The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation
Open accessAbstract
Amyloids are insoluble protein fibrillar aggregates. The importance of characterizing their aggregation has steadily increased because of their link to human diseases and material science applications. In particular, misfolding and aggregation of the Josephin domain of ataxin-3 is implicated in spinocerebellar ataxia-3. Infrared nanospectroscopy, simultaneously exploiting atomic force microscopy and infrared spectroscopy, can characterize at the nanoscale the conformational rearrangements of proteins during their aggregation. Here we demonstrate that we can individually characterize the oligomeric and fibrillar species formed along the amyloid aggregation. We describe their secondary structure, monitoring at the nanoscale an α-to-β transition, and couple these studies with an independent measurement of the evolution of their intrinsic stiffness. These results suggest that the aggregation of Josephin proceeds from the monomer state to the formation of spheroidal intermediates with a native structure. Only successively, these intermediates evolve into misfolded aggregates and into the final fibrils.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,423
Infrared spectroscopy of proteins
Barth, A. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.06.004 · Cited by 5,129
The Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure
Jackson, M., & Mantsch, H. H. (1995) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239509085140 · Cited by 2,037
Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen
Sunde, M., Serpell, L. C., Bartlam, M., Fraser, P. E., Pepys, M. B., & Blake, C. C. F. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1348 · Cited by 1,707
Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation
Chapman, M. R., Robinson, L. S., Pinkner, J. S., Roth, R., Heuser, J., Hammar, M., Normark, S., & Hultgren, S. J. (2002) · Science · doi:10.1126/science.1067484 · Cited by 1,298
Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010907200 · Cited by 1,096
Functional amyloid – from bacteria to humans
Fowler, D. M., Koulov, A. V., Balch, W. E., & Kelly, J. W. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.03.003 · Cited by 1,059
Nanomechanics of functional and pathological amyloid materials
Knowles, T. P. J., & Buehler, M. J. (2011) · Nature Nanotechnology · doi:10.1038/nnano.2011.102 · Cited by 784
FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils
Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., & Fändrich, M. (2004) · Protein Science · doi:10.1110/ps.041024904 · Cited by 725
Characterization of the nanoscale properties of individual amyloid fibrils
Smith, J. F., Knowles, T. P. J., Dobson, C. M., MacPhee, C. E., & Welland, M. E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604035103 · Cited by 640
Understanding amyloid aggregation by statistical analysis of atomic force microscopy images
Adamcik, J., Jung, J.-M., Flakowski, J., De Los Rios, P., Dietler, G., & Mezzenga, R. (2010) · Nature Nanotechnology · doi:10.1038/nnano.2010.59 · Cited by 619
Self-citationBiology of Amyloid: Structure, Function, and Regulation
Greenwald, J., & Riek, R. (2010) · Structure · doi:10.1016/j.str.2010.08.009 · Cited by 575
Dazzi, A., Prater, C. B., Hu, Q., Chase, D. B., Rabolt, J. F., & Marcott, C. (2012) · Applied Spectroscopy · doi:10.1366/12-06804 · Cited by 557
ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins
Sarroukh, R., Goormaghtigh, E., Ruysschaert, J.-M., & Raussens, V. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.04.012 · Cited by 446
Theory of infrared nanospectroscopy by photothermal induced resonance
Dazzi, A., Glotin, F., & Carminati, R. (2010) · Journal of Applied Physics · doi:10.1063/1.3429214 · Cited by 350
High-resolution Fourier-transform infrared chemical imaging with multiple synchrotron beams
Nasse, M. J., Walsh, M. J., Mattson, E. C., Reininger, R., Kajdacsy-Balla, A., Macias, V., Bhargava, R., & Hirschmugl, C. J. (2011) · Nature Methods · doi:10.1038/nmeth.1585 · Cited by 349
Distinct β-sheet structure in protein aggregates determined by ATR-FTIR spectroscopy
Shivu, B., Seshadri, S., Li, J., Oberg, K. A., Uversky, V. N., & Fink, A. L. (2013) · Biochemistry · doi:10.1021/bi400625v · Cited by 289
Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method
Adamcik, J., Lara, C., Usov, I., Jeong, J. S., Ruggeri, F. S., Dietler, G., Lashuel, H. A., Hamley, I. W., & Mezzenga, R. (2012) · Nanoscale · doi:10.1039/c2nr30768e · Cited by 198
Self-citationNicastro, G., Menon, R. P., Masino, L., Knowles, P. P., McDonald, N. Q., & Pastore, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501732102 · Cited by 188
Self-citationStructural Characteristics of α-Synuclein Oligomers Stabilized by the Flavonoid Baicalein
