Evidence map›Paper›PMID 26867737›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2016

Determining the Composition and Stability of Protein Complexes Using an Integrated Label-Free and Stable Isotope Labeling Strategy.

Todd M Greco, Amanda J Guise, Ileana M Cristea

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

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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

3 authors.

Todd M GrecoDepartment of Molecular Biology, Princeton University, 210 Lewis Thomas Laboratory, Washington Road, Princeton, NJ, 08544, USA.
Amanda J GuiseDepartment of Molecular Biology, Princeton University, 210 Lewis Thomas Laboratory, Washington Road, Princeton, NJ, 08544, USA.
Ileana M CristeaDepartment of Molecular Biology, Princeton University, 210 Lewis Thomas Laboratory, Washington Road, Princeton, NJ, 08544, USA. icristea@princeton.edu.

Funding

Mechanisms mediating immune response upon sensing of nuclear viral DNAR01GM114141 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 2015 to 2023
$2.6M
Functional investigation of the TBX20 cardiac interactomeR01HL127640 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CONLON, FRANK LEO, CRISTEA, ILEANA M. · 2015 to 2018
$2.5M
Direct and Quantitative Proteomic Approaches in XenopusR21HD073044 · NICHD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CONLON, FRANK LEO, CRISTEA, ILEANA M. · 2013 to 2014
$436k
Host Factors Required for Dengue and Yellow Fever Virus AmplificationR21AI102187 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CRISTEA, ILEANA M., THOMPSON, SUNNIE R · 2012 to 2013
$414k
NHLBI NIH HHS R01 HL127640NIAID NIH HHS R21 AI102187NIAID NIH HHS R21AI102187NICHD NIH HHS R21 HD073044NIGMS NIH HHS R01 GM114141NIGMS NIH HHS R01GM114141
6 · The paper itself

Abstract

In biological systems, proteins catalyze the fundamental reactions that underlie all cellular functions, including metabolic processes and cell survival and death pathways. These biochemical reactions are rarely accomplished alone. Rather, they involve a concerted effect from many proteins that may operate in a directed signaling pathway and/or may physically associate in a complex to achieve a specific enzymatic activity. Therefore, defining the composition and regulation of protein complexes is critical for understanding cellular functions. In this chapter, we describe an approach that uses quantitative mass spectrometry (MS) to assess the specificity and the relative stability of protein interactions. Isolation of protein complexes from mammalian cells is performed by rapid immunoaffinity purification, and followed by in-solution digestion and high-resolution mass spectrometry analysis. We employ complementary quantitative MS workflows to assess the specificity of protein interactions using label-free MS and statistical analysis, and the relative stability of the interactions using a metabolic labeling technique. For each candidate protein interaction, scores from the two workflows can be correlated to minimize nonspecific background and profile protein complex composition and relative stability.

Indexed as

AnimalsHumansIsotope LabelingMass SpectrometryProteinsProtein StabilityProteomicsProteinsAffinity isolationI-DIRTImmunoprecipitationLabel-free quantificationProtein complexesProtein interactionsSAINTStable isotope labeling quantification

Identifiers

PMID26867737
PMCPMC4916643

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Registered trials

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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.