Evidence map›Paper›PMID 22806901›Full record

ReviewHistology and histopathology2012

ArfGAP1 function in COPI mediated membrane traffic: currently debated models and comparison to other coat-binding ArfGAPs.

Yoko Shiba, Paul A Randazzo

Open access · greenAbstract readComparative StudyReview
In one paragraph

Review in Histology and histopathology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Length Polymorphism and Methylation Status of UPS29 Minisatellite of theInternational journal of molecular sciences · 2020
    Article
  10. ARF family GTPases with links to cilia.American journal of physiology. Cell physiology · 2020
    Review
  11. Article
  12. Review
  13. Article
  14. ArfGAPs: key regulators for receptor sorting.Receptors & clinical investigation · 2014
    Article
  15. Article
  16. Review
  17. Article
  18. Organization of the ER-Golgi interface for membrane traffic control.Nature reviews. Molecular cell biology · 2013
    Review
  19. Article
  20. Review
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.

Yoko ShibaNational Cancer Institute, Laboratory of Cellular and Molecular Biology, Bethesda, MD 20892, USA.
Paul A Randazzo
National Cancer Institute · US

Funding

Regulation of ADP-ribosylation factorZIABC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 2009 to 2025
$27.9M
REGULATION OF ADP-RIBOSYLATION FACTORZ01BC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 1996 to 2008
$3.3M
Intramural NIH HHS Z01 BC007365
6 · The paper itself

Abstract

The ArfGAPs are a family of proteins containing an ArfGAP catalytic domain that induces the hydrolysis of GTP bound to the small guanine nucleotide binding-protein ADP-ribosylation factor (Arf). Functional models for Arfs, which are regulators of membrane traffic, are based on the idea that guanine nucleotide-binding proteins function as switches: Arf with GTP bound is active and binds to effector proteins; the conversion of GTP to GDP inactivates Arf. The cellular activities of ArfGAPs have been examined primarily as regulatory proteins that inactivate Arf; however, Arf function in membrane traffic does not strictly adhere to the concept of a simple switch, adding complexity to models explaining the role of ArfGAPs. Here, we review the literature addressing the function Arf and ArfGAP1 in COPI mediated transport, focusing on two critical and integrated functions of membrane traffic, cargo sorting and vesicle coat polymerization. We briefly discuss other ArfGAPs that may have similar function in Arf-dependent membrane traffic outside the ER-Golgi.

Indexed as

AnimalsCell MembraneCoat Protein Complex IGTPase-Activating ProteinsHumansProtein TransportARFGAP1 protein, humanCoat Protein Complex IGTPase-Activating Proteins

Identifiers

PMID22806901
PMCPMC7477946
OpenAlexW10474832

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.