Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Human Ig superfamily CTLA-4 gene chromosomal localization and identity of protein sequence between murine and human CTLA-4 cytoplasmic domains.
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Original characterization of human CTLA4 as an Ig superfamily member on chromosome 2.
"Human Ig superfamily CTLA-4 gene: chromosomal localization and identity of protein sequence between murine and human CTLA-4 cytoplasmic domains"
Identification of residues in the V domain of CD80 (B7-1) implicated in functional interactions with CD28 and CTLA4.
CTLA-4 binding to the lipid kinase phosphatidylinositol 3-kinase in T cells.
Tyrosine phosphorylation controls internalization of CTLA-4 by regulating its interaction with clathrin-associated adaptor complex AP-2.
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Phosphorylation of Tyr-201 in YVKM motif prevents AP-2 binding and blocks endocytosis.
"Tyrosine phosphorylation controls internalization of CTLA-4 by regulating its interaction with clathrin-associated adaptor complex AP-2"
Interaction of the cytoplasmic tail of CTLA-4 (CD152) with a clathrin-associated protein is negatively regulated by tyrosine phosphorylation.
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Further evidence for CTLA4-PI3K p85 interaction and clathrin-associated protein binding.
"Interaction of the cytoplasmic tail of CTLA-4 (CD152) with a clathrin-associated protein is negatively regulated by tyrosine phosphorylation"
Resting lymphocyte kinase (Rlk/Txk) phosphorylates the YVKM motif and regulates PI 3-kinase binding to T-cell antigen CTLA-4.
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Rlk/Txk phosphorylates CTLA4 YVKM motif, regulating PI3K binding.
"Resting lymphocyte kinase (Rlk/Txk) phosphorylates the YVKM motif and regulates PI 3-kinase binding to T-cell antigen CTLA-4"
Structural basis for co-stimulation by the human CTLA-4/B7-2 complex.
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3.2A crystal structure of CTLA4/B7-2 complex reveals bivalent network formation at the immunological synapse, providing structural basis for CTLA4 inhibitory function.
"the 3.2-A resolution structure of the complex between the disulphide-linked homodimer of human CTLA-4 and the receptor-binding domain of human B7-2"
Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses.
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3.0A crystal structure of CTLA4/B7-1 complex reveals zipper-like oligomerization forming stable inhibitory signaling complexes.
"CTLA-4 and B7-1 pack in a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers"
Exocytosis of CTLA-4 is dependent on phospholipase D and ADP ribosylation factor-1 and stimulated during activation of regulatory T cells.
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CTLA4 localizes to Golgi, clathrin-coated vesicles, and perinuclear region; exocytosis is PLD and ARF1 dependent.
"Exocytosis of CTLA-4 is dependent on phospholipase D and ADP ribosylation factor-1 and stimulated during activation of regulatory T cells"
A molecular perspective of CTLA-4 function.
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Comprehensive review of CTLA4 molecular function, trafficking, and signaling.
"A molecular perspective of CTLA-4 function"
ATM, CTLA4, MNDA, and HEM1 in high versus low CD38 expressing B-cell chronic lymphocytic leukemia.
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Gene expression profiling in B-CLL identified CTLA4 overexpression associated with good clinical outcome in CD38-low CLL. Study is correlative rather than mechanistic.
"the overexpression of CTLA4 and MNDA was associated with good outcome"
CTLA-4 trafficking and surface expression.
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Review of CTLA4 constitutive endocytosis, recycling, and regulated surface expression.
"CTLA-4 trafficking and surface expression"
Acquisition of suppressive function by activated human CD4+ CD25- T cells is associated with the expression of CTLA-4 not FoxP3.
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CTLA4 expression, not FoxP3, associated with acquisition of suppressive function by activated CD4+CD25- T cells. Surface CTLA4 detected by flow cytometry.
"Acquisition of suppressive function by activated human CD4+ CD25- T cells is associated with the expression of CTLA-4 not FoxP3"
PD-L1 and PD-L2 differ in their molecular mechanisms of interaction with PD-1.
A secreted protein microarray platform for extracellular protein interaction discovery.
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
AUTOIMMUNE DISEASE. Patients with LRBA deficiency show CTLA4 loss and immune dysregulation responsive to abatacept therapy.
Structural basis for cancer immunotherapy by the first-in-class checkpoint inhibitor ipilimumab.
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3.0A crystal structure of ipilimumab bound to CTLA4 shows steric overlap with B7 ligand binding site. Cell-based mutant binding assays confirm surface expression and interaction determinants.
"The crystallographically observed binding interface was confirmed by a comprehensive cell-based binding assay against a library of CTLA-4 mutants"
A reference map of the human binary protein interactome.
A Human IgSF Cell-Surface Interactome Reveals a Complex Network of Protein-Protein Interactions.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
A physical wiring diagram for the human immune system.
Multimodal cell maps as a foundation for structural and functional genomics.
SHP2 phosphatase binds CTLA-4
Phosphorylation of CTLA-4
CTLA4 gene expression is stimulated by FOXP3 and inhibited by RUNX1
Deep research report on CTLA4 function, trafficking, and clinical applications.
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CTLA4 is a canonical Ig-superfamily inhibitory receptor that enforces early checkpoint control of T-cell priming via high-avidity binding to CD80/CD86 and Treg-mediated trans-endocytosis of these ligands.
"CTLA-4 inhibits T-cell activation primarily by binding CD80/CD86 with higher avidity than CD28, thereby limiting signal 2 co-stimulation and inducing tolerance/anergy at the priming phase in lymphoid tissues"