Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Low plasma concentrations of retinol-binding protein in individuals with mutations affecting position 84 of the transthyretin molecule.

Clinical chemistry - 1 Sept 1995

Waits R P, Yamada T, Uemichi T, Benson M D

Abstract excerpt

Retinol-binding protein (RBP), the principal carrier for vitamin A, is known to form a complex with transthyretin (TTR) for transport in plasma. Individuals from a kindred with the amino acid substitution of serine for isoleucine at position 84 (Ser84) of the TTR molecule show substantial reduction in plasma concentrations of RBP. In the present study, we measured plasma RBP in individuals from several kindreds,...

Topics

Humans
Isoleucine
Mutation
Prealbumin
Reference Values
Retinol-Binding Proteins
Retinol-Binding Proteins, Plasma
Serine

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 7656439

Genes

TTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7656439-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Low plasma concentrations of retinol-binding protein in individuals with mutations affecting position 84 of the transthyretin molecule.PMID 7656439Read ↗

A new transthyretin mutation associated with amyloidotic vitreous opacities. Asparagine for isoleucine at position 84.Semantic proximity Read ↗

A point mutation in transthyretin increases affinity for thyroxine and produces euthyroid hyperthyroxinemia.Semantic proximity Read ↗

Native disulfide bonds in plasma retinol-binding protein are not essential for all-trans-retinol-binding activity.Semantic proximity Read ↗

Studies on the metabolism of retinol and retinol-binding protein in transthyretin-deficient mice produced by homologous recombination.Semantic proximity Read ↗

Inherited defects of thyroxine-binding proteins.Semantic proximity Read ↗

An essential ligand-binding domain in the membrane receptor for retinol-binding protein revealed by large-scale mutagenesis and a human polymorphism.Semantic proximity Read ↗

Novel mutation p.A64D in the Serpina7 gene as a cause of partial thyroxine-binding globulin deficiency associated with increases affinity in transthyretin by a known p.A109T mutation in the TTR gene.Semantic proximity Read ↗

Transthyretin Ile84Thr is associated with familial amyloid polyneuropathy.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.