Evidence map›Paper›PMID 27626823›Full record

ArticleAnalytical chemistry2016

A High-Throughput Targeted Proteomic Approach for Comprehensive Profiling of Methylglyoxal-Induced Perturbations of the Human Kinome.

Weili Miao, Yongsheng Xiao, Lei Guo, Xiaogang Jiang, Ming Huang, Yinsheng Wang

Abstract read
In one paragraph

Article in Analytical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Proteome-Wide Characterizations ofAnalytical chemistry · 2021
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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.

Weili MiaoDepartment of Chemistry, and ‡Environmental Toxicology Graduate Program, University of California , Riverside, California 92521-0403, United States.
Yongsheng XiaoDepartment of Chemistry, and ‡Environmental Toxicology Graduate Program, University of California , Riverside, California 92521-0403, United States.
Lei GuoDepartment of Chemistry, and ‡Environmental Toxicology Graduate Program, University of California , Riverside, California 92521-0403, United States.
Xiaogang JiangDepartment of Chemistry, and ‡Environmental Toxicology Graduate Program, University of California , Riverside, California 92521-0403, United States.
Ming HuangDepartment of Chemistry, and ‡Environmental Toxicology Graduate Program, University of California , Riverside, California 92521-0403, United States.
Yinsheng WangDepartment of Chemistry, and ‡Environmental Toxicology Graduate Program, University of California , Riverside, California 92521-0403, United States.
University of California, Riverside · US

Funding

Chemistry and Biology of DNA CarboxyalkylationR01DK082779 · NIDDK · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI WANG, YINSHENG · 2009 to 2016
$3.0M
NIDDK NIH HHS R01 DK082779
6 · The paper itself

Abstract

Kinases are one of the most important families of enzymes that are involved in numerous cell signaling processes. Existing methods for studying kinase expression and activation have limited kinome coverage. Herein we established a multiple-reaction monitoring (MRM)-based targeted proteomic method that provided an unprecedented coverage (∼80%) of the human kinome. We employed this method for profiling comprehensively the alterations of the global kinome of HEK293T human embryonic kidney cells upon treatment with methylglyoxal, a glycolysis byproduct that is present at elevated levels in blood and tissues of diabetic patients and is thought to contribute to diabetic complications. Our results led to the quantification of 328 unique kinases. In particular, we found that methylglyoxal treatment gave rise to altered expression of a number of kinases in the MAPK pathway and diminished expression of several receptor tyrosine kinases, including epidermal growth factor receptor (EGFR), insulin growth factor 2 receptor (IGF2R), fibroblast growth factor receptor (FGFR), etc. Furthermore, we demonstrated that the diminished expression of EGFR occurred through a mechanism that is distinct from the reduced expression of IGF2R and FGFR1. Together, our targeted kinome profiling method offers a powerful resource for exploring kinase-mediated signaling pathways that are altered by extracellular stimuli, and the results from the present study suggest new mechanisms underlying the development of diabetic complications.

Indexed as

High-Throughput Screening AssaysProteomicsCells, CulturedGene Expression ProfilingHEK293 CellsHumansMolecular StructurePhosphotransferasesPyruvaldehydeReal-Time Polymerase Chain ReactionPhosphotransferasesPyruvaldehyde

Identifiers

PMID27626823
PMCPMC5050164
OpenAlexW2520929822

What OpenQuestion holds

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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.