Evidence map›Paper›PMID 24614601›Full record

ReviewPlant signaling & behavior2014

Emerging features of ER resident J-proteins in plants.

Masaru Ohta, Fumio Takaiwa

Open access · bronzeAbstract readReview
In one paragraph

Review in Plant signaling & behavior, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 23% of its field
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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. Linking redox and calcium signaling via thioredoxins.Journal of experimental botany · 2026
    Review
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  13. The expanding world of plant J-domain proteins.Critical reviews in plant sciences · 2019
    Article
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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 at 1 institution in 1 country.

Masaru OhtaFunctional Transgenic Crops Research Unit; Genetically Modified Organism Research Center; National Institute of Agrobiological Sciences; Tsukuba, Ibaraki, Japan.
Fumio TakaiwaFunctional Transgenic Crops Research Unit; Genetically Modified Organism Research Center; National Institute of Agrobiological Sciences; Tsukuba, Ibaraki, Japan.
Institute of Agrobiological Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

J-proteins are co-chaperone components of the HSP70 system. J-proteins stimulate Hsp70ATPase activity, which is responsible for stabilizing the interaction of Hsp70 with client proteins. J-proteins are localized in various intracellular compartments including the cytoplasm, mitochondria and endoplasmic reticulum (ER). Five types of ER resident J-proteins (ERdjs) have been found in plants (P58, ERdj2, ERdj2A, ERdj3B and ERdj7). Rice OsERdj3A is located in the vacuoleand protein storage vacuoles (PSV, PB-II) under conditions of ER stress. J-proteins that are localized to the vacuole or lysosome are not found in mammals and yeast, suggesting that the presence of OsERdj3A in the vacuole is plant-specific and one of the features unique to plant ERdjs. In this review, we summarize the current state of knowledge andrecent research advancements regarding plant ERdjs, and compare mammalian and yeast ERdjs with plant ERdjs.

Indexed as

AnimalsEndoplasmic ReticulumHSP40 Heat-Shock ProteinsOryzaPlant ProteinsHSP40 Heat-Shock ProteinsPlant ProteinsBiPendoplasmic reticulumHsp70J-proteinrice seedvacuole

Identifiers

PMID24614601
PMCPMC4091193
OpenAlexW1999274699

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.