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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

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Reference TypeJournal (article/letter/editorial)
TitleTwo-dimensional infrared spectra of isotopically diluted amyloid fibrils from A 40
JournalProceedings of the National Academy of Sciences
AuthorsKim, Y. S.Author
Liu, L.Author
Axelsen, P. H.Author
Hochstrasser, R. M.Author
Year2008 (June 3)Volume105
Issue22
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.0802993105Search in ResearchGate
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Mindat Ref. ID1750454Long-form Identifiermindat:1:5:1750454:4
GUID0
Full ReferenceKim, 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
Plain TextKim, 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
In(2008, June) Proceedings of the National Academy of Sciences Vol. 105 (22) Proceedings of the National Academy of Sciences

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Kim, Y. S., Liu, L., Axelsen, P. H., Hochstrasser, R. M. (2009) 2D IR provides evidence for mobile water molecules in  -amyloid fibrils. Proceedings of the National Academy of Sciences, 106 (42) 17751-17756 doi:10.1073/pnas.0909888106
Fang, C., Bauman, J. D., Das, K., Remorino, A., Arnold, E., Hochstrasser, R. M. (2008) Two-dimensional infrared spectra reveal relaxation of the nonnucleoside inhibitor TMC278 complexed with HIV-1 reverse transcriptase. Proceedings of the National Academy of Sciences, 105 (5) 1472-1477 doi:10.1073/pnas.0709320104
Douglas, P. M., Treusch, S., Ren, H.-Y., Halfmann, R., Duennwald, M. L., Lindquist, S., Cyr, D. M. (2008) Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proceedings of the National Academy of Sciences, 105 (20) 7206-7211 doi:10.1073/pnas.0802593105
Hochstrasser, R. M. (2007) Two-dimensional spectroscopy at infrared and optical frequencies. Proceedings of the National Academy of Sciences, 104 (36) 14190-14196 doi:10.1073/pnas.0704079104
Zhuang, W., Abramavicius, D., Voronine, D. V., Mukamel, S. (2007) Simulation of two-dimensional infrared spectroscopy of amyloid fibrils. Proceedings of the National Academy of Sciences, 104 (36) 14233-14236 doi:10.1073/pnas.0700392104
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
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
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
(2008) Correction for del Mercato et al., Charge transport and intrinsic fluorescence in amyloid-like fibrils. Proceedings of the National Academy of Sciences, 105 (16) 6208 doi:10.1073/pnas.0802398105
Zanni, M. T., Ge, N.-H., Kim, Y. S., Hochstrasser, R. M. (2001) Two-dimensional IR spectroscopy can be designed to eliminate the diagonal peaks and expose only the crosspeaks needed for structure determination. Proceedings of the National Academy of Sciences, 98 (20) 11265-11270 doi:10.1073/pnas.201412998
Maiti, S., Walker, G. C., Cowen, B. R., Pippenger, R., Moser, C. C., Dutton, P. L., Hochstrasser, R. M. (1994) Femtosecond coherent transient infrared spectroscopy of reaction centers from Rhodobacter sphaeroides. Proceedings of the National Academy of Sciences, 91 (22) 10360-10364 doi:10.1073/pnas.91.22.10360
 
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