Evidence map›Paper›PMID 18974045›Full record

SynthesisMolecular & cellular proteomics : MCP2009

Predicting protein post-translational modifications using meta-analysis of proteome scale data sets.

Daniel Schwartz, Michael F Chou, George M Church

Abstract readMeta-Analysis
In one paragraph

Synthesis in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
–field-weighted citation impact
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

58 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. The Okur-Chung Neurodevelopmental Syndrome Mutation CK2Frontiers in molecular biosciences · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Quantitative cardiac phosphoproteomics profiling during ischemia-reperfusion in an immature swine model.American journal of physiology. Heart and circulatory physiology · 2017
    Article
  14. Cushing's syndrome mutant PKAFEBS letters · 2017
    Article
  15. Article
  16. Global phosphoproteomic profiling reveals perturbed signaling in a mouse model of dilated cardiomyopathy.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors.

Daniel SchwartzDepartment of Genetics, Harvard Medical School, Boston, MA 02115, USA. dschwartz@genetics.med.harvard.edu
Michael F Chou
George M Church

Funding

THEORETICAL ANALYSIS OF FUNCTIONAL MODULESP50GM068763 · NIGMS · HARVARD UNIVERSITY · PI BENENSON, YAAKOV · 2003 to 2012
$28.9M
RESEARCH TRAINING IN VISUAL NEUROSCIENCET32EY007110 · NEI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BORN, RICHARD T · 1988 to 2023
$4.1M
NEI NIH HHS EY07110-17NEI NIH HHS T32 EY007110NIGMS NIH HHS GM068763NIGMS NIH HHS P50 GM068763
6 · The paper itself

Abstract

Protein post-translational modifications are an important biological regulatory mechanism, and the rate of their discovery using high throughput techniques is rapidly increasingly. To make use of this wealth of sequence data, we introduce a new general strategy designed to predict a variety of post-translational modifications in several organisms. We used the motif-x program to determine phosphorylation motifs in yeast, fly, mouse, and man and lysine acetylation motifs in man. These motifs were then scanned against proteomic sequence data using a newly developed tool called scan-x to globally predict other potential modification sites within these organisms. 10-fold cross-validation was used to determine the sensitivity and minimum specificity for each set of predictions, all of which showed improvement over other available tools for phosphoprediction. New motif discovery is a byproduct of this approach, and the phosphorylation motif analyses provide strong evidence of evolutionary conservation of both known and novel kinase motifs.

Indexed as

Databases, ProteinProtein Processing, Post-TranslationalAcetylationAlgorithmsAmino Acid MotifsAmino Acid SequenceAnimalsDrosophilaHumansMiceMolecular Sequence DataPhosphorylationProteomeReproducibility of ResultsROC CurveSaccharomyces cerevisiaeProteome

Identifiers

PMID18974045
PMCPMC2634583

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.