Evidence map›Paper›PMID 23937658›Full record

ArticleJournal of proteome research2013

Affinity purification strategies for proteomic analysis of transcription factor complexes.

Roberto Giambruno, Florian Grebien, Alexey Stukalov, Christian Knoll, Melanie Planyavsky, Elena L Rudashevskaya, Jacques Colinge, Giulio Superti-Furga, Keiryn L Bennett

Abstract read
In one paragraph

Article in Journal of proteome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

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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

15 citing papers in PubMed.

  1. Article
  2. TMBIM5 is the CaEMBO reports · 2022
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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

9 authors.

Roberto GiambrunoCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Lazarettgasse 14, AKH BT 25.3, 1090 Vienna, Austria.
Florian Grebien
Alexey Stukalov
Christian Knoll
Melanie Planyavsky
Elena L Rudashevskaya
Jacques Colinge
Giulio Superti-Furga
Keiryn L Bennett

Funding

Austrian Science Fund FWF P 22282
6 · The paper itself

Abstract

Affinity purification (AP) coupled to mass spectrometry (MS) has been successful in elucidating protein molecular networks of mammalian cells. These approaches have dramatically increased the knowledge of the interconnectivity present among proteins and highlighted biological functions within different protein complexes. Despite significant technical improvements reached in the past years, it is still challenging to identify the interaction networks and the subsequent associated functions of nuclear proteins such as transcription factors (TFs). A straightforward and robust methodology is therefore required to obtain unbiased and reproducible interaction data. Here we present a new approach for TF AP-MS, exemplified with the CCAAT/enhancer binding protein alpha (C/EBPalpha). Utilizing the advantages of a double tag and three different MS strategies, we conducted a total of six independent AP-MS strategies to analyze the protein-protein interactions of C/EBPalpha. The resultant data were combined to produce a cohesive C/EBPalpha interactome. Our study describes a new methodology that robustly identifies specific molecular complexes associated with transcription factors. Moreover, it emphasizes the existence of TFs as protein complexes essential for cellular biological functions and not as single, static entities.

Indexed as

AnimalsCCAAT-Enhancer-Binding Protein-alphaCell LineChromatography, AffinityChromatography, Reverse-PhaseHemagglutinin Glycoproteins, Influenza VirusProtein BindingProtein Interaction MappingProtein Interaction MapsRatsStreptavidinCCAAT-Enhancer-Binding Protein-alphaHemagglutinin Glycoproteins, Influenza VirusStreptavidin

Identifiers

PMID23937658
PMCPMC3768224

What OpenQuestion holds

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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.