4.7 Review

Transthyretin: a review from a structural perspective

Journal

CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 58, Issue 10, Pages 1491-1521

Publisher

SPRINGER BASEL AG
DOI: 10.1007/PL00000791

Keywords

transthyretin; throxine; retinol; vitamin A; amyloid; structure

Ask authors/readers for more resources

Transthyretin (formerly called prealbumin) plays important physiological roles as a transporter of thyroxine and retinol-binding protein. X-ray structural studies have provided information on the active conformation of the protein and the site of binding of both ligands. Transthyretin is also one of the precursor proteins commonly found in amyloid deposits. Both wild-type and single-amino-acid-substituted variants have been identified in amyloid deposits, the variants being more amyloidogenic. Sequencing of the gene and the resulting production of a transgenic mouse model have resulted in progress toward solving the mechanism of amyloid formation and detecting the variant gene in individuals at risk.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available