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MetabolomicsTowards engineering ectomycorrhization into switchgrass bioenergy crops via a lectin receptor-like kinase
Soil-borne microbes can establish compatible relationships with host plants, providing a large variety of nutritive and protective compounds in exchange for photosynthesized sugars. However, the molecular mechanisms mediating the establishment of these beneficial relationships remain unclear. Our pr...
2021-08-11 | MTBLS2597 | MetaboLights
ProteomicsAn unusual dual sugar-binding lectin domain controls the substrate specificity of a mucin-type O-glycosyltransferase
N-acetylgalactosaminyl transferases (GalNAc-Ts) initiate mucin-type O-glycosylation, an abundant and complex post-translational modification that regulates host-microbe interactions, tissue development, and metabolism. GalNAc-Ts contain a C-terminal lectin domain consisting of three homologous repea...
ORGANISM(S): Homo sapiens (Human) 
2024-05-23 | PXD047845 | Pride
Muc1 O-glycosylation Structure Lectin domain Substrate specificity 
ProteomicsGST-SH2 domain of 3BP2, pull down, curdlan-stimulated BMDC
Interacting molecules with GST-fusion protein of the wild-type SH2 domain of 3BP2 (WT) or the mutant form (R486K) were precipitated usng GSH beads and identified by DIA proteome analysis.
ORGANISM(S): Mus Musculus (mouse) 
2024-11-15 | PXD054171 | JPOST Repository
GenomicsArabidopsis PP2-A5, a TIR-Lectin Two-Domain Protein, Confers Defense Properties against Tetranychus urticae
Arabidopsis PP2-A5, a TIR-Lectin Two-Domain Protein, Confers Defense Properties against Tetranychus urticae
PRJNA1469080 | ENA
ProteomicsAntibody-lectin chimeras for glyco-immune checkpoint blockade
Despite the curative potential of checkpoint blockade immunotherapy, most patients remain unresponsive to existing treatments. Glyco-immune checkpoints – interactions of cell-surface glycans with lectin, or glycan-binding, immunoreceptors – have emerged as prominent mechanisms of immune evasion and ...
ORGANISM(S): Homo sapiens (Human) 
2025-08-13 | PXD063934 | Pride
Antibody-lectin chimeras for glyco-immune checkpoint blockade 
TranscriptomicsTranscription profiling of human monocyte derived dendritic cells treated with DC-SIGN initiates an immature dendritic cell phenotype triggering Rho activation that is utilised by HIV-1
DC-SIGN is a C-type lectin expressed by dendritic cells (DCs) that binds HIV-1, sequestering it within multivesicular bodies to facilitate transmission to CD4+ T cells. Here we characterize the molecular basis of signalling through DC-SIGN by large-scale gene expression profiling and phosphoproteome...
ORGANISM(S): Homo sapiens 
2008-06-14 | E-GEOD-6090 | biostudies-arrayexpress
UnknownProteins with an Euonymus lectin-like domain are ubiquitous in Embryophyta.
Not available
S-EPMC2788552 | biostudies-literature
UnknownTransmission of allostery through the lectin domain in selectin-mediated cell adhesion.
Not available
S-EPMC2629216 | biostudies-literature
UnknownAn F-type lectin domain directs the activity of Streptosporangium roseum alpha-l-fucosidase.
Not available
S-EPMC6455950 | biostudies-literature
UnknownThe C-type lectin domain of CD62P (P-selectin) functions as an integrin ligand.
Not available
S-EPMC10130748 | biostudies-literature
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