The DOI matches its Crossref record; 235 of the 235 references it cites were found in a registry or an index.
Serum amyloid A – a review
Open accessAbstract
Serum amyloid A (SAA) proteins were isolated and named over 50 years ago. They are small (104 amino acids) and have a striking relationship to the acute phase response with serum levels rising as much as 1000-fold in 24 hours. SAA proteins are encoded in a family of closely-related genes and have been remarkably conserved throughout vertebrate evolution. Amino-terminal fragments of SAA can form highly organized, insoluble fibrils that accumulate in "secondary" amyloid disease. Despite their evolutionary preservation and dynamic synthesis pattern SAA proteins have lacked well-defined physiologic roles. However, considering an array of many, often unrelated, reports now permits a more coordinated perspective. Protein studies have elucidated basic SAA structure and fibril formation. Appreciating SAA's lipophilicity helps relate it to lipid transport and metabolism as well as atherosclerosis. SAA's function as a cytokine-like protein has become recognized in cell-cell communication as well as feedback in inflammatory, immunologic, neoplastic and protective pathways. SAA likely has a critical role in control and possibly propagation of the primordial acute phase response. Appreciating the many cellular and molecular interactions for SAA suggests possibilities for improved understanding of pathophysiology as well as treatment and disease prevention.
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Cited by
Takata, F., Nakagawa, S., Matsumoto, J., & Dohgu, S. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.661838 · Cited by 651
Ultra-High-Throughput Clinical Proteomics Reveals Classifiers of COVID-19 Infection
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Pretorius, E., Vlok, M., Venter, C., Bezuidenhout, J. A., Laubscher, G. J., Steenkamp, J., & Kell, D. B. (2021) · Cardiovascular Diabetology · doi:10.1186/s12933-021-01359-7 · Cited by 518
Local and systemic responses to SARS-CoV-2 infection in children and adults
Yoshida, M., Worlock, K. B., Huang, N., Lindeboom, R. G. H., Butler, C. R., Kumasaka, N., Dominguez Conde, C., Mamanova, L., Bolt, L., Richardson, L., et al. (2022) · Nature · doi:10.1038/s41586-021-04345-x · Cited by 365
Halappanavar, S., van den Brule, S., Nymark, P., Gaté, L., Seidel, C., Valentino, S., Zhernovkov, V., Høgh Danielsen, P., De Vizcaya, A., Wolff, H., et al. (2020) · Particle and Fibre Toxicology · doi:10.1186/s12989-020-00344-4 · Cited by 246
Metadata
- Authors
- Sack, G. H.
- Venue
- Molecular Medicine
- Published
- 2018-08-30
- Volume
- 24
- Issue
- 1
- Pages
- 46-46
- ISSN
- 1076-1551 (ISSN-L)
- 1528-3658
- OpenAlex
- W2889145334
- Cited by
- 499
- References
- 235
- FWCI
- 14.13
- Type
- journal article
- Language
- en
- Open access
- gold
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