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Kellermayer, M. S. Z., Karsai, A., Benke, M., Soos, K., Penke, B. (2008) Stepwise dynamics of epitaxially growing single amyloid fibrils. Proceedings of the National Academy of Sciences, 105 (1) 141-144 doi:10.1073/pnas.0704305105

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Reference TypeJournal (article/letter/editorial)
TitleStepwise dynamics of epitaxially growing single amyloid fibrils
JournalProceedings of the National Academy of Sciences
AuthorsKellermayer, M. S. Z.Author
Karsai, A.Author
Benke, M.Author
Soos, K.Author
Penke, B.Author
Year2008 (January 8)Volume105
Issue1
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.0704305105Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID1747529Long-form Identifiermindat:1:5:1747529:7
GUID0
Full ReferenceKellermayer, M. S. Z., Karsai, A., Benke, M., Soos, K., Penke, B. (2008) Stepwise dynamics of epitaxially growing single amyloid fibrils. Proceedings of the National Academy of Sciences, 105 (1) 141-144 doi:10.1073/pnas.0704305105
Plain TextKellermayer, M. S. Z., Karsai, A., Benke, M., Soos, K., Penke, B. (2008) Stepwise dynamics of epitaxially growing single amyloid fibrils. Proceedings of the National Academy of Sciences, 105 (1) 141-144 doi:10.1073/pnas.0704305105
In(2008, January) Proceedings of the National Academy of Sciences Vol. 105 (1) Proceedings of the National Academy of Sciences

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Karsai, Á., Nagy, A., Kengyel, A., Mártonfalvi, Z., Grama, L., Penke, B., Kellermayer, M. S. Z. (2005) Effect of Lysine-28 Side-Chain Acetylation on the Nanomechanical Behavior of Alzheimer Amyloid β25−35 Fibrils. Journal of Chemical Information and Modeling, 45 (6) 1641-1646 doi:10.1021/ci0501701
Paravastu, A. K., Leapman, R. D., Yau, W.-M., Tycko, R. (2008) Molecular structural basis for polymorphism in Alzheimer's  -amyloid fibrils. Proceedings of the National Academy of Sciences, 105 (47) 18349-18354 doi:10.1073/pnas.0806270105
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Reddy, G., Straub, J. E., Thirumalai, D. (2009) Dynamics of locking of peptides onto growing amyloid fibrils. Proceedings of the National Academy of Sciences, 106 (29) 11948-11953 doi:10.1073/pnas.0902473106
Kim, Y. S., Liu, L., Axelsen, P. H., Hochstrasser, R. M. (2008) Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from A 40. Proceedings of the National Academy of Sciences, 105 (22) 7720-7725 doi:10.1073/pnas.0802993105
Rothbard, Jonathan B. (2022) Do amyloid fibrils induce inflammation, or does inflammation generate amyloid fibrils?. Proceedings of the National Academy of Sciences, 119 (40) doi:10.1073/pnas.2213903119
Grama, L., Somogyi, B., Kellermayer, M. S. Z. (2001) Global configuration of single titin molecules observed through chain-associated rhodamine dimers. Proceedings of the National Academy of Sciences, 98 (25) 14362-14367 doi:10.1073/pnas.191494098
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Rousseau, F., Schymkowitz, J., Oliveberg, M. (2008) ALS precursor finally shaken into fibrils. Proceedings of the National Academy of Sciences, 105 (48) 18649-18650 doi:10.1073/pnas.0810568106
Tennent, G. A., Lovat, L. B., Pepys, M. B. (1995) Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. Proceedings of the National Academy of Sciences, 92 (10) 4299-4303 doi:10.1073/pnas.92.10.4299
Fandrich, M., Forge, V., Buder, K., Kittler, M., Dobson, C. M., Diekmann, S. (2003) Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments. Proceedings of the National Academy of Sciences, 100 (26) 15463-15468 doi:10.1073/pnas.0303758100
 
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