ArticleScience (New York, N.Y.)2019
Structural basis for client recognition and activity of Hsp40 chaperones.
Article in Science (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
87 citing papers in PubMed, 158 citations in OpenAlex.
- Review
- Human Hsp70 paralogs display selective J-domain interactions tuning proteostasis under stress.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- YTHDC1 functions as a molecular chaperone to suppress ALS-linked hnRNPA1 mutants from aggregation.Nature communications · 2026Article
- Wiring of cellular proteostasis by J-domain proteins.Cell stress & chaperones · 2026Review
- Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026Review
- SARS-CoV-2 Helicase (NSP13) Interacts with Mammalian Polyamine and HSP Partners in Promoting Viral Replication.Current issues in molecular biology · 2026Article
- Origin of class B J-domain proteins involved in amyloid transactions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Heat shock proteins in male infertility: recent advances and clinical implications.Frontiers in cell and developmental biology · 2026Review
- Synaptic Chaperone Dysfunction as a Convergent Mechanism in Neurodegenerative and Psychiatric Disorders.Neuroscience insights · 2026Review
- Codon usage bias and molecular evolution ofFrontiers in genetics · 2026Article
- Ultraweak interactions drive cap-mediated positioning and elongation of the bacterial flagellar filament.Nature communications · 2025Article
- Heat shock proteins at the crossroads of endosomal trafficking pathways.Cell biology and toxicology · 2025Review
- An optimizedJournal of biomolecular NMR · 2025Article
- Heat shock protein DNAJA2 controls insulin signaling and glucose homeostasis by preventing spontaneous insulin receptor endocytosis.Nature communications · 2025Article
- Mechanisms of assembly and function of the Hsp70-Hsp40 chaperone machinery.Molecular cell · 2025Article
- Inhibition of the assembly ofmBio · 2025Article
- Remote on-off switching of protein activity by intrinsically disordered region.Nature structural & molecular biology · 2025Article
- Transcriptional Condensates: Epigenetic Reprogramming and Therapeutic Targets in Hematologic Malignancies.Cancers · 2025Review
- Biochemistry of Heat Shock Proteins From Human Intracellular Protozoan Parasites as Diagnostic and Therapeutic Biomarkers.Biochemistry · 2025Review
- A low-complexity linker as a driver of intra- and intermolecular interactions in DNAJB chaperones.Nature communications · 2025Article
27 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Hsp70 and Hsp40 chaperones work synergistically in a wide range of biological processes including protein synthesis, membrane translocation, and folding. We used nuclear magnetic resonance spectroscopy to determine the solution structure and dynamic features of an Hsp40 in complex with an unfolded client protein. Atomic structures of the various binding sites in the client complexed to the binding domains of the Hsp40 reveal the recognition pattern. Hsp40 engages the client in a highly dynamic fashion using a multivalent binding mechanism that alters the folding properties of the client. Different Hsp40 family members have different numbers of client-binding sites with distinct sequence selectivity, providing additional mechanisms for activity regulation and function modification. Hsp70 binding to Hsp40 displaces the unfolded client. The activity of Hsp40 is altered in its complex with Hsp70, further regulating client binding and release.
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What OpenQuestion holds
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.