Evidence map›Paper›PMID 11197326›Full record

ArticlePlant molecular biology2000

Two rice MADS domain proteins interact with OsMADS1.

J Lim, Y H Moon, G An, S K Jang

Abstract read
PubMed Publisher
In one paragraph

Article in Plant molecular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 126 citations in OpenAlex.

  1. A Novel OsMPK6-OsMADS47-PPKL1/3 Module Controls Grain Shape and Yield in Rice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Genome-Wide Analysis of theInternational journal of molecular sciences · 2023
    Article
  7. Article
  8. Article
  9. The ABC of Flower Development in Monocots: The Model of Rice Spikelet.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Article
  11. Article
  12. Comprehensive Analysis of FiveInternational journal of molecular sciences · 2021
    Article
  13. Article
  14. Article
  15. Conserved DNA-derived polymorphism, new markers for genetic diversity analysis of TunisianPhysiology and molecular biology of plants : an international journal of functional plant biology · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Genetic control of flowering time in rice: integration of Mendelian genetics and genomics.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2016
    Review
  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

4 authors at 1 institution in 1 country.

J LimDepartment of Life Science, Pohang University of Science and Technology, Kyunghuk, Korea.
Y H Moon
G An
S K Jang
Pohang University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

OsMADS1 is a MADS box gene controlling flower development in rice. In order to learn more about the function of OsMADS1, we searched for cellular proteins interacting with OsMADS1 employing the yeast two-hybrid system. Two novel proteins with MADS domains, which were named OsMADS14 and OsMADS15, were isolated from a rice cDNA library. OsMADS14 and -15 are highly homologous to the maize MADS box gene ZAP1 which is an orthologue of the floral homeotic gene APETALA1 (AP1). Interactions among the three MADS domain proteins were confirmed by in vitro experiments using GST-fused OsMADS1 expressed in Escherichia coli and in vitro translated proteins of OsMADS14 and -15. We determined which domains in OsMADS1, -14, and -15 were required for protein-protein interaction employing the two-hybrid system and pull-down experiments. While the K domain was essential for protein-protein interaction, a region preceded by the K domain augmented this interaction. Interestingly, the C-terminal region of OsMADS1 functioned as a transcriptional activation domain in yeast and mammalian cells, while, on the other hand, the C domains of OsMADS14 and -15 exhibited only very weak transcriptional activator functionality, if any at all.

Indexed as

Amino Acid SequenceBase SequenceBinding SitesDNA-Binding ProteinsDNA, PlantGenes, PlantMADS Domain ProteinsMolecular Sequence DataOryzaPlant ProteinsProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSequence Homology, Amino AcidTrans-ActivatorsTranscriptional ActivationDNA-Binding ProteinsDNA, PlantMADS Domain ProteinsPlant ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID11197326
OpenAlexW1735783583

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.