Evidence map›Paper›PMID 26938934›Full record

ArticleJournal of proteome research2016

Cleaning out the Litterbox of Proteomic Scientists' Favorite Pet: Optimized Data Analysis Avoiding Trypsin Artifacts.

Matthias Schittmayer, Katarina Fritz, Laura Liesinger, Johannes Griss, Ruth Birner-Gruenberger

Open access · hybridAbstract 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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

11 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. MS Amanda 2.0: Advancements in the standalone implementation.Rapid communications in mass spectrometry : RCM · 2021
    Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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

5 authors at 3 institutions in 1 country.

Matthias SchittmayerResearch Unit Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University of Graz , 8010 Graz, Austria.
Katarina FritzResearch Unit Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University of Graz , 8010 Graz, Austria.
Laura LiesingerResearch Unit Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University of Graz , 8010 Graz, Austria.
Johannes GrissDepartment of Dermatology, Medical University of Vienna , 1090 Vienna, Austria.
Ruth Birner-GruenbergerResearch Unit Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University of Graz , 8010 Graz, Austria.
Medical University of Graz · ATBioTechMed-Graz · ATMedical University of Vienna · AT

Funding

Austrian Science Fund FWF KLI 425Austrian Science Fund FWF W 1226
6 · The paper itself

Abstract

Chemically modified trypsin is a standard reagent in proteomics experiments but is usually not considered in database searches. Modification of trypsin is supposed to protect the protease against autolysis and the resulting loss of activity. Here, we show that modified trypsin is still subject to self-digestion, and, as a result, modified trypsin-derived peptides are present in standard digests. We depict that these peptides commonly lead to false-positive assignments even if native trypsin is considered in the database. Moreover, we present an easily implementable method to include modified trypsin in the database search with a minimal increase in search time and search space while efficiently avoiding these false-positive hits.

Indexed as

ArtifactsData Interpretation, StatisticalAmino Acid SequenceAnimalsBrain ChemistryBreast NeoplasmsCell LineChromatography, LiquidDatabases, ProteinHumansMembrane ProteinsMiceNeoplasm ProteinsNerve Tissue ProteinsPeptide FragmentsProtein Structure, SecondaryMembrane ProteinsNeoplasm ProteinsNerve Tissue ProteinsNumb protein, mousePeptide FragmentsSaccharomyces cerevisiae ProteinsTrypsinautolysis protected trypsindatabase searchfalse positivesmisassigned spectraproteomicssearch space restriction

Identifiers

PMID26938934
PMCPMC4820788
OpenAlexW2290131530

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.