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Appears in Networks 4

In-Edges 5

path(MESH:"Protein Aggregation, Pathological") negativeCorrelation p(HGNC:DNAJB1) View Subject | View Object

Studies of chaperone levels in tissue culture and mouse models of polyQ disease showed that the levels of HSP70 (HSPA1A/B) and DNAJ/HSP40 (DNAJB1), as well as some cochaperones, decline with protein aggregation (64, 65). PubMed:25784053

a(HBP:"polyQ aggregates") decreases act(p(HGNC:DNAJB1)) View Subject | View Object

It has been proposed that such an imbalance may trigger the onset of many neurodegenerative diseases (10, 26), and recent studies report that polyglutamine (polyQ)-based aggregates can se- quester and inhibit the function of a low-abundance cochaper- one, Sis1p/DNAJB1, in protein degradation (27). PubMed:24706768

a(CHEBI:heme) increases p(HGNC:DNAJB1) View Subject | View Object

However, in the presence of 40 μM heme, the toxic response was characterized by the strong induction of heat shock proteins, namely HSP70 (HSPA1B, HSPA4, HSPA5, DNAJB1), HSP72 (HSPA1A), HSP105 (HSPH1), and HSP10 (HSPE1), as well as the proteasome adaptor protein sequestosome. PubMed:26794659

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Cell Ontology (CL)
epithelial cell
MeSH
Kidney
Text Location
Results

Out-Edges 2

p(HGNC:DNAJB1) negativeCorrelation path(MESH:"Protein Aggregation, Pathological") View Subject | View Object

Studies of chaperone levels in tissue culture and mouse models of polyQ disease showed that the levels of HSP70 (HSPA1A/B) and DNAJ/HSP40 (DNAJB1), as well as some cochaperones, decline with protein aggregation (64, 65). PubMed:25784053

p(HGNC:DNAJB1) increases complex(p(HGNC:DNAJB1), p(INTERPRO:"Heat shock protein 70 family"), p(INTERPRO:"Heat shock protein Hsp90 family")) View Subject | View Object

Two subnetworks emerged within this central network, corresponding to known Hsp90 and Hsp70 chaperone complexes (Figure 2, blue and orange squares, respectively). These two subnetworks were bridged by a unique set of cochaperones (Figure 2, tan squares). Among these were the wellknown bridging factors HOP/STIP1, TPR2/DNAJC7, and CHIP/ STUB1, validating our approach (Brychzy et al., 2003; Schmid et al., 2012; Xu et al., 2002). Other bridging factors in this first tier of organization included members of the Hsp40 chaperone family (DNAJB1 and DNAJB6), HSP70-binding protein 1 (HSPBP1), the TPR domain protein EDRF1, and the E3 ligase NRDP1/RNF41 PubMed:25036637

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.