ArticleTrends in biochemical sciences2012
Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions.
Article in Trends in biochemical sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 258 papers.
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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
258 citing papers in PubMed, 530 citations in OpenAlex.
- The kinetic basis of photosynthetic heat tolerance.Nature ecology & evolution · 2026Article
- Caenorhabditis elegans small heat-shock protein HSP-12.6 has a highly specialized protective function towards muscle thick filaments in vivo.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Article
- Genome-Wide Characterization and Heat Responsive Expression Profiling of the HSP10 Co-Chaperonin Gene Family inInternational journal of molecular sciences · 2026Article
- Conditionally essential: A testis-enriched heat shock protein from fall armyworm safeguards fertility and survival under heat stress.Pest management science · 2026Article
- Article
- Integrated Proteomic and Functional Analyses Reveal the Roles of Organelle-Specific Small Heat Shock Proteins (sHSPs) in Tomato Thermotolerance.Plants (Basel, Switzerland) · 2026Article
- Cellular Stress and Immune Activation in Celiac Disease: Is the Chaperone System a Key Player?Biology · 2026Review
- Small heat shock proteins HspB1 and HspB5 differentially alter the condensation and aggregation of the TDP-43 low-complexity domain.Protein science : a publication of the Protein Society · 2026Article
- Structural and functional characterization of sHsp from the marine cyanobacteriumBiochemistry and biophysics reports · 2026Article
- Revisiting the Small Heat Shock Protein Family inmicroPublication biology · 2026Article
- Genome-wide Characterization of Heat Shock Protein (HSP) Genes in Tuta (Phthorimaea) Absoluta: Insights into Thermal Stress Response.Neotropical entomology · 2025Article
- Solid-Phase Synthesis Approaches and U-Rich RNA-Binding Activity of Homotrimer Nucleopeptide Containing Adenine Linked toInternational journal of molecular sciences · 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
- Genome-wide identification and multi-level analysis of the HSP gene superfamily in Aphidoletes aphidimyza: sHSP gene family expansion and its role in diapause regulation.BMC genomics · 2025Article
- Regulatory role of serine 59 in the oligomeric dynamics and chaperone function of αB-crystallin.Scientific reports · 2025Article
- Novel cardiac biomarkers and multiple-marker approach in the early detection, prognosis, and risk stratification of cardiac diseases.World journal of cardiology · 2025Review
- Unraveling developmental gene regulation in holometabolous insects through comparative transcriptomics and proteomics.Communications biology · 2025Article
- Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025Review
- Genome-Wide Identification and Evolution-Profiling Analysis ofInternational journal of molecular sciences · 2025Article
- The CRY1-COP1-HY5 axis mediates blue-light regulation of Arabidopsis thermotolerance.Plant communications · 2025Article
198 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The small heat shock proteins (sHSPs) and the related α-crystallins (αCs) are virtually ubiquitous proteins that are strongly induced by a variety of stresses, but that also function constitutively in multiple cell types in many organisms. Extensive research has demonstrated that a majority of sHSPs and αCs can act as ATP-independent molecular chaperones by binding denaturing proteins and thereby protecting cells from damage due to irreversible protein aggregation. As a result of their diverse evolutionary history, their connection to inherited human diseases, and their novel protein dynamics, sHSPs and αCs are of significant interest to many areas of biology and biochemistry. However, it is increasingly clear that no single model is sufficient to describe the structure, function or mechanism of action of sHSPs and αCs. In this review, we discuss recent data that provide insight into the variety of structures of these proteins, their dynamic behavior, how they recognize substrates, and their many possible cellular roles.
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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.