99mTc-DPD scintigraphy in transthyretin-related familial amyloidotic polyneuropathy
✍ Scribed by Max Puille, Klaus Altland, Reinhold P. Linke, Mary K. Steen-Müller, Rigobert Klett, Dagmar Steiner, Richard Bauer
- Publisher
- Springer
- Year
- 2002
- Tongue
- English
- Weight
- 62 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0340-6997
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Amyloidosis is characterised by the extracellular deposition of certain different proteins in a distinctively abnormal fibrillar conformation. All types of amyloid fibril share remarkably similar structural and biophysical properties despite substantial chemical heterogeneity among their respective
Mutations in the serum protein transthyretin (TTR) cause amyloidosis involving the peripheral nerves, heart, and other organs. In Ashkenazic Jews, the only TTR variant described to date has been TTR Ile 33. We have studied DNA from another Ashkenazic Jewish kindred with familial amyloidotic polyneur