The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins
Open accessAbstract
Amyloid refers to insoluble protein aggregates that are responsible for amyloid diseases but are also implicated in important physiological functions (functional amyloids). The widespread presence of protein aggregates but also, in most of the cases, their deleterious effects explain worldwide efforts made to understand their formation, structure and biological functions. We emphasized the role of FTIR and especially ATR-FTIR techniques in amyloid protein and/or peptide studies. The multiple advantages provided by ATR-FTIR allow an almost continuous structural view of protein/peptide conversion during the aggregation process. Moreover, it is now well-established that infrared can differentiate oligomers from fibrils simply on their spectral features. ATR-FTIR is certainly the fastest and easiest method to obtain this information. ATR-FTIR occupies a key position in the analysis and comprehension of the complex aggregation mechanism(s) at the oligomer and/or fibril level. These mechanism(s) seem to present strong similarities between different amyloid proteins and might therefore be extremely important to understand for both disease-associated and functional amyloid proteins. This article is part of a Special Issue entitled: FTIR in membrane proteins and peptide studies.
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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RetractedThe 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
Infrared spectroscopy of proteins
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“vibrations (for a complete description of this method sees the following references [103,104]).”
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“[21] recognizes a wide variety of amyloidogenic oligomers (Aβ, hIAPP, α-synuclein, lysosyme, insulin) as well as pore-forming proteins (α-hemolysin, .”
BackgroundInherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
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Cited by
A new era for understanding amyloid structures and disease
Iadanza, M. G., Jackson, M. P., Hewitt, E. W., Ranson, N. A., & Radford, S. E. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0060-8 · Cited by 980
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Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N.-V., Coté, S., De Simone, A., Doig, A. J., Faller, P., Garcia, A., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 584
Ruggeri, F. S., Longo, G., Faggiano, S., Lipiec, E., Pastore, A., & Dietler, G. (2015) · Nature Communications · doi:10.1038/ncomms8831 · Cited by 289
How to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy
Moran, S. D., & Zanni, M. T. (2014) · The Journal of Physical Chemistry Letters · doi:10.1021/jz500794d · Cited by 264
Metadata
- Authors
- Sarroukh, R., Goormaghtigh, E., Ruysschaert, J.-M., & Raussens, V.
- Venue
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Publisher
- Elsevier BV
- Published
- 2013-10
- Volume
- 1828
- Issue
- 10
- Pages
- 2328-2338
- ISSN
- 0005-2736 (ISSN-L)
- OpenAlex
- W2160829101
- Cited by
- 446
- References
- 13
- FWCI
- 11.77
- Type
- journal article
- Language
- en
- Open access
- bronze
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