The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Amyloid nomenclature 2018: recommendations by the International Society of Amyloidosis (ISA) nomenclature committee
Open accessAbstract
The nomenclature committee of the International Society of Amyloidosis (ISA) meets every second year to discuss and formulate recommendations. The conclusions from the discussion at the XVI International Symposium on Amyloidosis in Kumamoto, Japan, 25-29 March 2018 and afterwards are summarized in this Nomenclature Article. From having recommended the use of the designation "amyloid fibril" for in vivo material only, ISA's nomenclature committee now accepts its use more broadly following the international scientific literature. However, it is important always to stress the origin of the β-fibrils in order to avoid misunderstanding. Given the more broad use of the word "amyloid" several classes of amyloid fibrils may be distinguished. For the medical in vivo situation, and to be included in the amyloid nomenclature list, "amyloid" still means mainly extracellular tissue deposits of protein fibrils, recognized by specific properties, such as green-yellow birefringence after staining with Congo red. It should also be underlined that in vivo amyloid fibrils, in addition to the main protein contain associated compounds, particularly serum amyloid P-component (SAP) and proteoglycans, mainly heparan sulfate proteoglycan. With this definition there are presently 36 human amyloid proteins of which 14 appear only associated with systemic amyloidosis and 19 as localized forms. Three proteins can occur both as localized and systemic amyloidosis. Strictly intracellular aggregates are not included in this list.
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Cites
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
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
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Amyloid Deposits and Amyloidosis: The β-Fibrilloses(First of Two Parts)
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The Amyloid State of Proteins in Human Diseases
Eisenberg, D., & Jucker, M. (2012) · Cell · doi:10.1016/j.cell.2012.02.022 · Cited by 1,744
Self-citationX-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS
EANES, E. D., & GLENNER, G. G. (1968) · Journal of Histochemistry & Cytochemistry · doi:10.1177/16.11.673 · Cited by 823
Sipe, J. D., Benson, M. D., Buxbaum, J. N., Ikeda, S.-I., Merlini, G., Saraiva, M. J. M., & Westermark, P. (2016) · Amyloid · doi:10.1080/13506129.2016.1257986 · Cited by 605
Self-citationAtomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks
Hughes, M. P., Sawaya, M. R., Boyer, D. R., Goldschmidt, L., Rodriguez, J. A., Cascio, D., Chong, L., Gonen, T., & Eisenberg, D. S. (2018) · Science · doi:10.1126/science.aan6398 · Cited by 450
Self-citationOnline Registry for Mutations in Hereditary Amyloidosis Including Nomenclature Recommendations
Rowczenio, D. M., Noor, I., Gillmore, J. D., Lachmann, H. J., Whelan, C., Hawkins, P. N., Obici, L., Westermark, P., Grateau, G., & Wechalekar, A. D. (2014) · Human Mutation · doi:10.1002/humu.22619 · Cited by 308
Self-citationImmunotherapeutic clearance of systemic amyloid deposits by antibodies to serum amyloid P component
Pepys, M. B. (2016) · Amyloid · doi:10.1080/13506129.2016.1269735 · Cited by 6
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Garcia-Pavia, P., Rapezzi, C., Adler, Y., Arad, M., Basso, C., Brucato, A., Burazor, I., Caforio, A. L. P., Damy, T., Eriksson, U., et al. (2021) · European Heart Journal · doi:10.1093/eurheartj/ehab072 · Cited by 1,231
Self-citationNguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Dorbala, S., Ando, Y., Bokhari, S., Dispenzieri, A., Falk, R. H., Ferrari, V. A., Fontana, M., Gheysens, O., Gillmore, J. D., Glaudemans, A. W. J. M., et al. (2019) · Journal of Nuclear Cardiology · doi:10.1007/s12350-019-01760-6 · Cited by 484
Self-citationThe expanding amyloid family: Structure, stability, function, and pathogenesis
Sawaya, M. R., Hughes, M. P., Rodriguez, J. A., Riek, R., & Eisenberg, D. S. (2021) · Cell · doi:10.1016/j.cell.2021.08.013 · Cited by 475
Self-citationHereditary transthyretin amyloidosis: a model of medical progress for a fatal disease
Adams, D., Koike, H., Slama, M., & Coelho, T. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0210-4 · Cited by 448
Metadata
- Authors
- Benson, M. D., Buxbaum, J. N., Eisenberg, D. S., Merlini, G., Saraiva, M. J. M., Sekijima, Y., Sipe, J. D., & Westermark, P.
- Venue
- Amyloid
- Publisher
- Informa UK Limited
- Published
- 2018-10-02
- Volume
- 25
- Issue
- 4
- Pages
- 215-219
- ISSN
- 1350-6129 (ISSN-L)
- 1744-2818
- OpenAlex
- W2909222904
- Cited by
- 566
- References
- 9
- FWCI
- 23.86
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Benson, M. D., Buxbaum, J. N., Eisenberg, D. S., Merlini, G., Saraiva, M. J. M., Sekijima, Y., Sipe, J. D., & Westermark, P. (2018). Amyloid nomenclature 2018: recommendations by the International Society of Amyloidosis (ISA) nomenclature committee. Amyloid. https://doi.org/10.1080/13506129.2018.1549825
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