Evidence map›Paper›PMID 32338005›Full record

ArticleJournal of proteome research2020

Crystal-C: A Computational Tool for Refinement of Open Search Results.

Hui-Yin Chang, Andy T Kong, Felipe da Veiga Leprevost, Dmitry M Avtonomov, Sarah E Haynes, Alexey I Nesvizhskii

Abstract read
In one paragraph

Article in Journal of proteome research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

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  6. A transcriptomic, proteomic, and functional genetic atlas dissects neurofibromin function in the peripheral nervous system.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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.

Hui-Yin ChangDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.ORCID 0000-0003-1767-1874
Andy T KongDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.
Felipe da Veiga LeprevostDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.
Dmitry M AvtonomovDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.
Sarah E HaynesDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.
Alexey I NesvizhskiiDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.

Funding

COMPUTATIONAL TOOLS FOR MASS SPECTROMETRY-BASED INTERACTOME DATAR01GM094231 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Alexey I Nesvizhskii · 2010 to 2026
$5.4M
Michigan Compound Identification Development Cores (MCIDC)U2CES030164 · NIEHS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NESVIZHSKII, ALEXEY I · 2018 to 2021
$4.1M
University of Michigan Proteogenomics Data Analysis CenterU24CA210967 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHINNAIYAN, ARUL M, DHANASEKARAN, SARAVANA M · 2016 to 2020
$4.1M
NCI NIH HHS U24 CA210967NIEHS NIH HHS U2C ES030164NIGMS NIH HHS R01 GM094231
6 · The paper itself

Abstract

Shotgun proteomics using liquid chromatography coupled to mass spectrometry (LC-MS) is commonly used to identify peptides containing post-translational modifications. With the emergence of fast database search tools such as MSFragger, the approach of enlarging precursor mass tolerances during the search (termed "open search") has been increasingly used for comprehensive characterization of post-translational and chemical modifications of protein samples. However, not all mass shifts detected using the open search strategy represent true modifications, as artifacts exist from sources such as unaccounted missed cleavages or peptide co-fragmentation (chimeric MS/MS spectra). Here, we present Crystal-C, a computational tool that detects and removes such artifacts from open search results. Our analysis using Crystal-C shows that, in a typical shotgun proteomics data set, the number of such observations is relatively small. Nevertheless, removing these artifacts helps to simplify the interpretation of the mass shift histograms, which in turn should improve the ability of open search-based tools to detect potentially interesting mass shifts for follow-up investigation.

Indexed as

ProteomicsTandem Mass SpectrometryDatabases, ProteinPeptidesProtein Processing, Post-TranslationalPeptidesLC-MSliquid chromatography coupled to mass spectrometryopen searchpeptide identificationpost-translational modifications

Identifiers

PMID32338005
PMCPMC7460724

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.