ReviewPlant molecular biology1996
Molecular chaperones and protein folding in plants.
Review in Plant molecular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 169 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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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
169 citing papers in PubMed, 605 citations in OpenAlex.
- Rational gene stacking for seed-specific carbon partitioning to simultaneously enhance lipid and protein contents in Arabidopsis.Journal of experimental botany · 2026Article
- Heat stress triggers enhanced nuclear localization of HYPONASTIC LEAVES 1 to regulate microRNA biogenesis and thermotolerance in plants.The Plant cell · 2025Article
- Genome-Wide Identification and Evolution-Profiling Analysis ofInternational journal of molecular sciences · 2025Article
- The Effect of Heat Stress on Wheat Flag Leaves Revealed by Metabolome and Transcriptome Analyses During the Reproductive Stage.International journal of molecular sciences · 2025Article
- Proteomic Analysis of Plants with Binding Immunoglobulin Protein Overexpression Reveals Mechanisms Related to Defense AgainstPlants (Basel, Switzerland) · 2025Article
- Two sides of the same coin: heat shock proteins as biomarkers and therapeutic targets for some complex diseases.Frontiers in molecular biosciences · 2025Review
- Heat Shock Factor HSFA6b Mediates Mitochondrial Unfolded Protein Response inPlants (Basel, Switzerland) · 2024Article
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- Potentials of single nucleotide polymorphisms and genetic diversity studies at HSP90AB1 gene in Nigerian White Fulani, Muturu, and N'Dama cattle breeds.Tropical animal health and production · 2024Article
- Jasmonate: A Hormone of Primary Importance for Temperature Stress Response in Plants.Plants (Basel, Switzerland) · 2023Review
- Overexpression of AHL proteins enhances root hair production by altering the transcription of RHD6-downstream genes.Plant direct · 2023Article
- Multiomics Reveals the Regulatory Mechanisms of Arabidopsis Tissues under Heat Stress.International journal of molecular sciences · 2023Article
- Genome-wide transcriptional profiling provides clues to molecular mechanisms underlying cold tolerance in chickpea.Scientific reports · 2023Article
- Protective Responses at the Biochemical and Molecular Level Differ between aPlants (Basel, Switzerland) · 2022Article
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- Integrated sRNA-seq and RNA-seq Analyses Reveal a microRNA Regulation Network Involved in Cold Response inGenes · 2022Article
- Near-Isogenic Barley Lines Show Enhanced Susceptibility to Powdery Mildew Infection Following High-Temperature Stress.Plants (Basel, Switzerland) · 2022Article
- Confocal Fluorescence Microscopy Investigation for the Existence of Subdomains within Protein Storage Vacuoles in Soybean Cotyledons.International journal of molecular sciences · 2022Article
- Genome-wide identification and expression analysis of theFrontiers in plant science · 2022Article
- Development ofFrontiers in genetics · 2022Article
109 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
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein folding in vivo is mediated by an array of proteins that act either as 'foldases' or 'molecular chaperones'. Foldases include protein disulfide isomerase and peptidyl prolyl isomerase, which catalyze the rearrangement of disulfide bonds or isomerization of peptide bonds around Pro residues, respectively. Molecular chaperones are a diverse group of proteins, but they share the property that they bind substrate proteins that are in unstable, non-native structural states. The best understood chaperone systems are HSP70/DnaK and HSP60/GroE, but considerable data support a chaperone role for other proteins, including HSP100, HSP90, small HSPs and calnexin. Recent research indicates that many, if not all, cellular proteins interact with chaperones and/or foldases during their lifetime in the cell. Different chaperone and foldase systems are required for synthesis, targeting, maturation and degradation of proteins in all cellular compartments. Thus, these diverse proteins affect an exceptionally broad array of cellular processes required for both normal cell function and survival of stress conditions. This review summarizes our current understanding of how these proteins function in plants, with a major focus on those systems where the most detailed mechanistic data are available, or where features of the chaperone/foldase system or substrate proteins are unique to plants.
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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.