Evidence map›Paper›PMID 21427533›Full record

ReviewPlant signaling & behavior2011

Chaperones and foldases in endoplasmic reticulum stress signaling in plants.

Dinesh Gupta, Narendra Tuteja

Abstract readReview
In one paragraph

Review in Plant signaling & behavior, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed.

  1. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Dinesh GuptaInternational Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi, India.
Narendra Tuteja

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular chaperones and foldases are a diverse group of proteins that in vivo bind to misfolded or unfolded proteins (non-native or unstable proteins) and play important role in their proper folding. Stress conditions compel altered and heightened chaperone and foldase expression activity in the endoplasmic reticulum (ER), which highlights the role of these proteins, due to which several of the proteins under these classes were identified as heat shock proteins. Different chaperones and foldases are active in different cellular compartment performing specific tasks. The review will discuss the role of the ER chaperones and foldases under stress conditions to maintain proper protein folding dynamics in the plant cells and recent advances in the field. The ER chaperones and foldases, which are described in article, are binding protein (BiP), glucose regulated protein (GRP94), protein-disulfide isomerase (PDI), peptidyl-prolyl isomerases (PPI), immunophilins, calnexin and calreticulin.

Indexed as

Signal TransductionStress, PhysiologicalEndoplasmic ReticulumHSP70 Heat-Shock ProteinsMembrane ProteinsMolecular ChaperonesPeptidylprolyl IsomerasePlant ProteinsPlantsProtein Disulfide-Isomerasesglucose-regulated proteinsHSP70 Heat-Shock ProteinsMembrane ProteinsMolecular ChaperonesPeptidylprolyl IsomerasePlant ProteinsProtein Disulfide-Isomerases

Identifiers

PMID21427533
PMCPMC3121983

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.