Evidence map›Paper›PMID 28894154›Full record

ArticleScientific reports2017

N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen.

Iain J Berry, Veronica M Jarocki, Jessica L Tacchi, Benjamin B A Raymond, Michael Widjaja, Matthew P Padula, Steven P Djordjevic

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

25 citing papers in PubMed, 36 citations in OpenAlex.

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  10. TheFrontiers in microbiology · 2022
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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

7 authors at 1 institution in 1 country.

Iain J BerryThe ithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia.ORCID 0000-0002-0322-2595
Veronica M JarockiThe ithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia.
Jessica L TacchiThe ithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia.
Benjamin B A RaymondThe ithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia.
Michael WidjajaThe ithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia.
Matthew P PadulaThe ithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia.
Steven P DjordjevicThe ithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia. Steven.Djordjevic@uts.edu.au.
University of Technology Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteolytic processing alters protein function. Here we present the first systems-wide analysis of endoproteolysis in the genome-reduced pathogen Mycoplasma hyopneumoniae. 669 N-terminal peptides from 164 proteins were identified, demonstrating that functionally diverse proteins are processed, more than half of which 75 (53%) were accessible on the cell surface. Multiple cleavage sites were characterised, but cleavage with arginine in P1 predominated. Putative functions for a subset of cleaved fragments were assigned by affinity chromatography using heparin, actin, plasminogen and fibronectin as bait. Binding affinity was correlated with the number of cleavages in a protein, indicating that novel binding motifs are exposed, and protein disorder increases, after a cleavage event. Glyceraldehyde 3-phosphate dehydrogenase was used as a model protein to demonstrate this. We define the rules governing methionine excision, show that several aminopeptidases are involved, and propose that through processing, genome-reduced organisms can expand protein function.

Indexed as

ProteomeProteomicsAminopeptidasesBacterial ProteinsBiotinylationChromatography, LiquidComputational BiologyMethionineProteolysisTandem Mass SpectrometryAminopeptidasesBacterial ProteinsMethionineProteome

Identifiers

PMID28894154
PMCPMC5593965
OpenAlexW2751849381

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.