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 keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state.
Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterin.
Mildly acidic pH activates the extracellular molecular chaperone clusterin.
Clusterin: the intriguing guises of a widely expressed glycoprotein.
Apolipoprotein J (clusterin) activates rodent microglia in vivo and in vitro.
Association of apolipoprotein J-positive beta-amyloid plaques with dystrophic neurites in Alzheimer's disease brain.
Clusterin inhibits apoptosis by interacting with activated Bax.
Human colostrum: identification of minor proteins in the aqueous phase by proteomics.
Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection.
Isolation and characterization of human apolipoprotein M-containing lipoproteins.
Disrupted in Schizophrenia 1 Interactome: evidence for the close connectivity of risk genes and a potential synaptic basis for schizophrenia.
ERp57 is essential for efficient folding of glycoproteins sharing common structural domains.
The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures.
Characterization of an eppin protein complex from human semen and spermatozoa.
Multiple pathways regulating the anti-apoptotic protein clusterin in breast cancer.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Clusterin is a short half-life, poly-ubiquitinated protein, which controls the fate of prostate cancer cells.
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
Identification of human plasma proteins as major clients for the extracellular chaperone clusterin.
Overexpression of low-density lipoprotein receptor in the brain markedly inhibits amyloid deposition and increases extracellular A beta clearance.
Clusterin facilitates COMMD1 and I-kappaB degradation to enhance NF-kappaB activity in prostate cancer cells.
A comprehensive resource of interacting protein regions for refining human transcription factor networks.
Proteomics characterization of extracellular space components in the human aorta.
Neural hyperactivation in carriers of the Alzheimer's risk variant on the clusterin gene.
Common Alzheimer's disease risk variant within the CLU gene affects white matter microstructure in young adults.
The APP intracellular domain (AICD) potentiates ER stress-induced apoptosis.
The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide.
Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability.
Search for amyloid-binding proteins by affinity chromatography.
GRP78 regulates clusterin stability, retrotranslocation and mitochondrial localization under ER stress in prostate cancer.
Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones.
Clusterin regulates β-amyloid toxicity via Dickkopf-1-driven induction of the wnt-PCP-JNK pathway.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
Purification and characterization of apolipoprotein J.
Apolipoproteins E and J interfere with amyloid-beta uptake by primary human astrocytes and microglia in vitro.
Intracellular clusterin interacts with brain isoforms of the bridging integrator 1 and with the microtubule-associated protein Tau in Alzheimer's disease.
The chaperone activity of clusterin is dependent on glycosylation and redox environment.
PACAP inhibits tumor growth and interferes with clusterin in cervical carcinomas.
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins.
TREM2 Binds to Apolipoproteins, Including APOE and CLU/APOJ, and Thereby Facilitates Uptake of Amyloid-Beta by Microglia.
Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation.
α-Synuclein Interacts with Lipoproteins in Plasma.
LILRB4 signalling in leukaemia cells mediates T cell suppression and tumour infiltration.
α-synuclein-lipoprotein interactions and elevated ApoE level in cerebrospinal fluid from Parkinson's disease patients.
HENA, heterogeneous network-based data set for Alzheimer's disease.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Structural basis of soluble membrane attack complex packaging for clearance.
Interaction of transforming growth factor beta receptors with apolipoprotein J/clusterin.
Potent inhibition of terminal complement assembly by clusterin: characterization of its impact on C9 polymerization.
Interaction of apolipoprotein J-amyloid beta-peptide complex with low density lipoprotein receptor-related protein-2/megalin. A mechanism to prevent pathological accumulation of amyloid beta-peptide.
Possible neuroprotective role of clusterin in Alzheimer's disease: a quantitative immunocytochemical study.
Exocytosis of platelet alpha granule contents
EPPIN protein complex binds bacteria
Clusterin binds C5b-C7, C8, C9
Deep research report on CLU
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CLU central extracellular proteostasis/complement/lipid node
"Converging evidence positions clusterin as a central node at the intersection of extracellular proteostasis, complement regulation, and lipid transport."