Results 201 to 210 of about 155,572 (257)

Reprogramming CD8+ T-cell Branched N-Glycosylation Limits Exhaustion, Enhancing Cytotoxicity and Tumor Killing. [PDF]

open access: yesCancer Immunol Res
Azevedo CM   +17 more
europepmc   +1 more source

α2,3‐Sialyltransferase (ST3Gal1) regulates endometrioid‐type epithelial ovarian cancer cell migration and invasion via VEGF‐R2/JAK2/STAT3 signaling cascades

open access: yesInternational Journal of Gynecology &Obstetrics, EarlyView.
Abstract Objective To investigate the role of ST3 β‐galactoside α‐2,3‐sialyltransferase 1 (ST3Gal1) and vascular endothelial growth factor receptor 2 (VEGF‐R2) in endometrioid‐type epithelial ovarian cancer (E‐OC) because aberrant α2,3‐sialylation mediated by ST3Gal1 and VEGF‐R2‐related angiogenesis is linked with tumor progression. Methods ST3Gal1 and
Wei‐Ting Chao   +5 more
wiley   +1 more source

Comparative N-Glycoproteomics Reveals Subtype-Specific N-Glycosylation Signatures and Immune Associations in Cholangiocarcinoma. [PDF]

open access: yesMol Cell Proteomics
Xia Z   +18 more
europepmc   +1 more source

Hybrid Adjuvant-Allergen H1sD2 Proteoforms Enhance Innate Immunity Activation via Distinct N-Glycosylation Profiles. [PDF]

open access: yesCells
Lopandić Z   +5 more
europepmc   +1 more source

N-Glycosylation as a Key Requirement for the Positive Interaction of Integrin and uPAR in Glioblastoma. [PDF]

open access: yesInt J Mol Sci
Ferreira GM   +7 more
europepmc   +1 more source

N-Glycosylation

2021
N-glycosylation is a highly conserved glycan modification, and more than 7000 proteins are N-glycosylated in humans. N-glycosylation has many biological functions such as protein folding, trafficking, and signal transduction. Thus, glycan modification to proteins is profoundly involved in numerous physiological and pathological processes.
Tetsuya, Hirata, Yasuhiko, Kizuka
openaire   +2 more sources

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