Evidence map›Paper›PMID 27451424›Full record

ArticleMolecular & cellular proteomics : MCP2016

Proteoform-Specific Insights into Cellular Proteome Regulation.

Emma L Norris, Madeleine J Headlam, Keyur A Dave, David D Smith, Alexander Bukreyev, Toshna Singh, Buddhika A Jayakody, Keith J Chappell, Peter L Collins, Jeffrey J Gorman

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. 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
0.2field-weighted citation impact, top 35% 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, 4 citations in OpenAlex.

  1. Proteomics Tracing the Footsteps of Infectious Disease.Molecular & cellular proteomics : MCP · 2017
    Review
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

10 authors at 3 institutions in 2 countries.

Emma L NorrisFrom the ‡Protein Discovery Centre and.
Madeleine J HeadlamFrom the ‡Protein Discovery Centre and.
Keyur A DaveFrom the ‡Protein Discovery Centre and.
David D Smith§Statistics Unit, QIMR Berghofer Medical Research Institute, Herston, Queensland, Australia.
Alexander Bukreyev¶Respiratory Virus Section, Laboratory of Infectious Diseases, National Institute for Allergy and Infectious Diseases, NIH, Bethesda, Maryland, and.
Toshna SinghFrom the ‡Protein Discovery Centre and.
Buddhika A JayakodyFrom the ‡Protein Discovery Centre and.
Keith J Chappell‖School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, Australia.
Peter L Collins¶Respiratory Virus Section, Laboratory of Infectious Diseases, National Institute for Allergy and Infectious Diseases, NIH, Bethesda, Maryland, and.
Jeffrey J GormanFrom the ‡Protein Discovery Centre and ‖School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, Australia jeff.gorman@qimr.edu.au.
QIMR Berghofer Medical Research Institute · AUNational Institute of Allergy and Infectious Diseases · USUniversity of Queensland · AU

Funding

Laboratory Studies of Human Respiratory Syncytial Virus and Other PneumovirusesZIAAI000372 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI BUCHHOLZ, URSULA · 2009 to 2025
$21.8M
6 · The paper itself

Abstract

Knowledge regarding compositions of proteomes at the proteoform level enhances insights into cellular phenotypes. A strategy is described herein for discovery of proteoform-specific information about cellular proteomes. This strategy involved analysis of data obtained by bottom-up mass spectrometry of multiple protein OGE separations on a fraction by fraction basis. The strategy was exemplified using five matched sets of lysates of uninfected and human respiratory syncytial virus-infected A549 cells. Template matching demonstrated that 67.3% of 10475 protein profiles identified focused to narrow pI windows indicative of efficacious focusing. Furthermore, correlation between experimental and theoretical pI gradients indicated reproducible focusing. Based on these observations a proteoform profiling strategy was developed to identify proteoforms, detect proteoform diversity and discover potential proteoform regulation. One component of this strategy involved examination of the focusing profiles for protein groups. A novel concordance analysis facilitated differentiation between proteoforms, including proteoforms generated by alternate splicing and proteolysis. Evaluation of focusing profiles and concordance analysis were applicable to cells from a single and/or multiple biological states. Statistical analyses identified proteoform variation between biological states. Regulation relevant to cellular responses to human respiratory syncytial virus was revealed. Western blotting and Protomap analyses validated the proteoform regulation. Discovery of STAT1, WARS, MX1, and HSPB1 proteoform regulation by human respiratory syncytial virus highlighted the impact of the profiling strategy. Novel truncated proteoforms of MX1 were identified in infected cells and phosphorylation driven regulation of HSPB1 proteoforms was correlated with infection. The proteoform profiling strategy is generally applicable to investigating interactions between viruses and host cells and the analysis of other biological systems.

Indexed as

A549 CellsChromatography, LiquidGene Expression RegulationHumansPhosphorylationProteolysisProteomeProteomicsRespiratory Syncytial Virus, HumanTandem Mass SpectrometryProteome

Identifiers

PMID27451424
PMCPMC5054351
OpenAlexW2486797327

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.