Hong, D.-P., Fink, A. L., & Uversky, V. N. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.08.039 · Cited by 177
Chemical Imaging Beyond the Diffraction Limit: Experimental Validation of the PTIR Technique
Lahiri, B., Holland, G., & Centrone, A. (2013) · Small · doi:10.1002/smll.201200788 · Cited by 175
The Two-stage Pathway of Ataxin-3 Fibrillogenesis Involves a Polyglutamine-independent Step
Ellisdon, A. M., Thomas, B., & Bottomley, S. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601470200 · Cited by 164
Structural Insights into Functional and Pathological Amyloid
Shewmaker, F., McGlinchey, R. P., & Wickner, R. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.227108 · Cited by 159
Chemical mapping of the distribution of viruses into infected bacteria with a photothermal method
Dazzi, A., Prazérès, R., Glotin, F., Ortéga, J. M., Al-Sawaftah, M., & de Frutos, M. (2007) · Ultramicroscopy · doi:10.1016/j.ultramic.2007.10.008 · Cited by 146
Masino, L., Nicastro, G., Menon, R. P., Piaz, F. D., Calder, L. J., & Pastore, A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.09.065 · Cited by 120
Self-citationAmyloid structure – one but not the same: the many levels of fibrillar polymorphism
Pedersen, J. S., Andersen, C. B., & Otzen, D. E. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07888.x · Cited by 119
Katzenmeyer, A. M., Aksyuk, V., & Centrone, A. (2013) · Analytical Chemistry · doi:10.1021/ac303620y · Cited by 95
Ellisdon, A. M., Pearce, M. C., & Bottomley, S. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.02.058 · Cited by 80
Gales, L., Cortes, L., Almeida, C. M., Melo, C. V., Costa, M. D. C., Maciel, P., Clarke, D. T., Damas, A. M., & Macedo‐Ribeiro, S. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.061 · Cited by 80
Functional interactions as a survival strategy against abnormal aggregation
Masino, L., Nicastro, G., Calder, L. J., Vendruscolo, M., & Pastore, A. (2010) · The FASEB Journal · doi:10.1096/fj.10-161208 · Cited by 76
Self-citationA Major Role for Side-Chain Polyglutamine Hydrogen Bonding in Irreversible Ataxin-3 Aggregation
Natalello, A., Frana, A. M., Relini, A., Apicella, A., Invernizzi, G., Casari, C. S., Gliozzi, A., Doglia, S. M., Tortora, P., & Regonesi, M. E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018789 · Cited by 64
Nanoscale spatially resolved infrared spectra from single microdroplets
Müller, T., Ruggeri, F. S., Kulik, A. J., Shimanovich, U., Mason, T. O., Knowles, T. P. J., & Dietler, G. (2014) · Lab on a Chip · doi:10.1039/c3lc51219c · Cited by 56
Self-citationThe Josephin domain determines the morphological and mechanical properties of ataxin-3 fibrils.
Masino, L., Nicastro, G., Simone, A. D., Calder, L., Molloy, J., & Pastore, A. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.02.056 · Cited by 54
Self-citationSelf-folding and aggregation of amyloid nanofibrils
Paparcone, R., Cranford, S. W., & Buehler, M. J. (2011) · Nanoscale · doi:10.1039/c0nr00840k · Cited by 52
Nicastro, G., Habeck, M., Masino, L., Svergun, D. I., & Pastore, A. (2006) · Journal of Biomolecular NMR · doi:10.1007/s10858-006-9092-z · Cited by 47
Self-citationBemporad, F., & Chiti, F. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.07.013 · Cited by 36
Santambrogio, C., Frana, A. M., Natalello, A., Papaleo, E., Regonesi, M. E., Doglia, S. M., Tortora, P., Invernizzi, G., & Grandori, R. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08438.x · Cited by 18
Cited by
AFM-IR: Technology and Applications in Nanoscale Infrared Spectroscopy and Chemical Imaging
Dazzi, A., & Prater, C. B. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00448 · Cited by 1,082
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
De, S., Wirthensohn, D. C., Flagmeier, P., Hughes, C., Aprile, F. A., Ruggeri, F. S., Whiten, D. R., Emin, D., Xia, Z., Varela, J. A., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09477-3 · Cited by 448
Self-citationModern Scattering‐Type Scanning Near‐Field Optical Microscopy for Advanced Material Research
Chen, X., Hu, D., Mescall, R., You, G., Basov, D. N., Dai, Q., & Liu, M. (2019) · Advanced Materials · doi:10.1002/adma.201804774 · Cited by 401
Infrared and Raman chemical imaging and spectroscopy at the nanoscale
Kurouski, D., Dazzi, A., Zenobi, R., & Centrone, A. (2020) · Chemical Society Reviews · doi:10.1039/c8cs00916c · Cited by 324
Metadata
- Authors
- Ruggeri, F. S., Longo, G., Faggiano, S., Lipiec, E., Pastore, A., & Dietler, G.
- Venue
- Nature Communications
- Published
- 2015-07-28
- Volume
- 6
- Issue
- 1
- Pages
- 7831-7831
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W1852088381
- Cited by
- 289
- References
- 39
- FWCI
- 12.89
- Type
- journal article
- Language
- en
- Open access
- gold
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
