Evidence map›Paper›PMID 27291504›Full record

ArticleJournal of proteome research2016

Characterization of Proteoforms with Unknown Post-translational Modifications Using the MIScore.

Qiang Kou, Binhai Zhu, Si Wu, Charles Ansong, Nikola Tolić, Ljiljana Paša-Tolić, Xiaowen Liu

Abstract read
In one paragraph

Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  3. Article
  4. Article
  5. TopMSV: A Web-Based Tool for Top-Down Mass Spectrometry Data Visualization.Journal of the American Society for Mass Spectrometry · 2021
    Article
  6. Article
  7. Article
  8. TopPIC Gateway: A Web Gateway for Top-Down Mass Spectrometry Data Interpretation.PEARC20 : Practice and Experience in Advanced Research Computing 2020 : Catch the wave : July 27-31, 2020, Portland, Or Virtual Conference. Practice and Experience in Advanced Research Computing (Conference) (2020 : Online) · 2020
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Top-Down Proteomics: Ready for Prime Time?Analytical chemistry · 2018
    Review
  15. 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

7 authors at 5 institutions in 1 country.

Qiang KouDepartment of BioHealth Informatics, Indiana University-Purdue University Indianapolis , Indianapolis, Indiana 46202, United States.
Binhai ZhuDepartment of Computer Science, Montana State University , Bozeman, Montana 59717, United States.
Si WuDepartment of Chemistry and Biochemistry, Univeristy of Oklahoma , Norman, Oklahoma 73019-5251, United States.
Charles Ansong
Nikola Tolić
Ljiljana Paša-Tolić
Xiaowen LiuDepartment of BioHealth Informatics, Indiana University-Purdue University Indianapolis , Indianapolis, Indiana 46202, United States.
Indiana University School of MedicineIndiana University – Purdue University Indianapolis · USMontana State University · USPacific Northwest National Laboratory · USUniversity of Oklahoma · US

Funding

Computational tools for top down mass spectrometry based proteoform identification and proteogenomicsR01GM118470 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI Xiaowen Liu · 2016 to 2026
$2.7M
NIGMS NIH HHS R01 GM118470
6 · The paper itself

Abstract

Various proteoforms may be generated from a single gene due to primary structure alterations (PSAs) such as genetic variations, alternative splicing, and post-translational modifications (PTMs). Top-down mass spectrometry is capable of analyzing intact proteins and identifying patterns of multiple PSAs, making it the method of choice for studying complex proteoforms. In top-down proteomics, proteoform identification is often performed by searching tandem mass spectra against a protein sequence database that contains only one reference protein sequence for each gene or transcript variant in a proteome. Because of the incompleteness of the protein database, an identified proteoform may contain unknown PSAs compared with the reference sequence. Proteoform characterization is to identify and localize PSAs in a proteoform. Although many software tools have been proposed for proteoform identification by top-down mass spectrometry, the characterization of proteoforms in identified proteoform-spectrum matches still relies mainly on manual annotation. We propose to use the Modification Identification Score (MIScore), which is based on Bayesian models, to automatically identify and localize PTMs in proteoforms. Experiments showed that the MIScore is accurate in identifying and localizing one or two modifications.

Indexed as

Protein Processing, Post-TranslationalBayes TheoremEscherichia coliProteomeProteomicsSalmonella typhimuriumSoftwareTandem Mass SpectrometryProteomepost-translational modificationproteoform

Identifiers

PMID27291504
PMCPMC5359983
OpenAlexW2424385274

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.