ReviewProtoplasma2012
Chaperone receptors: guiding proteins to intracellular compartments.
Review in Protoplasma, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 34 citations in OpenAlex.
- siRNA-mediated inhibition of NTT-MMP-2 reduces oxidative stress and apoptotic signaling in an ex vivo model of ischemia/reperfusion injury.Scientific reports · 2025Article
- Identification of thePlants (Basel, Switzerland) · 2025Article
- Salt stress proteins in plants: An overview.Frontiers in plant science · 2022Review
- Go your own way: membrane-targeting sequences.Plant physiology · 2021Article
- Lipid Body Dynamics in Shoot Meristems: Production, Enlargement, and Putative Organellar Interactions and Plasmodesmal Targeting.Frontiers in plant science · 2021Article
- Transcriptional analyses of two soybean cultivars under salt stress.Molecular biology reports · 2020Article
- Genetically Modified Heat Shock Protein90s and Polyamine Oxidases inPlants (Basel, Switzerland) · 2019Article
- Multiple PPR protein interactions are involved in the RNA editing system inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- The heat-shock protein/chaperone network and multiple stress resistance.Plant biotechnology journal · 2017Review
- New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.Journal of molecular biology · 2015Review
- A comparative glycoproteome study of developing endosperm in the hexose-deficient miniature1 (mn1) seed mutant and its wild type Mn1 in maize.Frontiers in plant science · 2014Article
- A central role for inducible heat-shock protein 70 in autoimmune vitiligo.Experimental dermatology · 2013Review
- AtTPR7 as part of the Arabidopsis Sec post-translocon.Plant signaling & behavior · 2013Article
- The Bam machine: a molecular cooper.Biochimica et biophysica acta · 2012Review
- A novel intracellular isoform of matrix metalloproteinase-2 induced by oxidative stress activates innate immunity.PloS one · 2012Article
- Chloroplast envelope protein targeting fidelity is independent of cytosolic components in dual organelle assays.Frontiers in plant science · 2012Article
- A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex.The Journal of biological chemistry · 2011Article
- Study of receptor-chaperone interactions using the optical technique of spectroscopic ellipsometry.Biophysical journal · 2011Article
- Heat Shock Protein-70 Expression in Vitiligo and its Relation to the Disease Activity.Indian journal of dermatologyArticle
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 1 institution in 1 country.
Funding
Abstract
Despite mitochondria and chloroplasts having their own genome, 99% of mitochondrial proteins (Rehling et al., Nat Rev Mol Cell Biol 5:519-530, 2004) and more than 95% of chloroplast proteins (Soll, Curr Opin Plant Biol 5:529-535, 2002) are encoded by nuclear DNA, synthesised in the cytosol and imported post-translationally. Protein targeting to these organelles depends on cytosolic targeting factors, which bind to the precursor, and then interact with membrane receptors to deliver the precursor into a translocase. The molecular chaperones Hsp70 and Hsp90 have been widely implicated in protein targeting to mitochondria and chloroplasts, and receptors capable of recognising these chaperones have been identified at the surface of both these organelles (Schlegel et al., Mol Biol Evol 24:2763-2774, 2007). The role of these chaperone receptors is not fully understood, but they have been shown to increase the efficiency of protein targeting (Young et al., Cell 112:41-50, 2003; Qbadou et al., EMBO J 25:1836-1847, 2006). Whether these receptors contribute to the specificity of targeting is less clear. A class of chaperone receptors bearing tetratricopeptide repeat domains is able to specifically bind the highly conserved C terminus of Hsp70 and/or Hsp90. Interestingly, at least of one these chaperone receptors can be found on each organelle (Schlegel et al., Mol Biol Evol 24:2763-2774, 2007), which suggests a universal role in protein targeting for these chaperone receptors. This review will investigate the role that chaperone receptors play in targeting efficiency and specificity, as well as examining recent in silico approaches to find novel chaperone receptors.
Indexed as
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.