Evidence map›Paper›PMID 18801062›Full record

ReviewTraffic (Copenhagen, Denmark)2008

Mechanisms of EHD/RME-1 protein function in endocytic transport.

Barth D Grant, Steve Caplan

Open access · greenAbstract readReview
In one paragraph

Review in Traffic (Copenhagen, Denmark), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
7.4field-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

102 citing papers in PubMed, 146 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The endocytic fission protein EHD1 interacts with tubulin and regulates microtubule function.Biochimica et biophysica acta. Molecular cell research · 2026
    Article
  5. Article
  6. mCancer communications (London, England) · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. WAVE facilitates polarized E-cadherin transport.Molecular biology of the cell · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. A Role of Phosphatidylserine in the Function of Recycling Endosomes.Frontiers in cell and developmental biology · 2021
    Review
  18. Review
  19. Article
  20. Article

42 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 2 institutions in 1 country.

Barth D GrantDepartment of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08854, USA. grant@biology.rutgers.edu
Steve Caplan
Rutgers, The State University of New Jersey · USUniversity of Nebraska Medical Center · US

Funding

Membrane Traffic in C. elegans and MammalsR01GM067237 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI GRANT, BARTH DEMIAN · 2003 to 2019
$6.1M
Molecular Mechanisms Controlling Endocytic RecyclingR01GM074876 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CAPLAN, STEVEN H · 2006 to 2015
$2.6M
NIGMS NIH HHS GM067237NIGMS NIH HHS GM074876NIGMS NIH HHS R01 GM067237NIGMS NIH HHS R01 GM074876
6 · The paper itself

Abstract

The evolutionarily conserved Eps15 homology domain (EHD)/receptor-mediated endocytosis (RME)-1 family of C-terminal EH domain proteins has recently come under intense scrutiny because of its importance in intracellular membrane transport, especially with regard to the recycling of receptors from endosomes to the plasma membrane. Recent studies have shed new light on the mode by which these adenosine triphosphatases function on endosomal membranes in mammals and Caenorhabditis elegans. This review highlights our current understanding of the physiological roles of these proteins in vivo, discussing conserved features as well as emerging functional differences between individual mammalian paralogs. In addition, these findings are discussed in light of the identification of novel EHD/RME-1 protein and lipid interactions and new structural data for proteins in this family, indicating intriguing similarities to the Dynamin superfamily of large guanosine triphosphatases.

Indexed as

EndocytosisAnimalsBiological TransportHumansLipid MetabolismNucleotidesProtein BindingVesicular Transport ProteinsNucleotidesVesicular Transport Proteins

Identifiers

PMID18801062
PMCPMC2766864
OpenAlexW2034913511

What OpenQuestion holds

Textmetadata
LicenceTDM
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.