Evidence map›Paper›PMID 20144949›Full record

ArticleNucleic acids research2010

Rapid interactome profiling by massive sequencing.

Roberto Di Niro, Ana-Marija Sulic, Flavio Mignone, Sara D'Angelo, Roberta Bordoni, Michele Iacono, Roberto Marzari, Tiziano Gaiotto, Miha Lavric, Andrew R M Bradbury and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
9.4field-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

37 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
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  6. Article
  7. The RNA-binding protein ILF3 binds to transposable element sequences in SINEUP lncRNAs.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  8. High-resolution protein-protein interaction mapping using all-The Journal of biological chemistry · 2019
    Article
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  11. Review
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  14. Article
  15. Article
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  18. From deep sequencing to actual clones.Protein engineering, design & selection : PEDS · 2014
    Article
  19. Article
  20. Interaction analysis through proteomic phage display.BioMed research international · 2014
    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

15 authors at 2 institutions in 2 countries.

Roberto Di NiroDepartment of Life Sciences, University of Trieste, Trieste, Italy.
Ana-Marija Sulic
Flavio Mignone
Sara D'Angelo
Roberta Bordoni
Michele Iacono
Roberto Marzari
Tiziano Gaiotto
Miha Lavric
Andrew R M Bradbury
Luigi Biancone
Dina Zevin-Sonkin
Gianluca De Bellis
Claudio Santoro
Daniele Sblattero
Los Alamos National Laboratory · USUniversity of Trieste · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have developed a high-throughput protein expression and interaction analysis platform that combines cDNA phage display library selection and massive gene sequencing using the 454 platform. A phage display library of open reading frame (ORF) fragments was created from mRNA derived from different tissues. This was used to study the interaction network of the enzyme transglutaminase 2 (TG2), a multifunctional enzyme involved in the regulation of cell growth, differentiation and apoptosis, associated with many different pathologies. After two rounds of panning with TG2 we assayed the frequency of ORFs within the selected phage population using 454 sequencing. Ranking and analysis of more than 120,000 sequences allowed us to identify several potential interactors, which were subsequently confirmed in functional assays. Within the identified clones, three had been previously described as interacting proteins (fibronectin, SMOC1 and GSTO2), while all the others were new. When compared with standard systems, such as microtiter enzyme-linked immunosorbant assay, the method described here is dramatically faster and yields far more information about the interaction under study, allowing better characterization of complex systems. For example, in the case of fibronectin, it was possible to identify the specific domains involved in the interaction.

Indexed as

DNA, ComplementaryGTP-Binding ProteinsHumansOpen Reading FramesPeptide LibraryProtein Glutamine gamma Glutamyltransferase 2Protein Interaction Domains and MotifsProtein Interaction MappingSequence Analysis, DNATransglutaminasesDNA, ComplementaryGTP-Binding ProteinsPeptide LibraryProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID20144949
PMCPMC2875021
OpenAlexW1996099028

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.