Evidence map›Paper›PMID 31992638›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Mapping proteome-wide targets of protein kinases in plant stress responses.

Pengcheng Wang, Chuan-Chih Hsu, Yanyan Du, Peipei Zhu, Chunzhao Zhao, Xing Fu, Chunguang Zhang, Juan Sebastian Paez, Alberto P Macho, W Andy Tao and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
26.4field-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

85 citing papers in PubMed, 176 citations in OpenAlex.

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  14. SnRK2s: Kinases or Substrates?Plants (Basel, Switzerland) · 2025
    Review
  15. Genome-Wide Analysis ofInternational journal of molecular sciences · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

25 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

11 authors at 2 institutions in 2 countries.

Pengcheng WangShanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032 Shanghai, China; pcwang@sibs.ac.cn watao@purdue.edu jkzhu@sibs.ac.cn.ORCID 0000-0001-6043-4132
Chuan-Chih HsuDepartment of Biochemistry, Purdue University, West Lafayette, IN 47907.ORCID 0000-0002-7100-1401
Yanyan DuShanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032 Shanghai, China.
Peipei ZhuDepartment of Chemistry, Purdue University, West Lafayette, IN 47907.
Chunzhao ZhaoShanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032 Shanghai, China.
Xing FuShanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032 Shanghai, China.
Chunguang ZhangDepartment of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN 47907.
Juan Sebastian PaezDepartment of Biochemistry, Purdue University, West Lafayette, IN 47907.
Alberto P MachoShanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032 Shanghai, China.ORCID 0000-0001-9935-8026
W Andy TaoDepartment of Biochemistry, Purdue University, West Lafayette, IN 47907; pcwang@sibs.ac.cn watao@purdue.edu jkzhu@sibs.ac.cn.
Jian-Kang ZhuShanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032 Shanghai, China; pcwang@sibs.ac.cn watao@purdue.edu jkzhu@sibs.ac.cn.ORCID 0000-0001-5134-731X
Chinese Academy of Sciences · CNPurdue University West Lafayette · US

Funding

A Proteomic Platform to identify and Validate Biomarkers in Metabolic Syndrome and Coronary Artery DiseaseR01GM111788 · NIGMS · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2015 to 2017
$900k
NIGMS NIH HHS R01 GM111788
6 · The paper itself

Abstract

Protein kinases are major regulatory components in almost all cellular processes in eukaryotic cells. By adding phosphate groups, protein kinases regulate the activity, localization, protein-protein interactions, and other features of their target proteins. It is known that protein kinases are central components in plant responses to environmental stresses such as drought, high salinity, cold, and pathogen attack. However, only a few targets of these protein kinases have been identified. Moreover, how these protein kinases regulate downstream biological processes and mediate stress responses is still largely unknown. In this study, we introduce a strategy based on isotope-labeled in vitro phosphorylation reactions using in vivo phosphorylated peptides as substrate pools and apply this strategy to identify putative substrates of nine protein kinases that function in plant abiotic and biotic stress responses. As a result, we identified more than 5,000 putative target sites of osmotic stress-activated SnRK2.4 and SnRK2.6, abscisic acid-activated protein kinases SnRK2.6 and casein kinase 1-like 2 (CKL2), elicitor-activated protein kinase CDPK11 and MPK6, cold-activated protein kinase MPK6, H

Indexed as

ArabidopsisArabidopsis ProteinsPhosphorylationProtein Interaction MappingProtein Interaction MapsProtein KinasesProteomeStress, PhysiologicalArabidopsis ProteinsProtein KinasesProteomecold stressoxidative stressphosphorylationsalt stresssubstrate

Identifiers

PMID31992638
PMCPMC7022181
OpenAlexW3003348627

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.