Evidence map›Paper›PMID 19582228›Full record

ReviewInternational journal of molecular sciences2009

Yeast two-hybrid, a powerful tool for systems biology.

Anna Brückner, Cécile Polge, Nicolas Lentze, Daniel Auerbach, Uwe Schlattner

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 253 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
253citing papers in PubMed, 1 pooled it
–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

253 citing papers in PubMed, 1 synthesis or guideline pooled it.

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193 more citing papers are in PubMed but not listed here.

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

5 authors.

Anna BrücknerINSERM U884, Université Joseph Fourier, Laboratoire de Bioénergétique Fondamentale et Appliquée, 2280 Rue de la Piscine, BP 53, Grenoble Cedex 9, France.
Cécile PolgeINSERM U884, Université Joseph Fourier, Laboratoire de Bioénergétique Fondamentale et Appliquée, 2280 Rue de la Piscine, BP 53, Grenoble Cedex 9, France.
Nicolas LentzeDualsystems Biotech AG / Grabenstrasse 11a, 8952 Schlieren, Switzerland.
Daniel AuerbachDualsystems Biotech AG / Grabenstrasse 11a, 8952 Schlieren, Switzerland.
Uwe SchlattnerINSERM U884, Université Joseph Fourier, Laboratoire de Bioénergétique Fondamentale et Appliquée, 2280 Rue de la Piscine, BP 53, Grenoble Cedex 9, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A key property of complex biological systems is the presence of interaction networks formed by its different components, primarily proteins. These are crucial for all levels of cellular function, including architecture, metabolism and signalling, as well as the availability of cellular energy. Very stable, but also rather transient and dynamic protein-protein interactions generate new system properties at the level of multiprotein complexes, cellular compartments or the entire cell. Thus, interactomics is expected to largely contribute to emerging fields like systems biology or systems bioenergetics. The more recent technological development of high-throughput methods for interactomics research will dramatically increase our knowledge of protein interaction networks. The two most frequently used methods are yeast two-hybrid (Y2H) screening, a well established genetic in vivo approach, and affinity purification of complexes followed by mass spectrometry analysis, an emerging biochemical in vitro technique. So far, a majority of published interactions have been detected using an Y2H screen. However, with the massive application of this method, also some limitations have become apparent. This review provides an overview on available yeast two-hybrid methods, in particular focusing on more recent approaches. These allow detection of protein interactions in their native environment, as e.g. in the cytosol or bound to a membrane, by using cytosolic signalling cascades or split protein constructs. Strengths and weaknesses of these genetic methods are discussed and some guidelines for verification of detected protein-protein interactions are provided.

Indexed as

Two-Hybrid System TechniquesMass SpectrometryProtein Interaction MapsProteinsRNA Polymerase IIISystems BiologyProteinsRNA Polymerase IIIinteractomicsmass spectrometryprotein-protein interactionsystems bioenergeticsyeast two-hybrid

Identifiers

PMID19582228
PMCPMC2705515

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.