ReviewThe Journal of biological chemistry2019
Small heat shock proteins: Simplicity meets complexity.
Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 149 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.
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Who cites it
149 citing papers in PubMed, 297 citations in OpenAlex.
- Identification and characterization of a gene conferring stress resistance in Escherichia coli and cyanobacteria.FEBS open bio · 2026Article
- Intermolecular disulfide bond formation promotes Hsp42 higher-order assembly and shapes client selection in yeast.bioRxiv : the preprint server for biology · 2026Article
- Molecular Equilibrist: The Small Heat Shock Protein IbpA from Mycoplasma.Biomolecules · 2026Article
- Small heat shock proteins with two alpha-crystallin domains: a new set of proteins in the earthworm Eisenia fetida with differential transcriptional responses to stressors.Environmental science and pollution research international · 2026Article
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- Pharmacological Inhibition of the HSPB1-NF-κB Axis Alleviates Brain Injury in a Rat Veno-Venous Extracorporeal Membrane Oxygenation Model.Molecular neurobiology · 2026Article
- Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026Review
- Structural and functional characterization of sHsp from the marine cyanobacteriumBiochemistry and biophysics reports · 2026Article
- Association-induced folding governs surrogate light chain and pre-B cell receptor core assembly.Nature communications · 2026Article
- Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals.Journal of sport and health science · 2025Article
- Anti-aggregation Properties of the Mini-Peptides Derived from Alpha Crystallin Domain of the Small Heat Shock Protein, Tpv HSP 14.3.Molecular biotechnology · 2025Article
- A genetically encoded selection for amyloid-β oligomer binders.Nature chemical biology · 2025Article
- Multiplex neurodegeneration proteotoxicity platform reveals DNAJB6 promotes non-toxic FUS condensate gelation and inhibits neurotoxicity.Nature communications · 2025Article
- Targeting proteostasis pathways for cancer therapy.Journal of pharmaceutical analysis · 2025Review
- Regulatory role of serine 59 in the oligomeric dynamics and chaperone function of αB-crystallin.Scientific reports · 2025Article
- Catalyzing Protein Folding by Chaperones.Biology · 2025Review
- Single Particle Dynamics of Protein Aggregation and Disaggregation in the Presence of the sHsp Proteins IbpAB.Biochemistry · 2025Article
- Comparative Characterization of Plasmodium falciparum Small Heat Shock Proteins and Their Inhibition by Quercetin (3,3',4',5,7-Pentahydroxyflavone).The protein journal · 2025Article
- How does protein aggregate structure affect mechanisms of disaggregation?Biochemical Society transactions · 2025Review
- ER stress and/or ER-phagy in drug resistance? Three coincidences are proof.Cell communication and signaling : CCS · 2025Review
89 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 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small heat shock proteins (sHsps) are a ubiquitous and ancient family of ATP-independent molecular chaperones. A key characteristic of sHsps is that they exist in ensembles of iso-energetic oligomeric species differing in size. This property arises from a unique mode of assembly involving several parts of the subunits in a flexible manner. Current evidence suggests that smaller oligomers are more active chaperones. Thus, a shift in the equilibrium of the sHsp ensemble allows regulating the chaperone activity. Different mechanisms have been identified that reversibly change the oligomer equilibrium. The promiscuous interaction with non-native proteins generates complexes that can form aggregate-like structures from which native proteins are restored by ATP-dependent chaperones such as Hsp70 family members. In recent years, this basic paradigm has been expanded, and new roles and new cofactors, as well as variations in structure and regulation of sHsps, have emerged.
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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.