Evidence map›Paper›PMID 28055292›Full record

ReviewSmall GTPases2018

Molecular control of Rab activity by GEFs, GAPs and GDI.

Matthias P Müller, Roger S Goody

Open access · bronzeAbstract readReview
In one paragraph

Review in Small GTPases, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
9.8field-weighted citation impact, top 1% 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

134 citing papers in PubMed, 232 citations in OpenAlex.

  1. Article
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  6. RAB5C Increases Endothelial Release of VWF by Regulating Vesicle Trafficking.Arteriosclerosis, thrombosis, and vascular biology · 2026
    Article
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  15. Review
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74 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

2 authors at 1 institution in 1 country.

Matthias P Müllera Department of Structural Biochemistry , Max Planck Institute of Molecular Physiology , Dortmund , Germany.ORCID 0000-0002-1529-8933
Roger S Goodya Department of Structural Biochemistry , Max Planck Institute of Molecular Physiology , Dortmund , Germany.ORCID 0000-0002-0772-0444
Max Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rab proteins are the major regulators of vesicular trafficking in eukaryotic cells. Their activity can be tightly controlled within cells: Regulated by guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs), they switch between an active GTP-bound state and an inactive GDP-bound state, interacting with downstream effector proteins only in the active state. Additionally, they can bind to membranes via C-terminal prenylated cysteine residues and they can be solubilized and shuttled between membranes by chaperone-like molecules called GDP dissociation inhibitors (GDIs). In this review we give an overview of Rab proteins with a focus on the current understanding of their regulation by GEFs, GAPs and GDI.

Indexed as

Amino Acid SequenceAnimalsCell MembraneGTPase-Activating ProteinsGuanine Nucleotide Dissociation InhibitorsGuanine Nucleotide Exchange FactorsHumansProtein Prenylationrab GTP-Binding ProteinsGTPase-Activating ProteinsGuanine Nucleotide Dissociation InhibitorsGuanine Nucleotide Exchange Factorsrab GTP-Binding ProteinsGAPSGDIGEFsintracellular traffickingposttranslational modificationsRab proteinsvesicular transport

Identifiers

PMID28055292
PMCPMC5902221
OpenAlexW2571487949

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.