IDENTIFICATION OF TRANSTHYRETIN BINDING DRUGS WITH POTENTIAL THERAPEUTIC USAGE IN HEREDO FAMILIAL AMYLOIDOSIS
- 1 Anni 1998/1999
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Pubblicazioni Scientifiche
- AMERICAN JOURNAL OF PATHOLOGY
The new apolipoprotein A-I variant Leu174 → Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide
- AMERICAN JOURNAL OF PATHOLOGY
4′-iodo-4′-deoxydoxorubicin disrupts the fibrillar structure of transthyretin amyloid
- CELLULAR AND MOLECULAR LIFE SCIENCES
Biological activity and pathological implications of misfolded proteins
- ELECTROPHORESIS
Affinity capillary electrophoresis is a powerful tool to identify transthyretin binding drugs for potential therapeutic use in amyloidosis
- JOURNAL OF INTERNAL MEDICINE
The systemic amyloidoses: clearer understanding of the molecular mechanisms offers hope for more effective therapies
- PROTEIN SCIENCE
Removal of the N-terminal hexapeptide from human β2-microglobulin facilitates protein aggregation and fibril formation