology. Front Mol Neurosci 2019;12:233. [PMID: 31632238 DOI: 10.3389/fnmol.2019.00233] [Cited by in Crossref: 9] [Cited by in F6Publishing: 15] [Article Influence: 3.0] [Reference Citation Analysis]
3 Hornemann S, Schwarz P, Rushing EJ, Connolly MD, Zuckermann RN, Yam AY, Aguzzi A. Enhanced detection of prion infectivity from blood by preanalytical enrichment with peptoid-conjugated beads. PLoS One 2019;14:e0216013. [PMID: 31513666 DOI: 10.1371/journal.pone.0216013] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 0.7] [Reference Citation Analysis]
4 Dear AJ, Šarić A, Michaels TCT, Dobson CM, Knowles TPJ. Statistical Mechanics of Globular Oligomer Formation by Protein Molecules. J Phys Chem B 2018;122:11721-30. [PMID: 30336667 DOI: 10.1021/acs.jpcb.8b07805] [Cited by in Crossref: 8] [Cited by in F6Publishing: 8] [Article Influence: 2.0] [Reference Citation Analysis]
5 Nizynski B, Nieznanska H, Dec R, Boyko S, Dzwolak W, Nieznanski K. Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils. PLoS One 2018;13:e0201182. [PMID: 30024984 DOI: 10.1371/journal.pone.0201182] [Cited by in Crossref: 18] [Cited by in F6Publishing: 17] [Article Influence: 4.5] [Reference Citation Analysis]
6 Löffler S, Melican K, Nilsson KPR, Richter-Dahlfors A. Organic bioelectronics in medicine. J Intern Med 2017;282:24-36. [PMID: 28181720 DOI: 10.1111/joim.12595] [Cited by in Crossref: 23] [Cited by in F6Publishing: 20] [Article Influence: 4.6] [Reference Citation Analysis]
7 Surmacz-Chwedoruk W, Babenko V, Dec R, Szymczak P, Dzwolak W. The emergence of superstructural order in insulin amyloid fibrils upon multiple rounds of self-seeding. Sci Rep 2016;6:32022. [PMID: 27558445 DOI: 10.1038/srep32022] [Cited by in Crossref: 11] [Cited by in F6Publishing: 12] [Article Influence: 1.8] [Reference Citation Analysis]
8 Munoz-Montesino C, Sizun C, Moudjou M, Herzog L, Reine F, Chapuis J, Ciric D, Igel-Egalon A, Laude H, Béringue V, Rezaei H, Dron M. Generating Bona Fide Mammalian Prions with Internal Deletions. J Virol 2016;90:6963-75. [PMID: 27226369 DOI: 10.1128/JVI.00555-16] [Cited by in Crossref: 9] [Cited by in F6Publishing: 9] [Article Influence: 1.5] [Reference Citation Analysis]
9 Garcia GA, Cohen SIA, Dobson CM, Knowles TPJ. Nucleation-conversion-polymerization reactions of biological macromolecules with prenucleation clusters. Phys Rev E 2014;89. [DOI: 10.1103/physreve.89.032712] [Cited by in Crossref: 33] [Cited by in F6Publishing: 33] [Article Influence: 4.1] [Reference Citation Analysis]
10 Eisele YS. From soluble aβ to progressive aβ aggregation: could prion-like templated misfolding play a role? Brain Pathol 2013;23:333-41. [PMID: 23587139 DOI: 10.1111/bpa.12049] [Cited by in Crossref: 23] [Cited by in F6Publishing: 22] [Article Influence: 2.6] [Reference Citation Analysis]
11 Saverioni D, Notari S, Capellari S, Poggiolini I, Giese A, Kretzschmar HA, Parchi P. Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions. J Biol Chem 2013;288:27972-85. [PMID: 23897825 DOI: 10.1074/jbc.M113.477547] [Cited by in Crossref: 29] [Cited by in F6Publishing: 24] [Article Influence: 3.2] [Reference Citation Analysis]
12 Solforosi L, Milani M, Mancini N, Clementi M, Burioni R. A closer look at prion strains: characterization and important implications. Prion 2013;7:99-108. [PMID: 23357828 DOI: 10.4161/pri.23490] [Cited by in Crossref: 24] [Cited by in F6Publishing: 22] [Article Influence: 2.7] [Reference Citation Analysis]
