Evidence map›Paper›PMID 23410677›Full record

ArticleMethods (San Diego, Calif.)2013

Applications of selected reaction monitoring (SRM)-mass spectrometry (MS) for quantitative measurement of signaling pathways.

Yingxin Zhao, Allan R Brasier

Abstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 53 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Yingxin ZhaoSealy Center for Molecular Medicine, University of Texas Medical Branch, Galveston, TX, USA.
Allan R Brasier
The University of Texas Medical Branch at Galveston · US

Funding

Virus, Tissue Culture and ImmunoassayP01AI062885 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI BOLDOGH, ISTVAN STEVEN · 2005 to 2022
$23.9M
Synthetic Organic Chemistry CoreP30ES006676 · NIEHS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI ELFERINK, CORNELIS JOHAN · 1995 to 2017
$21.7M
UTMB Clinical and Translational Science AwardUL1TR000071 · NCATS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI BRASIER, ALLAN R. · 2012 to 2014
$14.4M
Collaborative Research : Stochastic Modeling and Estimation of Gene TranscriptionR01GM086885 · NIGMS · RICE UNIVERSITY · PI KIMMEL, MAREK · 2008 to 2011
$1.7M
UTMB Clinical and Translational Science AwardKL2TR000072 · NCATS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI BRASIER, ALLAN R. · 2012 to 2014
$422k
NCATS NIH HHS KL2 TR000072NCATS NIH HHS UL1 TR000071NCATS NIH HHS UL1TR000071NHLBI NIH HHS HHSN268201000037CNIAID NIH HHS HHSN272200800048CNIAID NIH HHS P01 AI062885NIEHS NIH HHS P30 ES006676
6 · The paper itself

Abstract

Quantitative measurement of the major regulatory proteins in signaling networks poses several technical challenges, including low abundance, the presence of post-translational modifications (PTMs), and the lack of suitable affinity detection reagents. Using the innate immune response (IIR) as a model signaling pathway, we illustrate the approach of stable isotope dilution (SID)-selected reaction monitoring (SRM)-mass spectrometry (MS) assays for quantification of low abundance signaling proteins. A work flow for SID-SRM-MS assay development is established for proteins with experimentally observed MS spectra and for those without. Using the interferon response factor (IRF)-3 transcription factor as an example, we illustrate the steps in high responding signature peptide identification, SID-SRM-MS assay optimization, and evaluation. SRM assays for normalization of IIR abundance to invariant housekeeping proteins are presented. We provide an example of SID-SRM assay development for post-translational modification (PTM) detection using an activating phospho-Ser modified NF-κB/RelA transcription factor, and describe challenges inherent in PTM-SID-SRM-MS assay development. Application of highly qualified quantitative, SID-SRM-MS assays will enable a systems-level approach to understanding the dynamics and kinetics of signaling in host cells, such as the IIR.

Indexed as

Biological AssayProtein Processing, Post-TranslationalSignal TransductionAmino Acid SequenceCarbon IsotopesCell Line, TumorEpithelial CellsHumansImmunity, InnateIndicator Dilution TechniquesInterferon Regulatory Factor-3Isotope LabelingMolecular Sequence DataNitrogen IsotopesPeptide FragmentsPhosphorylationCarbon IsotopesInterferon Regulatory Factor-3Nitrogen IsotopesPeptide FragmentsRELA protein, humanTranscription Factor RelA

Identifiers

PMID23410677
PMCPMC3763905
OpenAlexW1984226667

What OpenQuestion holds

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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.