Evidence map›Paper›PMID 30884002›Full record

ArticleRapid communications in mass spectrometry : RCM2019

Identification of N-terminal protein processing sites by chemical labeling mass spectrometry.

Santosh A Misal, Sujun Li, Haixu Tang, Predrag Radivojac, James P Reilly

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Rapid communications in mass spectrometry : RCM, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 54% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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 1 institution in 1 country.

Santosh A MisalDepartment of Chemistry, Indiana University, Bloomington, Indiana, USA.ORCID https://orcid.org/0000-0002-8835-0130
Sujun LiSchool of Informatics, Computing, and Engineering, Indiana University, Bloomington, Indiana, USA.
Haixu TangSchool of Informatics, Computing, and Engineering, Indiana University, Bloomington, Indiana, USA.
Predrag RadivojacSchool of Informatics, Computing, and Engineering, Indiana University, Bloomington, Indiana, USA.
James P ReillyDepartment of Chemistry, Indiana University, Bloomington, Indiana, USA.ORCID https://orcid.org/0000-0002-9784-1804
Indiana University Bloomington · US

Funding

Interactions Regulating Translation and Protein Biogenesis in VivoU54GM105816 · NIGMS · UNIVERSITY OF NOTRE DAME · PI BUSKIRK, ALLEN ROWDON, CLARK, PATRICIA LOUISE · 2013 to 2017
$3.7M
Influence of Translation on Protein FoldingR01GM074807 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CLARK, PATRICIA LOUISE · 2005 to 2014
$2.8M
Computational approaches to protein identification and quantification using MS/MSR01GM103725 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI RADIVOJAC, PREDRAG · 2012 to 2015
$1.7M
NIGMS NIH HHS R01 GM074807NIGMS NIH HHS R01 GM103725NIGMS NIH HHS U54 GM105816NIH HHS U54 GM074807
6 · The paper itself

Abstract

rationaleProteins undergo post-translational modifications and proteolytic processing that can affect their biological function. Processing often involves the loss of single residues. Cleavage of signal peptides from the N-terminus is commonly associated with translocation. Recent reports have suggested that other processing sites also exist.

methodsThe secreted proteins from S. aureus N315 were precipitated with trichloroacetic acid (TCA) and amidinated with S-methyl thioacetimidate (SMTA). Amidinated proteins were digested with trypsin and analyzed with a high-resolution orbitrap mass spectrometer.

resultsSixteen examples of Staphylococcus aureus secretory proteins that lose an N-terminal signal peptide during their export were identified using this amidination approach. The N-termini of proteins with and without methionine were identified. Unanticipated protein cleavages due to sortase and an unknown protease were also uncovered.

conclusionsA simple N-terminal amidination based mass spectrometry approach is described that facilitates identification of the N-terminus of a mature protein and the discovery of unexpected processing sites.

Indexed as

Amino Acid MotifsAmino Acid SequenceBacterial ProteinsBiocatalysisButyratesMass SpectrometryProtein Processing, Post-TranslationalProtein Sorting SignalsProteolysisStaphylococcus aureusSulfhydryl CompoundsTrichloroacetic AcidTrypsinBacterial ProteinsButyratesProtein Sorting SignalsS-methyl thiobutanoateSulfhydryl CompoundsTrichloroacetic AcidTrypsin

Identifiers

PMID30884002
PMCPMC6522274
OpenAlexW2924287439

What OpenQuestion holds

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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.