13 Zhu C, Liu L, Yang Q, Lv F, Wang S. Water-soluble conjugated polymers for imaging, diagnosis, and therapy. Chem Rev 2012;112:4687-735. [PMID: 22670807 DOI: 10.1021/cr200263w] [Cited by in Crossref: 886] [Cited by in F6Publishing: 891] [Article Influence: 88.6] [Reference Citation Analysis]
14 Cohen SI, Vendruscolo M, Dobson CM, Knowles TP. From macroscopic measurements to microscopic mechanisms of protein aggregation. J Mol Biol 2012;421:160-71. [PMID: 22406275 DOI: 10.1016/j.jmb.2012.02.031] [Cited by in Crossref: 307] [Cited by in F6Publishing: 303] [Article Influence: 30.7] [Reference Citation Analysis]
15 Hedlin P, Taschuk R, Potter A, Griebel P, Napper S. Detection and control of prion diseases in food animals. ISRN Vet Sci 2012;2012:254739. [PMID: 23738120 DOI: 10.5402/2012/254739] [Cited by in Crossref: 8] [Cited by in F6Publishing: 6] [Article Influence: 0.8] [Reference Citation Analysis]
16 Cohen SI, Vendruscolo M, Welland ME, Dobson CM, Terentjev EM, Knowles TP. Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments. J Chem Phys 2011;135:065105. [PMID: 21842954 DOI: 10.1063/1.3608916] [Cited by in Crossref: 209] [Cited by in F6Publishing: 209] [Article Influence: 20.9] [Reference Citation Analysis]
17 Alvarez-martinez M, Fontes P, Zomosa-signoret V, Arnaud J, Hingant E, Pujo-menjouet L, Liautard J. Dynamics of polymerization shed light on the mechanisms that lead to multiple amyloid structures of the prion protein. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2011;1814:1305-17. [DOI: 10.1016/j.bbapap.2011.05.016] [Cited by in Crossref: 19] [Cited by in F6Publishing: 18] [Article Influence: 1.7] [Reference Citation Analysis]
18 Shi Q, Zhang BY, Gao C, Han J, Wang GR, Chen C, Tian C, Dong XP. The diversities of PrP(Sc) distributions and pathologic changes in various brain regions from a Chinese patient with G114V genetic CJD. Neuropathology 2012;32:51-9. [PMID: 21732990 DOI: 10.1111/j.1440-1789.2011.01237.x] [Cited by in Crossref: 14] [Cited by in F6Publishing: 12] [Article Influence: 1.3] [Reference Citation Analysis]
19 Wallace R. Structure and dynamics of the ‘protein folding code’ inferred using Tlusty's topological rate distortion approach. Biosystems 2011;103:18-26. [DOI: 10.1016/j.biosystems.2010.09.007] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 0.4] [Reference Citation Analysis]
20 Manuelidis L. Nuclease resistant circular DNAs copurify with infectivity in scrapie and CJD. J Neurovirol 2011;17:131-45. [PMID: 21165784 DOI: 10.1007/s13365-010-0007-0] [Cited by in Crossref: 29] [Cited by in F6Publishing: 31] [Article Influence: 2.4] [Reference Citation Analysis]
21 Gabrielsson EO, Tybrandt K, Hammarström P, Berggren M, Nilsson KPR. Spatially Controlled Amyloid Reactions Using Organic Electronics. Small 2010;6:2153-61. [DOI: 10.1002/smll.201001157] [Cited by in Crossref: 13] [Cited by in F6Publishing: 10] [Article Influence: 1.1] [Reference Citation Analysis]
22 Mossuto MF, Dhulesia A, Devlin G, Frare E, Kumita JR, de Laureto PP, Dumoulin M, Fontana A, Dobson CM, Salvatella X. The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity. J Mol Biol 2010;402:783-96. [PMID: 20624399 DOI: 10.1016/j.jmb.2010.07.005] [Cited by in Crossref: 73] [Cited by in F6Publishing: 78] [Article Influence: 6.1] [Reference Citation Analysis]