ReviewMicrobiology and molecular biology reviews : MMBR2002
Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.
Review in Microbiology and molecular biology reviews : MMBR, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 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.
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Who cites it
175 citing papers in PubMed, 537 citations in OpenAlex.
- Genome-Wide Characterization and Heat Responsive Expression Profiling of the HSP10 Co-Chaperonin Gene Family inInternational journal of molecular sciences · 2026Article
- Response of nitrogen-fixing plant symbioses to changing temperature.Journal of integrative plant biology · 2026Review
- Impact of N-terminal domain on the sHSP Lo18 function.Scientific reports · 2025Article
- A novel lineage of large aquatic bacteriophages identified through metagenomics.Archives of virology · 2025Article
- In silico approach on structural and functional characterization of heat shock protein from Sulfobacillus acidophilus.Journal of applied genetics · 2025Article
- Article
- Heat tolerance and genetic adaptations in Caenorhabditis briggsae: insights from comparative studies with Caenorhabditis elegans.Genetics · 2025Article
- Among-population proteomic differences in Schistocephalus solidus based on excretory/secretory and total body protein predictions.Parasites & vectors · 2025Article
- Review
- ASR gene family: a case of tandem-drive evolution.Frontiers in molecular biosciences · 2025Article
- Article
- Heat Shock Response and Heat Shock Proteins: Current Understanding and Future Opportunities in Human Diseases.International journal of molecular sciences · 2024Review
- Novel Strategy for In Vitro Validation of Babesia orientalis Heat Shock Proteins Chaperone Activity and Thermostability.Acta parasitologica · 2024Article
- Effects of small heat shock proteins from thermotolerant bacteria on the stress resistance of Escherichia coli to temperature, pH, and hyperosmolarity.Extremophiles : life under extreme conditions · 2024Article
- In Silico Safety Assessment ofInternational journal of molecular sciences · 2024Article
- Effects of Heat Stress on Plant-Nutrient Relations: An Update on Nutrient Uptake, Transport, and Assimilation.International journal of molecular sciences · 2023Review
- Hypoviral-regulated HSP90 co-chaperone p23 (CpCop23) determines the colony morphology, virulence, and viral response of chestnut blight fungus Cryphonectria parasitica.Molecular plant pathology · 2023Article
- Genesis-DB: a database for autonomous laboratory systems.Bioinformatics advances · 2023Article
- Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?Cell stress & chaperones · 2023Review
- Combining enhanced sampling and deep learning dimensionality reduction for the study of the heat shock protein B8 and its pathological mutant K141E.RSC advances · 2022Article
115 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
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alpha-crystallins were originally recognized as proteins contributing to the transparency of the mammalian eye lens. Subsequently, they have been found in many, but not all, members of the Archaea, Bacteria, and Eucarya. Most members of the diverse alpha-crystallin family have four common structural and functional features: (i) a small monomeric molecular mass between 12 and 43 kDa; (ii) the formation of large oligomeric complexes; (iii) the presence of a moderately conserved central region, the so-called alpha-crystallin domain; and (iv) molecular chaperone activity. Since alpha-crystallins are induced by a temperature upshift in many organisms, they are often referred to as small heat shock proteins (sHsps) or, more accurately, alpha-Hsps. Alpha-crystallins are integrated into a highly flexible and synergistic multichaperone network evolved to secure protein quality control in the cell. Their chaperone activity is limited to the binding of unfolding intermediates in order to protect them from irreversible aggregation. Productive release and refolding of captured proteins into the native state requires close cooperation with other cellular chaperones. In addition, alpha-Hsps seem to play an important role in membrane stabilization. The review compiles information on the abundance, sequence conservation, regulation, structure, and function of alpha-Hsps with an emphasis on the microbial members of this chaperone family.
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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.