The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Amyloidosis
Abstract
The biochemistry of amyloidosis as it relates to clinical medicine and experimental pathology is presented. Amyloidoses are complex disorders in which normally soluble precursors undergo pathological conformational changes and polymerize as insoluble fibrils with the beta-pleated sheet conformation. Over the past 20 years, 16 biochemically diverse proteins have been identified as fibrillar constituents of amyloid deposits; in all cases the protein-protein interactions that result in amyloid fibril formation appear to be stabilized both by the structure and the microenvironment of the precursor protein. Either genetic predisposition or dysfunctions of the immune system favor amyloid fibril formation. In particular, macrophage function is a factor in the pathogenesis of many of the amyloidoses. The diagnosis of amyloidosis involves acquisition of a tissue biopsy, staining of the specimen with Congo red, and observation of classic green birefringence on polarization microscopy. The subdiagnosis of the systemic amyloidoses involves characterization of variant or monoclonal plasma amyloid precursor proteins in the context of clinical symptoms. Treatment is generally supportive, with the use of antiinflammatory therapy, dialysis, or transplantation and genetic counseling where indicated.
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Cites
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
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Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease
KIDD, M. (1963) · Nature · doi:10.1038/197192b0 · Cited by 1,012
Interleukin 1 of the central nervous system is produced by ameboid microglia.
Giulian, D., Baker, T. J., Shih, L. C., & Lachman, L. B. (1986) · The Journal of experimental medicine · doi:10.1084/jem.164.2.594 · Cited by 859
Perry, G., Friedman, R., Shaw, G., & Chau, V (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.9.3033 · Cited by 623
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Cited by
Alternative conformations of amyloidogenic proteins govern their behavior
Kelly, J. W. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80089-3 · Cited by 593
Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in Vitro
Kayed, R., Bernhagen, J., Greenfield, N., Sweimeh, K., Brunner, H., Voelter, W., & Kapurniotu, A. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2646 · Cited by 351
Meng, F., Abedini, A., Plesner, A., Verchere, C. B., & Raleigh, D. P. (2010) · Biochemistry · doi:10.1021/bi100939a · Cited by 282
Therapeutic strategies for human amyloid diseases
Sacchettini, J. C., & Kelly, J. W. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd769 · Cited by 261
Convertino, M., Das, J., & Dokholyan, N. V. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00195 · Cited by 105
Metadata
- Authors
- Sipe, J. D., & Cohen, A. S.
- Venue
- Critical Reviews in Clinical Laboratory Sciences
- Publisher
- Informa UK Limited
- Published
- 1994-01
- Volume
- 31
- Issue
- 4
- Pages
- 325-354
- ISSN
- 1040-8363 (ISSN-L)
- 1549-781X
- OpenAlex
- W4211192758
- Cited by
- 165
- References
- 7
- FWCI
- 0.40
- Type
- journal article
- Language
- en
- Open access
- closed
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- Sipe, J. D., & Cohen, A. S. (1994). Amyloidosis. Critical Reviews in Clinical Laboratory Sciences. https://doi.org/10.3109/10408369409084679
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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.
