ArticleThe Journal of biological chemistry2019
The N terminus of the small heat shock protein HSPB7 drives its polyQ aggregation-suppressing activity.
Article 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 12 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
12 citing papers in PubMed, 19 citations in OpenAlex.
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- Impact of N-terminal domain on the sHSP Lo18 function.Scientific reports · 2025Article
- The Role of Small Heat Shock Proteins in Protein Misfolding Associated Motoneuron Diseases.International journal of molecular sciences · 2022Review
- Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.Frontiers in molecular biosciences · 2022Review
- Genome-wide analysis of HSP20 gene family and expression patterns under heat stress in cucumber (Frontiers in plant science · 2022Article
- Quaternary Structure and Hetero-Oligomerization of Recombinant Human Small Heat Shock Protein HspB7 (cvHsp).International journal of molecular sciences · 2021Article
- FOXO1 controls protein synthesis and transcript abundance of mutant polyglutamine proteins, preventing protein aggregation.Human molecular genetics · 2021Article
- Structural basis of substrate recognition and thermal protection by a small heat shock protein.Nature communications · 2021Article
- HSPB7 regulates osteogenic differentiation of human adipose derived stem cells via ERK signaling pathway.Stem cell research & therapy · 2020Article
- Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.International journal of molecular sciences · 2020Review
- Structural aspects of the human small heat shock proteins related to their functional activities.Cell stress & chaperones · 2020Review
- Pathogenesis of SCA3 and implications for other polyglutamine diseases.Neurobiology of disease · 2020Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat shock protein family B (small) member 7 (HSPB7) is a unique, relatively unexplored member within the family of human small heat shock proteins (HSPBs). Unlike most HSPB family members, HSPB7 does not oligomerize and so far has not been shown to associate with any other member of the HSPB family. Intriguingly, it was found to be the most potent member within the HSPB family to prevent aggregation of proteins with expanded polyglutamine (polyQ) stretches. How HSPB7 suppresses polyQ aggregation has remained elusive so far. Here, using several experimental strategies, including
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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.