Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Defining the membrane proteome of NK cells.
Malectin forms a complex with ribophorin I for enhanced association with misfolded glycoproteins.
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Malectin forms stable complex with ribophorin I (RPN1)
"we found that malectin formed a stable complex with an endoplasmic reticulum-resident transmembrane protein, ribophorin I"
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RPN1 enhances malectin association with misfolded glycoproteins
"Co-expression of malectin and ribophorin I significantly enhanced the association between malectin and a folding-defective alpha1-antitrypsin variant (null Hong Kong)"
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RPN1 may function as a chaperone recognizing misfolded proteins
"ribophorin I preferentially interacted with misfolded ribonuclease A but not with the native form, suggesting that ribophorin I may function as a chaperone that recognizes misfolded proteins inside cells"
Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.
Cryo-electron microscopy structures of human oligosaccharyltransferase complexes OST-A and OST-B.
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Cryo-EM structure at 3.50 angstroms resolution showing OST complex architecture
"we present high-resolution cryo-electron microscopy structures of human OST-A and OST-B"
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Ribophorin I forms a four-helix bundle in OST-A
"In OST-A, interactions with TMEM258 and STT3A allow ribophorin-I to form a four-helix bundle that can bind to a translating ribosome"
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Removal of the second glucose by glucosidase II
Exocytosis of specific granule membrane proteins
Deep research review of MLEC gene function
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Malectin is a type I ER membrane lectin with lumenal carbohydrate-binding domain
"Human MLEC (Malectin), UniProt Q14165 -- type I membrane protein with a lumenal carbohydrate-binding (malectin) domain, single transmembrane helix and short cytosolic tail"
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Malectin binds specifically to di-glucosylated N-glycans
"Strong, selective recognition of di-glucosylated high-mannose N-glycans (Glc2Man9GlcNAc2, G2M9); epitope centers on a Glc-alpha-1,3-Glc disaccharide"
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Malectin promotes ERAD of misfolded glycoproteins
"In human cells, malectin stably associates with misfolded alpha1-antitrypsin (ATNHK) via G2M9; malectin overexpression enhances ER-associated degradation (ERAD) of ATNHK and reduces its secretion"
Cyberian deep research on MLEC function