Evidence map›Paper›PMID 10749927›Full record

ArticleMolecular biology of the cell2000

A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi.

A L Boman, C j Zhang, X Zhu, R A Kahn

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
10.9field-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

114 citing papers in PubMed, 261 citations in OpenAlex.

  1. Article
  2. Review
  3. The Recycling Endosomal (NaActa physiologica (Oxford, England) · 2026
    Article
  4. Article
  5. Article
  6. Arfs on the Golgi: four conductors, one orchestra.Frontiers in molecular biosciences · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Protein sorting from endosomes to the TGN.Frontiers in cell and developmental biology · 2023
    Review
  13. Article
  14. Getting where you want to go.Molecular biology of the cell · 2022
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

54 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

4 authors at 1 institution in 1 country.

A L BomanDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322-3050, USA.
C j Zhang
X Zhu
R A Kahn
Emory University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A family of three structurally related proteins were cloned from human cDNA libraries by their ability to interact preferentially with the activated form of human ADP-ribosylation factor 3 (ARF3) in two-hybrid assays. The specific and GTP-dependent binding was later confirmed through direct protein binding of recombinant proteins. The three proteins share large ( approximately 300 residues) domains at their N termini that are 60-70% identical to each other and a shorter (73 residues) domain at their C termini with 70% homology to the C-terminal "ear" domain of gamma-adaptin. Although GGA1 is found predominantly as a soluble protein by cell fractionation, all three proteins were found to localize to the trans-Golgi network (TGN) by indirect immunofluorescence. The binding of GGAs to TGN was sensitive to brefeldin A, consistent with this being an ARF-dependent event. Thus, these proteins have been named Golgi-localizing, gamma-adaptin ear homology domain, ARF-binding proteins, or GGAs. The finding that overexpression of GGAs was sufficient to alter the distribution of markers of the TGN (TGN38 and mannose 6-phosphate receptors) led us to propose that GGAs are effectors for ARFs that function in the regulation of membrane traffic through the TGN.

Indexed as

Adaptor Proteins, Vesicular TransportProteinsADP-Ribosylation FactorsAmino Acid SequenceAnimalsBiological TransportBlotting, NorthernCarrier ProteinsCells, CulturedFibroblastsFluorescent Antibody Technique, IndirectGolgi ApparatusHumansImmunoblottingIntracellular MembranesKidneyAdaptor Proteins, Vesicular TransportADP-Ribosylation FactorsARF3 protein, humanArf3 protein, ratCarrier ProteinsGGA2 protein, humanGGA adaptor proteinsProteins

Identifiers

PMID10749927
PMCPMC14844
OpenAlexW2128969723

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.