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

Phenotype-related differential alpha-2,6- or alpha-2,3-sialylation of glycoprotein N-glycans in human chondrocytes.

Osteoarthritis and cartilage - 1 Feb 2010

Toegel S, Pabst M, Wu S Q, Grass J, Goldring M B, Chiari C, Kolb A, Altmann F, Viernstein H, Unger F M

Abstract excerpt

OBJECTIVE: Sialic acids frequently occur at the terminal positions of glycoprotein N-glycans present at chondrocyte surfaces or in the cartilage matrix. Sialic acids are transferred to glycoproteins in either alpha-2,3 or alpha-2,6 linkage by specific sialyltransferases (SiaTs) and can potentially affect cell functions and cell-matrix interactions. The present study aimed to assess the relationship between the...

Read the complete abstract on PubMed

Topics

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

Share to Chondrocytes
Share to Cell Proliferation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytokines

Share to Glycoproteins

Share to Interleukin-1beta

Share to Reverse Transcriptase Polymerase Chain Reaction

Share to Sialyltransferases

Share to Tumor Necrosis Factor-alpha

Source

Open in PubMed Open full text

Identifiers

PMID: 19800998
DOI: 10.1016/j.joca.2009.09.004
PMCID: PMC2818349

Genes

TNF

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

Phenotype-related differential alpha-2,6- or alpha-2,3-sialylation of glycoprotein N-glycans in human chondrocytes.PMID 19800998Read ↗

IL-1beta and TNF-alpha alter the glycophenotype of primary human chondrocytes in vitro.Semantic proximity Read ↗

Loss of α2-6 sialylation promotes the transformation of synovial fibroblasts into a pro-inflammatory phenotype in Rheumatoid ArthritisSemantic proximity Read ↗

Loss of α2-6 sialylation promotes the transformation of synovial fibroblasts into a pro-inflammatory phenotype in arthritis.Semantic proximity Read ↗

Lectin binding patterns reflect the phenotypic status of in vitro chondrocyte models.Semantic proximity Read ↗

Sialoglycans Modulate Siglec-5 – TLR4 Interactions in OsteoarthritisSemantic proximity Read ↗

Regulation of the metastatic cell phenotype by sialylated glycans.Semantic proximity Read ↗

Sialyltransferases functions in cancersSemantic proximity Read ↗

ST8Sia2 polysialyltransferase protects against infection by <i>Trypanosoma cruzi</i>Semantic proximity Read ↗

Evolution of sialic acids: Implications in xenotransplant biologySemantic proximity Read ↗

Polysialylation is a general feature of immune activationSemantic proximity Read ↗

Identification of sialoylation-related genes as a new diagnostic biomarker of atherosclerosis by machine learningSemantic proximity Read ↗

Glycosylation as a marker for inflammatory arthritisSemantic proximity Read ↗

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