Evidence map›Paper›PMID 26442027›Full record

ArticleFrontiers in plant science2015

Differentially expressed seed aging responsive heat shock protein OsHSP18.2 implicates in seed vigor, longevity and improves germination and seedling establishment under abiotic stress.

Harmeet Kaur, Bhanu P Petla, Nitin U Kamble, Ajeet Singh, Venkateswara Rao, Prafull Salvi, Shraboni Ghosh, Manoj Majee

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed, 1 pooled it
15.0field-weighted citation impact, top 1% 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

73 citing papers in PubMed, 1 synthesis or guideline pooled it, 152 citations in OpenAlex.

  1. Pooled it
  2. Natural variation inScience advances · 2026
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  18. Review
  19. Review
  20. A Golden2-like transcription factor regulates Brassica napus seed vigor after artificial aging.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025
    Article

13 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 1 country.

Harmeet KaurNational Institute of Plant Genome Research New Delhi, India.
Bhanu P PetlaNational Institute of Plant Genome Research New Delhi, India.
Nitin U KambleNational Institute of Plant Genome Research New Delhi, India.
Ajeet SinghNational Institute of Plant Genome Research New Delhi, India.
Venkateswara RaoNational Institute of Plant Genome Research New Delhi, India.
Prafull SalviNational Institute of Plant Genome Research New Delhi, India.
Shraboni GhoshNational Institute of Plant Genome Research New Delhi, India.
Manoj MajeeNational Institute of Plant Genome Research New Delhi, India.
National Institute of Plant Genome Research · INGovind Ballabh Pant University of Agriculture and Technology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small heat shock proteins (sHSPs) are a diverse group of proteins and are highly abundant in plant species. Although majority of these sHSPs were shown to express specifically in seed, their potential function in seed physiology remains to be fully explored. Our proteomic analysis revealed that OsHSP18.2, a class II cytosolic HSP is an aging responsive protein as its abundance significantly increased after artificial aging in rice seeds. OsHSP18.2 transcript was found to markedly increase at the late maturation stage being highly abundant in dry seeds and sharply decreased after germination. Our biochemical study clearly demonstrated that OsHSP18.2 forms homooligomeric complex and is dodecameric in nature and functions as a molecular chaperone. OsHSP18.2 displayed chaperone activity as it was effective in preventing thermal inactivation of Citrate Synthase. Further, to analyze the function of this protein in seed physiology, seed specific Arabidopsis overexpression lines for OsHSP18.2 were generated. Our subsequent functional analysis clearly demonstrated that OsHSP18.2 has ability to improve seed vigor and longevity by reducing deleterious ROS accumulation in seeds. In addition, transformed Arabidopsis seeds also displayed better performance in germination and cotyledon emergence under adverse conditions. Collectively, our work demonstrates that OsHSP18.2 is an aging responsive protein which functions as a molecular chaperone and possibly protect and stabilize the cellular proteins from irreversible damage particularly during maturation drying, desiccation and aging in seeds by restricting ROS accumulation and thereby improves seed vigor, longevity and seedling establishment.

Indexed as

CDTchaperoneseed vigorsHSPstress

Identifiers

PMID26442027
PMCPMC4568394
OpenAlexW1958124514

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.