Evidence map›Paper›PMID 15101820›Full record

ArticleThe Biochemical journal2004

The water- and salt-stress-regulated Asr1 (abscisic acid stress ripening) gene encodes a zinc-dependent DNA-binding protein.

Yossi Kalifa, Ayelet Gilad, Zvia Konrad, Michele Zaccai, Pablo A Scolnik, Dudy Bar-Zvi

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
7.2field-weighted citation impact, top 3% 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

56 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. ASR gene family: a case of tandem-drive evolution.Frontiers in molecular biosciences · 2025
    Article
  3. Article
  4. Genome-Wide Identification of the PeanutInternational journal of molecular sciences · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Grape ASR Regulates Glucose Transport, Metabolism and Signaling.International journal of molecular sciences · 2022
    Article
  10. Article
  11. Article
  12. International journal of molecular sciences · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017
    Review
  17. Article
  18. Article
  19. Article
  20. Article
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

6 authors at 1 institution in 1 country.

Yossi KalifaDepartment of Life Sciences and The Doris and Bertie Black Center for Bioenergetics in Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.
Ayelet Gilad
Zvia Konrad
Michele Zaccai
Pablo A Scolnik
Dudy Bar-Zvi
Ben-Gurion University of the Negev · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tomato (Lycopersicon esculantum) ASR1 (abscisic acid stress ripening protein), a small plant-specific protein whose cellular mode of action defies deduction based on its sequence or homology analyses, is one of numerous plant gene products with unknown biological roles that become over-expressed under water- and salt-stress conditions. Steady-state cellular levels of tomato ASR1 mRNA and protein are transiently increased following exposure of plants to poly(ethylene glycol), NaCl or abscisic acid. Western blot and indirect immunofluorescence analysis with anti-ASR1 antibodies demonstrated that ASR1 is present both in the cytoplasmic and nuclear subcellular compartments; approx. one-third of the total ASR1 protein could be detected in the nucleus. Nuclear ASR1 is a chromatin-bound protein, and can be extracted with 1 M NaCl, but not with 0.5% Triton X-100. ASR1, overexpressed in Escherichia coli and purified to homogeneity, possesses zinc-dependent DNA-binding activity. Competitive-binding experiments and SELEX (systematic evolution of ligands by exponential enrichment) analysis suggest that ASR1 binds at a preferred DNA sequence.

Indexed as

Binding SitesCell FractionationDNA-Binding ProteinsDNA, PlantGene Expression Regulation, PlantPlant ProteinsSodium ChlorideSolanum lycopersicumSubcellular FractionsWaterZinc FingersAsr1 protein, Lycopersicon esculentumDNA-Binding ProteinsDNA, PlantPlant ProteinsSodium ChlorideWater

Identifiers

PMID15101820
PMCPMC1133842
OpenAlexW2034898802

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.