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Abstracts

XIX International Symposium on Amyloidosis Abstracts

References

  • Swuec P, Lavatelli F, Tasaki M, et al. Cryo-EM structure of ­cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient. Nat Commun. 2019;10(1):1269.
  • Puri S, Schulte T, Chaves-Sanjuan A, et al. The Cryo-EM structure of renal amyloid fibril suggests structurally homogeneous multiorgan aggregation in AL Amyloidosis. J Mol Biol. 2023;435(18):168215.

Reference

  • Puri S, Schulte T, Bolognesi M, et al. The Cryo-EM structure of renal amyloid fibril suggests structurally homogeneous multiorgan aggregation in AL amyloidosis. JMB. 2023;435:16215. (IF 6.1), Selected as Journal Cover.

References

  • Picken, MM. The pathology of amyloidosis in classification: a review. Acta Haematol. 2020;143(4):322–334. doi: 10.1159/000506696.
  • Störkel S, Bohl J, Schneider HM. Senile amyloidosis: principles of localization in a heterogeneous form of amyloidosis. Virchows Archiv B Cell Pathol. 1983;44:145. doi: 10.1007/BF02890166.
  • D'Souza A, Theis JD, Vrana JA, et al. Pharmaceutical amyloidosis associated with subcutaneous insulin and enfuvirtide administration. Amyloid. 2014;21(2):71–75. doi: 10.3109/13506129.2013.876984.
  • Samlaska C, Reber S, Murry T. Insulin-derived amyloidosis: the insulin ball, amyloidoma. JAAD Case Rep. 2020;6(4):351–353. doi: 10.1016/j.jdcr.2020.02.011.
  • Shiba M, Kitazawa T. Progressive insulin-derived amyloidosis in a patient with type 2 diabetes. Case Rep Plast Surg Hand Surg. 2016;3(1):73–76. doi: 10.1080/23320885.2016.1247650.
  • Nagase T, Iwaya K, Iwaki Y, et al. Insulin-derived amyloidosis and poor glycemic control: a case series. Am J Med. 2014;127(5):450–454. doi: 10.1016/j.amjmed.2013.10.029.
  • Sanchorawala V. Light-chain (AL) amyloidosis: diagnosis and treatment. Clin J Am Soc Nephrol. 2006;1;1(6):1331–4. doi: 10.2215/CJN.02740806.
  • Vaxman I, Dispenzieri A, Muchtar E, Gertz M. New developments in diagnosis, risk assessment and management in systemic amyloidosis. Blood Rev. 2020;40:100636. doi: 10.1016/j.blre.2019.100636.
  • Du Clos TW, Mold C. Pentraxins (CRP, SAP) in the process of complement activation and clearance of apoptotic bodies through Fcγ receptors. Curr Opin Organ Transplant. 2011;16(1):15–20. doi: 10.1097/MOT.0b013e32834253c7.
  • Multhoff G, Molls M, Radons J. Chronic inflammation in cancer development. Front Immunol. 2012: 2:1664–3224. doi: 10.3389/fimmu.2011.00098.

References

  • Le QC, Wood TC, Alpers CE. De novo AL amyloid in a renal allograft. Am J Nephrol. 1998;18(1):67–70. doi: 10.1159/000013308.
  • Chen DJ, Jiang H, Yang H, He Q, Wang HP, Chen JH. Unusual cause of proteinuria and re-renal failure after kidney transplantation: de novo localized AL amyloidosis in renal allograft. Int Urol Nephrol. 2010;42(2):507–511. doi: 10.1007/s11255-009-9635-9.
  • Qian Q, Nasr SH, Fidler ME, Cornell LD, Sethi S. De novo AL amyloidosis in the kidney allograft. Am J Transplant. 2011 Mar;11(3):606–12. doi: 10.1111/j.1600-6143.2010.03418.x. Epub 2011 Feb 7. PMID: 21342449.
  • Fotiou D, Skalioti C, Liapis G, Marinaki S, Kastritis E. De Novo AL Amyloidosis in Renal Allograft and Anti-CD38 Monoclonal Antibody Treatment. Hemasphere. 2021;5(12):e665. Published 2021 Nov 17. doi: 10.1097/HS9.0000000000000665.