Evidence map›Paper›PMID 23001859›Full record

ArticleMolecular & cellular proteomics : MCP2013

N-terminal protein processing: a comparative proteogenomic analysis.

Stefano Bonissone, Nitin Gupta, Margaret Romine, Ralph A Bradshaw, Pavel A Pevzner

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Probing Proteoform Heterogeneity From Single Human Oocytes.Molecular & cellular proteomics : MCP · 2026
    Article
  3. Article
  4. Principles ofbioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. An Enigma of N-termini dependent protein degradation.Biochemistry and biophysics reports · 2025
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  7. Article
  8. InPathogens (Basel, Switzerland) · 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

5 authors at 3 institutions in 1 country.

Stefano BonissoneBioinformatics Program, University of California San Diego, La Jolla, California, USA. sbonisso@ucsd.edu
Nitin Gupta
Margaret Romine
Ralph A Bradshaw
Pavel A Pevzner
University of California, San Diego · USPacific Northwest National Laboratory · USUniversity of California, San Francisco · US

Funding

Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
CENTER FOR COMPUTATIONAL MASS-SPECTROMETRYP41RR024851 · NCRR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PEVZNER, PAVEL A · 2008 to 2011
$5.2M
NCRR NIH HHS P41 RR024851NCRR NIH HHS P-41-RR24851NIGMS NIH HHS 8 P41 GM103481NIGMS NIH HHS P41 GM103481
6 · The paper itself

Abstract

N-terminal methionine excision (NME) and N-terminal acetylation (NTA) are two of the most common protein post-translational modifications. NME is a universally conserved activity and a highly specific mechanism across all life forms. NTA is very common in eukaryotes but occurs rarely in prokaryotes. By analyzing data sets from yeast, mammals and bacteria (including 112 million spectra from 57 bacterial species), the largest comparative proteogenomics study to date, it is shown that previous assumptions/perceptions about the specificity and purposes of NME are not entirely correct. Although NME, through the universal enzymatic specificity of the methionine aminopeptidases, results in the removal of the initiator Met in proteins when the second residue is Gly, Ala, Ser, Cys, Thr, Pro, or Val, the comparative genomic analyses suggest that this specificity may vary modestly in some organisms. In addition, the functional role of NME may be primarily to expose Ala and Ser rather than all seven of these residues. Although any of this group provide "stabilizing" N termini in the N-end rule, and de facto leave the remaining 13 amino acid types that are classed as "destabilizing" (in higher eukaryotes) protected by the initiator Met, the conservation of NME-substrate proteins through evolution suggests that the other five are not crucially important for proteins with these residues in the second position. They are apparently merely inconsequential players (their function is not affected by NME) that become exposed because their side chains are smaller or comparable to those of Ala and Ser. The importance of exposing mainly two amino acids at the N terminus, i.e. Ala and Ser, is unclear but may be related to NTA or other post-translational modifications. In this regard, these analyses also reveal that NTA is more prevalent in some prokaryotes than previously appreciated.

Indexed as

Protein Processing, Post-TranslationalAcetylationAmino AcidsAmino Acid SequenceBacteriaGenomicsMass SpectrometryMethionyl AminopeptidasesProteomicsAmino AcidsMethionyl Aminopeptidases

Identifiers

PMID23001859
PMCPMC3536895
OpenAlexW2169471791

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.