Related Overviews


'transthyretin' can also refer to...



Dangerous relationships: aortic stenosis and transthyretin cardiac amyloidosis

A new staging system for cardiac transthyretin amyloidosis

Identification of beta-amyloid-binding sites on transthyretin

Transthyretin variants with improved inhibition of β-amyloid aggregation

Maternal separation stress drastically decreases expression of transthyretin in the brains of adult rat offspring

Different disease-causing mutations in transthyretin trigger the same conformational conversion

Differential modification of Cys10 alters transthyretin's effect on beta-amyloid aggregation and toxicity

The Evolution of the Thyroid Hormone Distributor Protein Transthyretin in the Order Insectivora, Class Mammalia

Transthyretin Leu12Pro is associated with systemic, neuropathic and leptomeningeal amyloidosis

Speckle tracking echo to assess transthyretin amyloidosis type: is it useful (or necessary)?

Wild-type transthyretin amyloidosis as a cause of heart failure with preserved ejection fraction

Getting to the heart of the matter: cardiac involvement in transthyretin-related amyloidosis

Decrease of Transthyretin Synthesis at the Blood–Cerebrospinal Fluid Barrier of Old Sheep

Early detection of nerve injury in transthyretin-related familial amyloid polyneuropathy

Potent Competitive Interactions of Some Brominated Flame Retardants and Related Compounds with Human Transthyretin in Vitro

Transthyretin, Thyroxine, and Retinol-Binding Protein in Human Cerebrospinal Fluid: Effect of Lead Exposure

New Approaches to Assess the Transthyretin Binding Capacity of Bioactivated Thyroid Hormone Disruptors


More Like This

Show all results sharing these subjects:

  • Chemistry
  • Medicine and Health


Show Summary Details

Quick Reference

A plasma protein (4.5 mmol/L in plasma, thyroxine-binding prealbumin, a homotetramer of 127-aa subunits) that is a transport protein for both thyroxine and retinol (vitamin A). Transthyretin forms a complex with retinol-binding protein (2 mmol/L in plasma) and is found in neuritic plaques, neurofibrillary tangles, and microangiopathic lesions of senile cerebral amyloid. Point mutations lead to various distinct forms of amyloidosis and amyloid polyneuropathy.

Subjects: Chemistry — Medicine and Health.

Reference entries

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.