Evidence map›Paper›PMID 19664994›Full record

ArticleCell stem cell2009

Phosphoproteomic analysis of human embryonic stem cells.

Laurence M Brill, Wen Xiong, Ki-Bum Lee, Scott B Ficarro, Andrew Crain, Yue Xu, Alexey Terskikh, Evan Y Snyder, Sheng Ding

Open access · bronzeAbstract read
In one paragraph

Article in Cell stem cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed, 1 pooled it
12.4field-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

105 citing papers in PubMed, 1 synthesis or guideline pooled it, 189 citations in OpenAlex.

  1. Identification of IDUA and WNT16 Phosphorylation-Related Non-Synonymous Polymorphisms for Bone Mineral Density in Meta-Analyses of Genome-Wide Association Studies.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2016
    Pooled it
  2. Article
  3. Review
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  5. Article
  6. Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism.International journal of molecular sciences · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
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  15. JNK Signaling in Stem Cell Self-Renewal and Differentiation.International journal of molecular sciences · 2020
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. OncogenicProceedings of the National Academy of Sciences of the United States of America · 2019
    Article

45 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Laurence M BrillGenomics Institute of the Novartis Research Foundation, San Diego, CA 92109, USA. lbrill@burnham.org
Wen Xiong
Ki-Bum Lee
Scott B Ficarro
Andrew Crain
Yue Xu
Alexey Terskikh
Evan Y Snyder
Sheng Ding
Scripps Research Institute · USSanford Burnham Prebys Medical Discovery Institute · USGenomics Institute of the Novartis Research Foundation · US

Funding

The Stem Cell Center at The Burnham InstituteP20GM075059 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI SNYDER, EVAN YALE · 2005 to 2007
$3.0M
NIGMS NIH HHS 1 P20 GM 075059-01NIGMS NIH HHS P20 GM075059
6 · The paper itself

Abstract

Protein phosphorylation, while critical to cellular behavior, has been undercharacterized in pluripotent cells. Therefore, we performed phosphoproteomic analyses of human embryonic stem cells (hESCs) and their differentiated derivatives. A total of 2546 phosphorylation sites were identified on 1602 phosphoproteins; 389 proteins contained more phosphorylation site identifications in undifferentiated hESCs, whereas 540 contained more such identifications in differentiated derivatives. Phosphoproteins in receptor tyrosine kinase (RTK) signaling pathways were numerous in undifferentiated hESCs. Cellular assays corroborated this observation by showing that multiple RTKs cooperatively supported undifferentiated hESCs. In addition to bFGF, EGFR, VEGFR, and PDGFR activation was critical to the undifferentiated state of hESCs. PDGF-AA complemented a subthreshold bFGF concentration to maintain undifferentiated hESCs. Also consistent with phosphoproteomics, JNK activity participated in maintenance of undifferentiated hESCs. These results support the utility of phosphoproteomic data, provide guidance for investigating protein function in hESCs, and complement transcriptomics/epigenetics for broadening our understanding of hESC fate determination.

Indexed as

Embryonic Stem CellsHumansIntercellular Signaling Peptides and ProteinsPhosphoproteinsPhosphorylationProtein KinasesProteomeProteomicsSignal TransductionIntercellular Signaling Peptides and ProteinsPhosphoproteinsProtein KinasesProteome

Identifiers

PMID19664994
PMCPMC2726933
OpenAlexW2035415099

What OpenQuestion holds

Textmetadata
LicenceTDM
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.