Evidence map›Paper›PMID 19109415›Full record

ArticlePlant physiology2009

A rice kinase-protein interaction map.

Xiaodong Ding, Todd Richter, Mei Chen, Hiroaki Fujii, Young Su Seo, Mingtang Xie, Xianwu Zheng, Siddhartha Kanrar, Rebecca A Stevenson, Christopher Dardick and 15 more

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

61 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Update on the Roles of Rice MAPK Cascades.International journal of molecular sciences · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. A massively parallel barcoded sequencing pipeline enables generation of the first ORFeome and interactome map for rice.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Regulation ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

1 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

25 authors at 9 institutions in 2 countries.

Xiaodong DingDepartment of Plant Pathology , University of Florida, Gainesville, Florida 32611, USA.
Todd Richter
Mei Chen
Hiroaki Fujii
Young Su Seo
Mingtang Xie
Xianwu Zheng
Siddhartha Kanrar
Rebecca A Stevenson
Christopher Dardick
Ying Li
Hao Jiang
Yan Zhang
Fahong Yu
Laura E Bartley
Mawsheng Chern
Rebecca Bart
Xiuhua Chen
Lihuang Zhu
William G Farmerie
Michael Gribskov
Jian-Kang Zhu
Michael E Fromm
Pamela C Ronald
Wen-Yuan Song
Institute of Genetics and Developmental Biology · CNUniversity of Nebraska–Lincoln · USChinese Academy of Sciences · CNPurdue University West Lafayette · USUnited States Department of Agriculture · USAppalachian Fruit Research Laboratory · USUniversity of California, Davis · USUniversity of California, Riverside · USUniversity of Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants uniquely contain large numbers of protein kinases, and for the vast majority of the 1,429 kinases predicted in the rice (Oryza sativa) genome, little is known of their functions. Genetic approaches often fail to produce observable phenotypes; thus, new strategies are needed to delineate kinase function. We previously developed a cost-effective high-throughput yeast two-hybrid system. Using this system, we have generated a protein interaction map of 116 representative rice kinases and 254 of their interacting proteins. Overall, the resulting interaction map supports a large number of known or predicted kinase-protein interactions from both plants and animals and reveals many new functional insights. Notably, we found a potential widespread role for E3 ubiquitin ligases in pathogen defense signaling mediated by receptor-like kinases, particularly by the kinases that may have evolved from recently expanded kinase subfamilies in rice. We anticipate that the data provided here will serve as a foundation for targeted functional studies in rice and other plants. The application of yeast two-hybrid and TAPtag analyses for large-scale plant protein interaction studies is also discussed.

Indexed as

Amino Acid SequenceCasein Kinase IICyclin-Dependent KinasesMitogen-Activated Protein KinasesModels, BiologicalMolecular Sequence DataOryzaPhylogenyPlant ProteinsProtein BindingProtein Interaction MappingProtein KinasesTranscription FactorsTwo-Hybrid System TechniquesUbiquitin-Protein LigasesCasein Kinase IICyclin-Dependent KinasesMitogen-Activated Protein KinasesPlant ProteinsProtein KinasesTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID19109415
PMCPMC2649385
OpenAlexW2166681181

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.