ArticleJournal of molecular evolution1995
The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain".
Article in Journal of molecular evolution, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.
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Who cites it
111 citing papers in PubMed.
- Intermolecular disulfide bond formation promotes Hsp42 higher-order assembly and shapes client selection in yeast.bioRxiv : the preprint server for biology · 2026Article
- Transcriptional insights into molecular events occurring during tuber maturation of tigernut (Cyperus esculentus L.).Functional & integrative genomics · 2026Article
- Article
- TaHSP18.6 and TaSRT1 interact to confer resistance toProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Functional proteomic insights into the lateral oviduct-associated secretions of a bean bug.iScience · 2025Article
- A Study on the Temperature-Dependent Behavior of Small Heat Shock Proteins from Methanogens.International journal of molecular sciences · 2025Article
- Mechanism of small heat shock protein client sequestration and induced polydispersity.Nature communications · 2025Article
- Review
- A method for the analysis of the oligomerization profile of the Huntington's disease-associated, aggregation-prone mutant huntingtin protein by isopycnic ultracentrifugation.Frontiers in molecular biosciences · 2024Article
- Human Small Heat Shock Protein B8 Inhibits Protein Aggregation without Affecting the Native Folding Process.Journal of the American Chemical Society · 2023Article
- HSPB1 facilitates chemoresistance through inhibiting ferroptotic cancer cell death and regulating NF-κB signaling pathway in breast cancer.Cell death & disease · 2023Article
- Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?Cell stress & chaperones · 2023Review
- Endoplasmic Reticulum Stress of Gut Enterocyte and Intestinal Diseases.Frontiers in molecular biosciences · 2022Review
- Heat Shock Protein 20 Gene Superfamilies in Red Algae: Evolutionary and Functional Diversities.Frontiers in plant science · 2022Article
- Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.Frontiers in molecular biosciences · 2022Review
- Understanding Diversity, Evolution, and Structure of Small Heat Shock Proteins in Annelida Through in Silico Analyses.Frontiers in physiology · 2022Article
- Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.Nature communications · 2021Article
- Structural basis of substrate recognition and thermal protection by a small heat shock protein.Nature communications · 2021Article
- Genome-Wide Analysis of the HSP20 Gene Family and Expression Patterns ofFrontiers in genetics · 2021Article
- Analysis of insect nuclear small heat shock proteins and interacting proteins.Cell stress & chaperones · 2021Article
51 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ever-increasing number of proteins identified as belonging to the family of small heat-shock proteins (shsps) and alpha-crystallins enables us to reassess the phylogeny of this ubiquitous protein family. While the prokaryotic and fungal representatives are not properly resolved, most of the plant and animal shsps and related proteins are clearly grouped in distinct clades, reflecting a history of repeated gene duplications. The members of the shsp family are characterized by the presence of a conserved homologous "alpha-crystallin domain," which sometimes is present in duplicate. Predictions are made of secondary structure and solvent accessibility of this domain, which together with hydropathy profiles and intron positions support the presence of two similar hydrophobic beta-sheet-rich motifs, connected by a hydrophilic alpha-helical region. Together with an overview of the newly characterized members of the shsp family, these data help to define this family as being involved as stable structural proteins and as molecular chaperones during normal development and induced under pathological and stressful conditions.
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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.