Disease relevance of FBXL12

• Thus, a replication-deficient lacZ recombinant human adenovirus, which naturally does not infect avian cells, allowed highly efficient and specific gene transfer to the liver of ducks in vivo when complexed with N-acetylglucosamine, a ligand for the chicken hepatic lectin [1].

High impact information on FBXL12

• This molecule shows striking sequence homology with chicken asialoglycoprotein receptor (hepatic lectin), suggesting a possible role for Fc epsilon R in endocytosis [2].
• The Fc epsilon receptor showed a marked homology with animal lectins including human and rat asialoglycoprotein receptors, chicken hepatic lectin, and rat mannose binding proteins [3].
• Significant homology was found between the deduced amino acid sequence of the proteoglycan and two regions of a chicken hepatic lectin [4].
• The structure of the gene encoding a chicken liver receptor, the chicken hepatic lectin, which mediates endocytosis of glycoproteins has been established [5].
• Results from the present study suggest that in the plasma membrane, the functional species of the chicken hepatic lectin exists as a trimer [6].

Biological context of FBXL12

• Complete amino acid sequence of a membrane receptor for glycoproteins. Sequence of the chicken hepatic lectin [7].
• The binding site of chicken hepatic lectin [8].
• Phosphorylation of a membrane receptor for glycoproteins. Possible transmembrane orientation of the chicken hepatic lectin [9].
• Three of the exons, which are adjacent to one another, are very similar to the corresponding exons in the gene of a rat hepatic lectin as well as to an exon in the gene of human pulmonary surfactant-associated protein [10].

Anatomical context of FBXL12

• The oligomeric state of the chicken hepatic receptor for N-acetylglucosamine-terminated glycoproteins (the chicken hepatic lectin) has been examined in detergent solution, in various membrane preparations, and in hepatocytes [11].
• BMPG was found to have unique characteristics: it has three types of sugar chains and it shows a marked homology with animal lectins including the human asialoglycoprotein receptor, chicken hepatic lectin and the homing receptor of lymphocytes [12].

Associations of FBXL12 with chemical compounds

• A cDNA clone for the chicken liver receptor which mediates endocytosis of glycoproteins containing terminal N-acetylglucosamine has been isolated and sequenced, confirming the previously obtained amino acid sequence of this protein (which is also known as the chicken hepatic lectin) [13].
• The complete amino acid sequence of chicken hepatic lectin has been established by analysis of peptides generated by chemical cleavage at methionine or tryptophan residues [7].
• The deduced amino acid sequence contains a cysteine-rich region which is homologous with chicken hepatic lectin [14].

Analytical, diagnostic and therapeutic context of FBXL12

• To measure intracellular EGFR sorting, we developed a novel cell fractionation assay toward which cells were co-transfected for chicken hepatic lectin, a receptor for agialoglycoproteins [15].
• The subunit structure of soluble goat hepatic lectin was studied by determining molecular weight under nondenaturing conditions by gel filtration and denaturing conditions by SDS PAGE [16].

References