Evidence map›Paper›PMID 24736658›Full record

ArticlePloS one2014

Expression of a truncated ATHB17 protein in maize increases ear weight at silking.

Elena A Rice, Abha Khandelwal, Robert A Creelman, Cara Griffith, Jeffrey E Ahrens, J Philip Taylor, Lesley R Murphy, Siva Manjunath, Rebecca L Thompson, Matthew J Lingard and 27 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.2field-weighted citation impact, top 7% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Overexpression ofProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Article
  9. Article
  10. Cross-resistance to dicamba, 2,4-D, and fluroxypyr inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Article
  13. TheeLife · 2016
    Article
  14. Review
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

37 authors at 5 institutions in 2 countries.

Elena A RiceMonsanto Company, St. Louis, Missouri, United States of America.
Abha KhandelwalMonsanto Company, St. Louis, Missouri, United States of America.
Robert A CreelmanMendel Biotechnology Inc., Hayward, California, United States of America.
Cara GriffithMonsanto Company, St. Louis, Missouri, United States of America.
Jeffrey E AhrensMonsanto Company, St. Louis, Missouri, United States of America.
J Philip TaylorMonsanto Company, St. Louis, Missouri, United States of America.
Lesley R MurphyMonsanto Company, St. Louis, Missouri, United States of America.
Siva ManjunathMonsanto Company, St. Louis, Missouri, United States of America.
Rebecca L ThompsonMonsanto Company, St. Louis, Missouri, United States of America.
Matthew J LingardMonsanto Company, St. Louis, Missouri, United States of America.
Stephanie L BackMonsanto Company, St. Louis, Missouri, United States of America.
Huachun LarueMonsanto Company, St. Louis, Missouri, United States of America.
Bonnie R BraytonDupont-Pioneer Hi-Bred International, Waipahu, Hawaii, United States of America.
Amanda J BurekMendel Biotechnology Inc., Hayward, California, United States of America.
Shiv TiwariDupont-Pioneer Hi-Bred International, Hayward, California, United States of America.
Luc AdamABCAM, Burlingame, California, United States of America.
James A MorrellMonsanto Company, St. Louis, Missouri, United States of America.
Rico A CaldoMonsanto Company, St. Louis, Missouri, United States of America.
Qing HuaiMonsanto Company, Cambridge, Massachusetts, United States of America.
Jean-Louis K KouadioMonsanto Company, St. Louis, Missouri, United States of America.
Rosemarie KuehnMonsanto Company, St. Louis, Missouri, United States of America.
Anagha M SantMonsanto Company, St. Louis, Missouri, United States of America.
William J WingbermuehleMonsanto Company, St. Louis, Missouri, United States of America.
Rodrigo SalaMonsanto Company, St. Louis, Missouri, United States of America.
Matt FosterMonsanto Company, St. Louis, Missouri, United States of America.
Josh D KinserMonsanto Company, St. Louis, Missouri, United States of America.
Radha MohantyMonsanto Company, St. Louis, Missouri, United States of America.
Dongming JiangMonsanto Company, St. Louis, Missouri, United States of America.
Todd E ZieglerMonsanto Company, St. Louis, Missouri, United States of America.
Mingya G HuangMonsanto Company, St. Louis, Missouri, United States of America.
Saritha V KuriakoseMonsanto Company, Bangalore, Karnataka, India.
Kyle SkottkeMonsanto Company, St. Louis, Missouri, United States of America.
Peter P RepettiMendel Biotechnology Inc., Hayward, California, United States of America.
T Lynne ReuberMendel Biotechnology Inc., Hayward, California, United States of America.
Thomas G RuffMonsanto Company, St. Louis, Missouri, United States of America.
Marie E PetracekMonsanto Company, St. Louis, Missouri, United States of America.
Paul J LoidaMonsanto Company, St. Louis, Missouri, United States of America.
Monsanto (United States) · USMendel Biotechnology (United States) · USPioneer Hi-Bred · USAbcam (United States) · USMonsanto (India) · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATHB17 (AT2G01430) is an Arabidopsis gene encoding a member of the α-subclass of the homeodomain leucine zipper class II (HD-Zip II) family of transcription factors. The ATHB17 monomer contains four domains common to all class II HD-Zip proteins: a putative repression domain adjacent to a homeodomain, leucine zipper, and carboxy terminal domain. However, it also possesses a unique N-terminus not present in other members of the family. In this study we demonstrate that the unique 73 amino acid N-terminus is involved in regulation of cellular localization of ATHB17. The ATHB17 protein is shown to function as a transcriptional repressor and an EAR-like motif is identified within the putative repression domain of ATHB17. Transformation of maize with an ATHB17 expression construct leads to the expression of ATHB17Δ113, a truncated protein lacking the first 113 amino acids which encodes a significant portion of the repression domain. Because ATHB17Δ113 lacks the repression domain, the protein cannot directly affect the transcription of its target genes. ATHB17Δ113 can homodimerize, form heterodimers with maize endogenous HD-Zip II proteins, and bind to target DNA sequences; thus, ATHB17Δ113 may interfere with HD-Zip II mediated transcriptional activity via a dominant negative mechanism. We provide evidence that maize HD-Zip II proteins function as transcriptional repressors and that ATHB17Δ113 relieves this HD-Zip II mediated transcriptional repression activity. Expression of ATHB17Δ113 in maize leads to increased ear size at silking and, therefore, may enhance sink potential. We hypothesize that this phenotype could be a result of modulation of endogenous HD-Zip II pathways in maize.

Indexed as

Active Transport, Cell NucleusAmino Acid MotifsAmino Acid SequenceArabidopsis ProteinsBody WeightCell NucleusConsensus SequenceGene ExpressionMolecular Sequence DataProtein MultimerizationProtein Structure, QuaternaryProtoplastsReproductionSequence DeletionTranscription FactorsTranscription, GeneticArabidopsis ProteinsHB17 protein, ArabidopsisTranscription Factors

Identifiers

PMID24736658
PMCPMC3988052
OpenAlexW2000269766

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.