ArticlePlant physiology1994
A Low Molecular Mass Heat-Shock Protein Is Localized to Higher Plant Mitochondria.
Article in Plant physiology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 68 citations in OpenAlex.
- Mitochondrial Kinases and the Role of Mitochondrial Protein Phosphorylation in Health and Disease.Life (Basel, Switzerland) · 2021Review
- Mitochondria-Targeted SmsHSP24.1 Overexpression Stimulates Early Seedling Vigor and Stress Tolerance by Multi-Pathway Transcriptome-Reprogramming.Frontiers in plant science · 2021Article
- The Mitochondrial Small Heat Shock Protein HSP22 from Pea is a Thermosoluble Chaperone Prone to Co-Precipitate with Unfolding Client Proteins.International journal of molecular sciences · 2019Article
- Algae sense exact temperatures: small heat shock proteins are expressed at the survival threshold temperature in Cyanidioschyzon merolae and Chlamydomonas reinhardtii.Genome biology and evolution · 2014Article
- A low molecular weight proteome comparison of fertile and male sterile 8 anthers of Zea mays.Plant biotechnology journal · 2012Article
- Non-redundant functions of sHSP-CIs in acquired thermotolerance and their role in early seed development in Arabidopsis.Plant molecular biology · 2008Article
- Comparative analysis of the small heat shock proteins in three angiosperm genomes identifies new subfamilies and reveals diverse evolutionary patterns.Cell stress & chaperones · 2008Article
- Pea seed mitochondria are endowed with a remarkable tolerance to extreme physiological temperatures.Plant physiology · 2006Article
- Accumulation of small heat-shock protein homologs in the endoplasmic reticulum of cortical parenchyma cells in mulberry in association with seasonal cold acclimation.Plant physiology · 1999Article
- Heat-stress response of maize mitochondria.Plant physiology · 1998Article
- Tissue-Type-Specific Heat-Shock Response and Immunolocalization of Class I Low-Molecular-Weight Heat-Shock Proteins in Soybean.Plant physiology · 1997Article
- The 23-kDa light-stress-regulated heat-shock protein of chenopodium rubrum L. is located in the mitochondria.Planta · 1997Article
- Molecular chaperones and protein folding in plants.Plant molecular biology · 1996Review
- Post-termination-induced and hormonally dependent expression of low-molecular-weight heat shock protein genes in Douglas fir.Plant molecular biology · 1996Article
- Article
- Article
- Molecular characterization of cDNAs encoding low-molecular-weight heat shock proteins of soybean.Plant molecular biology · 1996Article
- Sequence and expression of the mRNA encoding HSP22, the mitochondrial small heat-shock protein in pea leaves.The Biochemical journal · 1995Article
- Estimating substitution rates in ribosomal RNA genes.Genetics · 1995Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
When pea (Pisum sativum L. var Douce Provence) plants are shifted from a normal growth temperature of 25[deg] C up to 40[deg] C for 3 h, a novel 22-kD protein is produced and accumulates in the matrix compartment of green leaf mitochondria. HSP22 was purified and used as antigen to prepare guinea pig antiserum. The expression of HSP22 was studied using immunodetection methods. HSP22 is a nuclear-encoded protein de novo synthesized in heat-stressed pea plants. The heat-shock response is rapid and can be detected as early as 30 min after the temperature is raised. On the other hand, HSP22 declines very slowly after pea leaves have been transferred back to 25[deg] C. After 100 h at 25[deg] C, the heat-shock pattern was undetectable. The precise localization of HSP22 was investigated and we demonstrated that HSP22 was found only in mitochondria, where it represents 1 to 2% of total matrix proteins. However, the induction of HSP22 does not seem to be tissue specific, since the protein was detected in green or etiolated pea leaves as well as in pea roots. Finally, examination of matrix extracts by nondenaturing polyacrylamide gel electrophoresis and immunoblotting with anti-HSP22 serum revealed a high-molecular mass heat-shock protein complex of 230 kD, which contains HSP22.
Identifiers
What OpenQuestion holds
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.