Evidence map›Paper›PMID 24952186›Full record

ReviewAdvances in experimental medicine and biology2014

A mass spectrometry view of stable and transient protein interactions.

Hanna G Budayeva, Ileana M Cristea

Open access · greenAbstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
15.1field-weighted citation impact, top 2% 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

27 citing papers in PubMed, 38 citations in OpenAlex.

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  19. Integrating molecular networks with genetic variant interpretation for precision medicine.Wiley interdisciplinary reviews. Systems biology and medicine · 2019
    Review
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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.

Hanna G BudayevaDepartment of Molecular Biology, 210 Lewis Thomas Laboratory, Princeton University, Princeton, NJ, 08544, USA.
Ileana M Cristea
Princeton University · US

Funding

Proteomic Tools to Uncover the Role of Chromatin Remodeling in HIV-1 InfectionDP1DA026192 · NIDA · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 2008 to 2012
$3.9M
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
NIAID NIH HHS R21 AI102187NIAID NIH HHS R21AI102187NICHD NIH HHS R21 HD073044NICHD NIH HHS R21 HD073044-01A1NIDA NIH HHS DP1 DA026192NIDA NIH HHS DP1DA026192
6 · The paper itself

Abstract

Through an impressive range of dynamic interactions, proteins succeed to carry out the majority of functions in a cell. These temporally and spatially regulated interactions provide the means through which one single protein can perform diverse functions and modulate different cellular pathways. Understanding the identity and nature of these interactions is therefore critical for defining protein functions and their contribution to health and disease processes. Here, we provide an overview of workflows that incorporate immunoaffinity purifications and quantitative mass spectrometry (frequently abbreviated as IP-MS or AP-MS) for characterizing protein-protein interactions. We discuss experimental aspects that should be considered when optimizing the isolation of a protein complex. As the presence of nonspecific associations is a concern in these experiments, we discuss the common sources of nonspecific interactions and present label-free and metabolic labeling mass spectrometry-based methods that can help determine the specificity of interactions. The effective regulation of cellular pathways and the rapid reaction to various environmental stresses rely on the formation of stable, transient, and fast-exchanging protein-protein interactions. While determining the exact nature of an interaction remains challenging, we review cross-linking and metabolic labeling approaches that can help address this important aspect of characterizing protein interactions and macromolecular assemblies.

Indexed as

AnimalsHumansIsotope LabelingMass SpectrometryProteinsProteins

Identifiers

PMID24952186
PMCPMC5978421
OpenAlexW6013862

What OpenQuestion holds

Textmetadata
LicenceTDM
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.