By S. Sarantseva
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Extra resources for Amyloidosis - Mechanisms and Prospects for Therapy
Gamez, J. , Madden, B. , Theis, J. , Bergen, H. , 3rd and Dogan, A. (2009). Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens. Blood 114,24: 4957-9. , Stevens, F. J. and Solomon, A. (1999). Thermodynamic instability of human lambda 6 light chains: correlation with fibrillogenicity. Biochemistry 38,42: 14101-8. Wall, J. , Stevens, F. and Dealwis, C. (2004). Structural basis of light chain amyloidogenicity: comparison of the thermodynamic properties, fibrillogenic potential and tertiary structural features of four Vlambda6 proteins.
2010). A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface. Structure 18,5: 563-70. Phipps, J. , Kestler, D. , Foster, J. , Kennel, S. , Weiss, D. , Solomon, A. and Wall, J. S. (2010). Inhibition of pathologic immunoglobulin-free light chain production by small interfering RNA molecules. Exp Hematol 38,11: 1006-13. Poshusta, T. , Sikkink, L. , Clark, R. , Dispenzieri, A. and Ramirez-Alvarado, M. (2009). Mutations in specific structural regions of immunoglobulin light chains are associated with free light chain levels in patients with AL amyloidosis.
Because AA amyloid fibril shows heterogeneity in organ deposition, clarification of the affinity of AA amyloid fibrils to various organs is needed. Addressing the involvement of various organs and systems- renal, GI, cardiac, thyroid, and autonomic nervous-may permit development of therapeutic countermeasures against complications. 9. Conclusion Although significant advances have been made in understanding of the pathology, pathogenesis, and clinical treatment of AA amyloidosis secondary to RA, the disease is still an important complication that warrants investigation.