Falcon deep research report for DNAJB2

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

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons.

The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities.

Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3.

The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation.

Molecular chaperone mediated late-stage neuroprotection in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis.

A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.

Protein kinase CK2 modulates HSJ1 function through phosphorylation of the UIM2 domain.

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b.

Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70.

Neuromuscular diseases due to chaperone mutations - a review and some new results.

Extension of the DNAJB2a isoform in a dominant neuromyopathy family.

Current advance on distal myopathy genetics.

J protein mutations and resulting proteostasis collapse.

Impaired DNAJB2 response to heat shock in fibroblasts from a neuropathy patient with DNAJB2/HSJ1 mutation - cystamine as a potential therapeutic intervention.

The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation.

HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome.

Molecular chaperone-mediated rescue of mitophagy by a Parkin RING1 domain mutant.

DNAJB2 source and assay guide