Article
Unusual duplication mutation in a surface loop of human transthyretin leads to an aggressive drug-resistant amyloid disease.
Proceedings of the National Academy of Sciences of the United States of America - 10 Jul 2018
Klimtchuk Elena S, Prokaeva Tatiana, Frame Nicholas M, Abdullahi Hassan A, Spencer Brian, Dasari Surendra, Cui Haili, Berk John L, Kurtin Paul J, Connors Lawreen H, Gursky Olga
Abstract excerpt
Transthyretin (TTR) is a globular tetrameric transport protein in plasma. Nearly 140 single amino acid substitutions in TTR cause life-threatening amyloid disease. We report a one-of-a-kind pathological variant featuring a Glu51, Ser52 duplication mutation (Glu51_Ser52dup). The proband, heterozygous for the mutation, exhibited an unusually aggressive amyloidosis that was refractory to treatment with the...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.