http://purl.uniprot.org/citations/25036637 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/25036637 | http://www.w3.org/2000/01/rdf-schema#comment | "Chaperones are abundant cellular proteins that promote the folding and function of their substrate proteins (clients). In vivo, chaperones also associate with a large and diverse set of cofactors (cochaperones) that regulate their specificity and function. However, how these cochaperones regulate protein folding and whether they have chaperone-independent biological functions is largely unknown. We combined mass spectrometry and quantitative high-throughput LUMIER assays to systematically characterize the chaperone-cochaperone-client interaction network in human cells. We uncover hundreds of chaperone clients, delineate their participation in specific cochaperone complexes, and establish a surprisingly distinct network of protein-protein interactions for cochaperones. As a salient example of the power of such analysis, we establish that NUDC family cochaperones specifically associate with structurally related but evolutionarily distinct β-propeller folds. We provide a framework for deciphering the proteostasis network and its regulation in development and disease and expand the use of chaperones as sensors for drug-target engagement."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2014.05.039"xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/author | "Gingras A.C."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/author | "Choi H."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/author | "Peng J."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/author | "Berger B."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/author | "Larsen B."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/author | "Lindquist S."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/author | "Lin Z.Y."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/author | "Taipale M."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/author | "Tucker G."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/author | "Krykbaeva I."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/pages | "434-448"xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/title | "A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways."xsd:string |
http://purl.uniprot.org/citations/25036637 | http://purl.uniprot.org/core/volume | "158"xsd:string |
http://purl.uniprot.org/citations/25036637 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25036637 |
http://purl.uniprot.org/citations/25036637 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/25036637 |
http://purl.uniprot.org/uniprot/O95816#attribution-B6EE8700A64D4CAC04F9FD76B13E12BB | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/25036637 |
http://purl.uniprot.org/uniprot/O43765#attribution-B6EE8700A64D4CAC04F9FD76B13E12BB | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/25036637 |
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http://purl.uniprot.org/uniprot/#_A0A0A6YX42-mappedCitation-25036637 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25036637 |