Discover Community Create You

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

Cis and trans actions of the cholinesterase-like domain within the thyroglobulin dimer.

The Journal of biological chemistry - 4 Jun 2010

Wang Xiaofan, Lee Jaemin, Di Jeso Bruno, Treglia A Sonia, Comoletti Davide, Dubi Noga, Taylor Palmer, Arvan Peter

Abstract excerpt

Thyroglobulin (Tg, precursor for thyroid hormone synthesis) is a large secreted glycoprotein composed of upstream regions I-II-III, followed by the approximately 570 residue cholinesterase-like (ChEL) domain. ChEL has two identified functions: 1) homodimerization, and 2) binding to I-II-III that facilitates I-II-III oxidative maturation required for intracellular protein transport. Like its homologs in the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Protein Folding
Share to Acetylcholinesterase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Adhesion Molecules, Neuronal

Share to Cholinesterases

Share to Dimerization

Share to Molecular Chaperones

Share to Oxidative Stress

Share to Thyroglobulin

Source

Open in PubMed Open full text

Identifiers

PMID: 20353937
DOI: 10.1074/jbc.M110.111641
PMCID: PMC2878521

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cis and trans actions of the cholinesterase-like domain within the thyroglobulin dimer.PMID 20353937Read ↗

The Cholinesterase-like Domain, Essential in Thyroglobulin Trafficking for Thyroid Hormone Synthesis, Is Required for Protein DimerizationSemantic proximity Read ↗

The acetylcholinesterase homology region is essential for normal conformational maturation and secretion of thyroglobulin.Semantic proximity Read ↗

Repeat motif-containing regions within thyroglobulin.Semantic proximity Read ↗

The cholinesterase-like domain of thyroglobulin functions as an intramolecular chaperone.Semantic proximity Read ↗

Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology.Semantic proximity Read ↗

Congenital hypothyroidism mutations affect common folding and trafficking in the α/β-hydrolase fold proteins.Semantic proximity Read ↗

Structural roles of acetylcholinesterase variants in biology and pathology.Semantic proximity Read ↗

The structure of human thyroglobulin.Semantic proximity Read ↗

Processing of cholinesterase-like α/β-hydrolase fold proteins: alterations associated with congenital disorders.Semantic proximity Read ↗

Trimerization domain of the collagen tail of acetylcholinesterase.Semantic proximity Read ↗

Hierarchy of Post-translational Modifications Involved in the Circulatory Longevity of GlycoproteinsSemantic proximity Read ↗

Oligomerization of chicken acetylcholinesterase does not require intersubunit disulfide bonds.Semantic proximity Read ↗

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