ArticleCell2014
A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.
Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 248 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
248 citing papers in PubMed.
- Safety, Tolerability and Pharmacokinetics of Icapamespib, a Selective Epichaperome Inhibitor, in Healthy Adults.The journal of prevention of Alzheimer's disease · 2022Trial
- First-in-human study of the epichaperome inhibitor PU-H71: clinical results and metabolic profile.Investigational new drugs · 2018Trial
- More than the 'master regulator of cytosolic proteostasis': new roles for HSF1 in promoting tissue health.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Dual proximity-based interactome mapping of FKBP51 and FKBP52 uncovers shared metabolic networks.Biochemical and biophysical research communications · 2026Article
- Structural proteomics reveals that misfolded nascent proteins expose buried lysines for ubiquitination and rapid proteasomal degradation.Cell reports · 2026Article
- Amyloid Precursor Protein Processing Links Female Urgency Urinary Incontinence with Alzheimer's Disease: Implications for Treatment.International journal of molecular sciences · 2026Article
- Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome.Cell stress & chaperones · 2026Article
- Structural basis of chaperone mechanisms in cells and the evolutionary emergence of the protein world.bioRxiv : the preprint server for biology · 2026Article
- NFYA regulates two sequential genome-wide transcriptional activation events during oocyte to embryo transition.bioRxiv : the preprint server for biology · 2026Article
- Domain-selective folding of the tandem β-propeller protein Coronin 7 (Coro7) by the chaperonin CCT/TRiC.The Journal of biological chemistry · 2026Article
- Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026Review
- CFTR functions as a tumor suppressor in adenoid cystic carcinoma and its silencing reveals an associated vulnerability involving the Hsp70 chaperone system.Frontiers in oncology · 2026Article
- R405W Desmin Knock-In Mice Highlight Alterations of Mitochondria, Protein Quality Control and Myofibrils in Myofibrillar Myopathy.Journal of cachexia, sarcopenia and muscle · 2025Article
- Multiplex neurodegeneration proteotoxicity platform reveals DNAJB6 promotes non-toxic FUS condensate gelation and inhibits neurotoxicity.Nature communications · 2025Article
- The Kelch 3 motif on gigaxonin mediates the interaction with NUDCD3 and regulates vimentin filament morphology.European journal of cell biology · 2025Article
- The Hsp90β Isoform: An Attractive Target for Drug Development.Medicinal research reviews · 2025Review
- Cardiopulmonary Bypass-Induced IL-17A Aggravates Caspase-12-Dependent Neuronal Apoptosis Through the Act1-IRE1-JNK1 Pathway.Biomolecules · 2025Article
- Heat shock protein 90 chaperone activity is required for hepatitis A virus replication.Journal of virology · 2025Article
- Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 2025Review
- Advances in the structures, mechanisms and targeting of molecular chaperones.Signal transduction and targeted therapy · 2025Review
188 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.