ArticleScientific reports2016
Multiple oligomeric structures of a bacterial small heat shock protein.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 38 citations in OpenAlex.
- Mechanism of small heat shock protein client sequestration and induced polydispersity.Nature communications · 2025Article
- Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles.International journal of molecular sciences · 2025Review
- Article
- Minimal Yet Powerful: The Role of Archaeal Small Heat Shock Proteins in Maintaining Protein Homeostasis.Frontiers in molecular biosciences · 2022Review
- The Small Ones Matter-sHsps in the Bacterial Chaperone Network.Frontiers in molecular biosciences · 2021Review
- Genome-wide screens identify Toxoplasma gondii determinants of parasite fitness in IFNγ-activated murine macrophages.Nature communications · 2020Article
- Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.International journal of molecular sciences · 2020Review
- Crystal structures of the naturally fused CS and cytochrome bActa crystallographica. Section D, Structural biology · 2019Article
- Small heat shock proteins: Simplicity meets complexity.The Journal of biological chemistry · 2019Review
- It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate.The Journal of biological chemistry · 2018Article
- Terminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3.Journal of molecular biology · 2018Article
- Oligomerization and chaperone-like activity of Drosophila melanogaster small heat shock protein DmHsp27 and three arginine mutants in the alpha-crystallin domain.Cell stress & chaperones · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small heat shock proteins are ubiquitous molecular chaperones that form the first line of defence against the detrimental effects of cellular stress. Under conditions of stress they undergo drastic conformational rearrangements in order to bind to misfolded substrate proteins and prevent cellular protein aggregation. Owing to the dynamic nature of small heat shock protein oligomers, elucidating the structural basis of chaperone action and oligomerization still remains a challenge. In order to understand the organization of sHSP oligomers, we have determined crystal structures of a small heat shock protein from Salmonella typhimurium in a dimeric form and two higher oligomeric forms: an 18-mer and a 24-mer. Though the core dimer structure is conserved in all the forms, structural heterogeneity arises due to variation in the terminal regions.
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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.