Evidence map›Paper›PMID 12972569›Full record

ArticleMolecular biology of the cell2003

Molecular evolution of the Rab-escort-protein/guanine-nucleotide-dissociation-inhibitor superfamily.

Christelle Alory, William E Balch

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

  1. Physiological adventures inMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  2. Membrane trafficking alterations in breast cancer progression.Frontiers in cell and developmental biology · 2024
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Intracellular Vesicle Trafficking Genes,Frontiers in genetics · 2019
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Hsp90 Co-localizes with Rab-GDI-1 and regulates agonist-induced amylase release in AR42J cells.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2009
    Article
  15. Article
  16. Article
  17. Article
  18. Article
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.

Christelle AloryDepartments of Cell and Molecular Biology and The Institute for Childhood and Neglected Diseases, The Scripps Research Institute, La Jolla, California 92130, USA. welbach@scripps.edu
William E Balch
Scripps Research Institute · US

Funding

Structure and Function of Guanine Nucleotide Dissociation InhibitorR01GM033301 · NIGMS · YALE UNIVERSITY · PI BALCH, WILLIAM EDWARD · 1985 to 2012
$4.6M
STRUCTURAL AND MOLECULAR ANALYSIS OF CHOROIDEREMIAR01EY011606 · NEI · SCRIPPS RESEARCH INSTITUTE · PI BALCH, WILLIAM EDWARD · 1997 to 2005
$1.6M
NEI NIH HHS EY11606NEI NIH HHS R01 EY011606NIGMS NIH HHS GM-33301NIGMS NIH HHS R01 GM033301
6 · The paper itself

Abstract

Prenylation of Rab GTPases regulating vesicle traffic by Rab geranylgeranyltransferase (RabGGTase) requires a complex formed by the association of newly synthesized Rab proteins with Rab-escort-protein (REP), the choroideremia-gene-product that is mutated in disease, leading to loss of vision. After delivery to the membrane by the REP-Rab complex, subsequent recycling to the cytosol requires the REP-related guanine-nucleotide-dissociation-inhibitor (GDI). Although REP and GDI share common Rab-binding properties, GDI cannot assist in Rab prenylation and REP cannot retrieve Rab proteins from the membranes. We have now isolated REP mutant proteins that are able to partially function as both REP and GDI. These results provide molecular insight into the functional and evolutionary organization of the REP/GDI superfamily.

Indexed as

Alkyl and Aryl TransferasesEscherichia coliEvolution, MolecularGuanine Nucleotide Dissociation InhibitorsModels, StructuralMutationProtein BindingProtein PrenylationProtein Structure, Tertiaryrab GTP-Binding ProteinsSaccharomyces cerevisiaeSignal TransductionAlkyl and Aryl TransferasesGuanine Nucleotide Dissociation InhibitorsRab geranylgeranyltransferaserab GTP-Binding Proteins

Identifiers

PMID12972569
PMCPMC196578
OpenAlexW2141017790

What OpenQuestion holds

Textmetadata
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.