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

Structural and functional analyses of the human Toll-like receptor 3. Role of glycosylation.

The Journal of biological chemistry - 21 Apr 2006

Sun Jingchuan, Duffy Karen E, Ranjith-Kumar C T, Xiong Jin, Lamb Roberta J, Santos Jon, Masarapu Hema, Cunningham Mark, Holzenburg Andreas, Sarisky Robert T, Mbow M Lamine, Kao Cheng

Abstract excerpt

Toll-like receptors (TLRs) play critical roles in bridging the innate and adaptive immune responses. The human TLR3 recognizes foreign-derived double-stranded RNA and endogenous necrotic cell RNA as ligands. Herein we characterized the contribution of glycosylation to TLR3 structure and function. Exogenous addition of purified extracellular domain of TLR3 (hTLR3 ECD) expressed in human embryonic kidney cells was...

Read the complete abstract on PubMed

Topics

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

Share to Tunicamycin
Share to Cell Separation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosylation

Share to Image Processing, Computer-Assisted

Share to Mass Spectrometry

Share to NF-kappa B

Share to RNA, Double-Stranded

Share to Toll-Like Receptor 3

Source

Identifiers

PMID: 16533755
DOI: 10.1074/jbc.M510442200

Genes

TLR3
ECD

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

Structural and functional analyses of the human Toll-like receptor 3. Role of glycosylation.PMID 16533755Read ↗

The dsRNA binding site of human Toll-like receptor 3.Semantic proximity Read ↗

Four N-linked glycosylation sites in human toll-like receptor 2 cooperate to direct efficient biosynthesis and secretion.Semantic proximity Read ↗

How and why plants and human N-glycans are different: Insight from molecular dynamics into the “glycoblocks” architecture of complex carbohydratesSemantic proximity Read ↗

Comprehensive modeling and functional analysis of Toll‐like receptor ligand‐recognition domainsSemantic proximity Read ↗

N-Linked glycosylation of the membrane protein ectodomain regulates infectious bronchitis virus-induced ER stress response, apoptosis and pathogenesisSemantic proximity Read ↗

Structural insights reveal interplay between LAG-3 homodimerization, ligand binding, and function.Semantic proximity Read ↗

Antiviral Protection by IFITM3 In VivoSemantic proximity Read ↗

N-terminal binding site in the human toll-like receptor 3 ectodomain.Semantic proximity Read ↗

The toll-like receptor 3:dsRNA signaling complex.Semantic proximity Read ↗

Human Toll-Like Receptor 4 (hTLR4): Structural and functional dynamics in cancerSemantic proximity Read ↗

Secretion of the human Toll-like receptor 3 ectodomain is affected by single nucleotide polymorphisms and regulated by Unc93b1.Semantic proximity Read ↗

Dimerization of Toll-like receptor 3 (TLR3) is required for ligand binding.Semantic proximity Read ↗

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