Gene Ontology annotation through association of InterPro records with GO terms
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
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell death.
Towards a proteome-scale map of the human protein-protein interaction network.
HspB8 chaperone activity toward poly(Q)-containing proteins depends on its association with Bag3, a stimulator of macroautophagy.
Mutation in BAG3 causes severe dominant childhood muscular dystrophy.
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A heterozygous BAG3 p.Pro209Leu mutation caused severe childhood-onset myofibrillar myopathy with cardiomyopathy, rigid spine in two patients, and rapid respiratory decline.
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BAG3opathy muscle showed Z-disk disruption, BAG3-positive protein aggregates, and apoptotic nuclei, supporting non-core anti-apoptotic relevance in diseased muscle.
Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3.
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BAG3 regulates macroautophagic protein quality control and recruits p62/SQSTM1 during cellular aging.
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The BAG1-to-BAG3 switch promotes autophagic degradation of insoluble aggregated quality-control substrates in aging cells.
Chaperone-assisted selective autophagy is essential for muscle maintenance.
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BAG3 is part of the CASA complex with HSPA8/HSC70, HSPB8, STUB1/CHIP, and p62.
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CASA is required for Z-disc maintenance in striated muscle and is distinct from canonical chaperone-mediated autophagy.
Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells.
BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins.
Next-generation sequencing to generate interactome datasets.
BAG3 and friends: co-chaperones in selective autophagy during aging and disease.
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BAG3 mediates a macroautophagy pathway using HSP70 specificity for misfolded proteins and involving HSPB8, p62/SQSTM1, LC3, and dynein-dependent aggresome transport.
Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6 cause limb-girdle muscular dystrophy.
Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy.
Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro.
Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease.
A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.
The functional landscape of Hsp27 reveals new cellular processes such as DNA repair and alternative splicing and proposes novel anticancer targets.
A proteome-scale map of the human interactome network.
E-cadherin interactome complexity and robustness resolved by quantitative proteomics.
BAG3 affects the nucleocytoplasmic shuttling of HSF1 upon heat stress.
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
Phenotypic and Interaction Profiling of the Human Phosphatases Identifies Diverse Mitotic Regulators.
BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins.
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BAG3 is a modular scaffolding factor that links HSP70-family chaperones with small heat shock proteins.
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BAG3 IPV motifs mediate small heat shock protein binding while BAG3 can bind HSP70 simultaneously.
Axonal Neuropathies due to Mutations in Small Heat Shock Proteins: Clinical, Genetic, and Functional Insights into Novel Mutations.
Architecture of the human interactome defines protein communities and disease networks.
Myopathy associated BAG3 mutations lead to protein aggregation by stalling Hsp70 networks.
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Myopathy-associated BAG3 mutations preserve HSP70 binding but impair HSP70-dependent client processing, causing aggregation of BAG3, HSP70, HSP70 clients, and BAG3 interactors.
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Genetic or pharmacological disruption of mutant BAG3-HSP70 binding reverses stress-induced protein aggregation in the tested models.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators.
HSP110s exchange ATP for ADP on HSP70s:ADP
Falcon deep research report on BAG3 function
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Synthesizes BAG3 as a force- and stress-responsive proteostasis hub centered on HSP70/sHSP scaffolding, CASA/aggrephagy, Z-disc maintenance, and non-core HSF1/apoptosis roles.