The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Amyloidosis: Pathogenesis and New Therapeutic Options
Open accessAbstract
The systemic amyloidoses are a group of complex diseases caused by tissue deposition of misfolded proteins that results in progressive organ damage. The most common type, immunoglobulin light chain amyloidosis (AL), is caused by clonal plasma cells that produce misfolded light chains. The purpose of this review is to provide up-to-date information on diagnosis and treatment options for AL amyloidosis. Early, accurate diagnosis is the key to effective therapy, and unequivocal identification of the amyloidogenic protein may require advanced technologies and expertise. Prognosis is dominated by the extent of cardiac involvement, and cardiac staging directs the choice of therapy. Treatment for AL amyloidosis is highly individualized, determined on the basis of age, organ dysfunction, and regimen toxicities, and should be guided by biomarkers of hematologic and cardiac response. Alkylator-based chemotherapy is effective in almost two thirds of patients. Novel agents are also active, and trials are ongoing to establish their optimal use. Treatment algorithms will continue to be refined through controlled trials. Advances in basic research have led to the identification of new drug targets and therapeutic approaches, which will be integrated with chemotherapy in the future.
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Cites
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
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“In that case, the FLC : ratio or the difference between involved and uninvolved free light chains should be monitored.(20)”
BackgroundSelf-citationTargeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
Pepys, M. B., Herbert, J., Hutchinson, W. L., Tennent, G. A., Lachmann, H. J., Gallimore, J. R., Lovat, L. B., Bartfai, T., Alanine, A., Hertel, C., et al. (2002) · Nature · doi:10.1038/417254a · Cited by 540
Amyloid β protein immunotherapy neutralizes Aβ oligomers that disrupt synaptic plasticity in vivo
Klyubin, I., Walsh, D. M., Lemere, C. A., Cullen, W. K., Shankar, G. M., Betts, V., Spooner, E. T., Jiang, L., Anwyl, R., Selkoe, D. J., et al. (2005) · Nature Medicine · doi:10.1038/nm1234 · Cited by 489
Cited by
Transthyretin (TTR) Cardiac Amyloidosis
Ruberg, F. L., & Berk, J. L. (2012) · Circulation · doi:10.1161/circulationaha.111.078915 · Cited by 708
Cibeira, M. T., Sanchorawala, V., Seldin, D. C., Quillen, K., Berk, J. L., Dember, L. M., Segal, A., Ruberg, F., Meier-Ewert, H., Andrea, N. T., et al. (2011) · Blood · doi:10.1182/blood-2011-01-330738 · Cited by 289
Self-citationLi, J.-M., Xue, Z.-Q., Deng, S.-H., Luo, X.-G., Patrylo, P. R., Rose, G. W., Cai, H., Cai, Y., & Yan, X.-X. (2013) · Neurotoxicity Research · doi:10.1007/s12640-012-9355-2 · Cited by 16
Afrough, A., Saliba, R. M., Hamdi, A., El Fakih, R., Varma, A., Dinh, Y. T., Rondon, G., Cornelison, A. M., Shah, N. D., Bashir, Q., et al. (2015) · Biology of Blood and Marrow Transplantation · doi:10.1016/j.bbmt.2015.03.025 · Cited by 6
Metadata
- Authors
- Merlini, G., Seldin, D. C., & Gertz, M. A.
- Venue
- Journal of Clinical Oncology
- Published
- 2011-05-10
- Volume
- 29
- Issue
- 14
- Pages
- 1924-1933
- ISSN
- 0732-183X (ISSN-L)
- 1527-7755
- OpenAlex
- W2151246487
- Cited by
- 509
- References
- 4
- FWCI
- 17.52
- Type
- journal article
- Language
- en
- Open access
- green
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- Merlini, G., Seldin, D. C., & Gertz, M. A. (2011). Amyloidosis: Pathogenesis and New Therapeutic Options. Journal of Clinical Oncology. https://doi.org/10.1200/jco.2010.32.2271
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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.