Evidence map›Paper›PMID 26918858›Full record

ArticleSmall GTPases2016

A pull-down procedure for the identification of unknown GEFs for small GTPases.

Daniel Koch, Amrita Rai, Imtiaz Ali, Nathalie Bleimling, Timon Friese, Andreas Brockmeyer, Petra Janning, Bruno Goud, Aymelt Itzen, Matthias P Müller and 1 more

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Article in Small GTPases, 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
1.3field-weighted citation impact, top 22% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

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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

11 authors at 3 institutions in 2 countries.

Daniel Kocha Department of Structural Biochemistry , Max Planck Institute of Molecular Physiology , Dortmund , Germany.
Amrita Raia Department of Structural Biochemistry , Max Planck Institute of Molecular Physiology , Dortmund , Germany.
Imtiaz Alia Department of Structural Biochemistry , Max Planck Institute of Molecular Physiology , Dortmund , Germany.
Nathalie Bleimlinga Department of Structural Biochemistry , Max Planck Institute of Molecular Physiology , Dortmund , Germany.
Timon Friesea Department of Structural Biochemistry , Max Planck Institute of Molecular Physiology , Dortmund , Germany.
Andreas Brockmeyerb Department of Chemical Biology , Max Planck Institute of Molecular Physiology , Dortmund , Germany.
Petra Janningb Department of Chemical Biology , Max Planck Institute of Molecular Physiology , Dortmund , Germany.
Bruno Goudc Institut Curie, PSL Research University, CNRS UMR 144 , Paris , France.
Aymelt Itzend Center for Integrated Protein Science Munich (CIPSM), Department of Chemistry, Technische Universität München , Garching , Germany.
Matthias P Müllera Department of Structural Biochemistry , Max Planck Institute of Molecular Physiology , Dortmund , Germany.
Roger S Goodya Department of Structural Biochemistry , Max Planck Institute of Molecular Physiology , Dortmund , Germany.
Max Planck Institute of Molecular Physiology · DECenter for Integrated Protein Science Munich · DECentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the family of small GTPases regulate a variety of important cellular functions. In order to accomplish this, tight temporal and spatial regulation is absolutely necessary. The two most important factors for this regulation are GTPase activating proteins (GAPs) and guanine nucleotide exchange factors (GEFs), the latter being responsible for the activation of the GTPase downstream pathways at the correct location and time. Although a large number of exchange factors have been identified, it is likely that a similarly large number remains unidentified. We have therefore developed a procedure to specifically enrich GEF proteins from biological samples making use of the high affinity binding of GEFs to nucleotide-free GTPases. In order to verify the results of these pull-down experiments, we have additionally developed two simple validation procedures: An in vitro transcription/translation system coupled with a GEF activity assay and a yeast two-hybrid screen for detection of GEFs. Although the procedures were established and tested using the Rab protein Sec4, the similar basic principle of action of all nucleotide exchange factors will allow the method to be used for identification of unknown GEFs of small GTPases in general.

Indexed as

Two-Hybrid System TechniquesGuanine Nucleotide Exchange Factorsrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGuanine Nucleotide Exchange Factorsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSEC2 protein, S cerevisiaeSEC4 protein, S cerevisiaeenrichmentGEFin vitro transcription/translationnucleotide exchange factorpull-downsmall GTPaseyeast two-hybrid

Identifiers

PMID26918858
PMCPMC4905258
OpenAlexW2280861519

What OpenQuestion holds

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LicenceCC BY-NC
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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.