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

The role of the asparagine-linked oligosaccharides of the alpha-subunit in human thyrotropin bioactivity.

Endocrinology - 1 Feb 1996

Fares F A, Gruener N, Kraiem Z

Abstract excerpt

TSH and the gonadotropins (FSH, LH, and hCG) are a family of heterodimeric proteins that share a common alpha-subunit and differ in their hormone-specific beta-subunit. The asparagine-linked (N-linked) oligosaccharides on these hormones are important in signal transduction. The N-linked oligosaccharides on the alpha-subunit have no effect on hCG and hFSH receptor binding, but are critical for their biological...

Read the complete abstract on PubMed

Topics

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

Share to CHO Cells
Share to Cricetinae
Share to Cyclic AMP

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosylation

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Recombinant Proteins

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 8593802
DOI: 10.1210/endo.137.2.8593802

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The role of the asparagine-linked oligosaccharides of the alpha-subunit in human thyrotropin bioactivity.PMID 8593802Read ↗

Effect of additional N-glycosylation signal in the N-terminal region on intracellular function of the human gonadotropin alpha-subunit.Semantic proximity Read ↗

Single chain human chorionic gonadotropin, hCGalphabeta: effects of mutations in the alpha subunit on structure and bioactivity.Semantic proximity Read ↗

Site-Directed Mutagenesis of the Human Thyrotropin Receptor: Role of Asparagine-Linked Oligosaccharides in the Expression of a Functional ReceptorSemantic proximity Read ↗

Specific roles for the asparagine-linked carbohydrate residues of recombinant human follicle stimulating hormone in receptor binding and signal transduction.Semantic proximity Read ↗

Human thyroid-stimulating hormone: structure-function analysis.Semantic proximity Read ↗

Thyrotropin, follitropin, and chorionic gonadotropin expressed as a single multifunctional unit reveal remarkable permissiveness in receptor-ligand interactions.Semantic proximity Read ↗

Engineering human glycoprotein hormone superactive analogues.Semantic proximity Read ↗

An insertion in the human thyrotropin receptor critical for high affinity hormone binding.Semantic proximity Read ↗

Role of amino acid residues at the interface of alpha52asparginyl-N-glycosyl chain of human choriogonadotropin.Semantic proximity Read ↗

The biological role of the carboxyl-terminal extension of human chorionic gonadotropin [corrected] beta-subunit.Semantic proximity Read ↗

Receptor binding and signal transduction are dissociable functions requiring different sites on follicle-stimulating hormone.Semantic proximity Read ↗

Specific roles for the asparagine-linked carbohydrate residues of recombinant human follicle stimulating hormone in receptor binding and signal transductionSemantic proximity Read ↗

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