Evidence map›Paper›PMID 18353293›Full record

ReviewCarbohydrate research2008

Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation.

Richard D Smith, Vladimir V Lupashin

Open access · greenAbstract readReview
In one paragraph

Review in Carbohydrate research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed, 1 pooled it
4.0field-weighted citation impact, top 6% 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

78 citing papers in PubMed, 1 synthesis or guideline pooled it, 152 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. GARP Complex in Golgi Physiology.Sub-cellular biochemistry · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Trafficking and localization of Golgi-residentFrontiers in plant science · 2025
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Population genetic analysis based on the polymorphisms mediated by transposons in the genomes of pig.DNA research : an international journal for rapid publication of reports on genes and genomes · 2024
    Article
  18. Article
  19. Tumor TargetingMicroRNA (Shariqah, United Arab Emirates) · 2024
    Article
  20. Article

18 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.

Richard D SmithDepartment of Physiology and Biophysics, College of Medicine, University of Arkansas for Medical Sciences, Biomed 261-2, Slot 505, 200 South Cedar St., Little Rock, AR 72205, USA.
Vladimir V Lupashin
University of Arkansas for Medical Sciences · US

Funding

Characterization of mammalian COG complex-interacting intra-Golgi trafficking macR01GM083144 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI VLADIMIR V LUPASHIN · 2008 to 2026
$6.5M
NIGMS NIH HHS R01 GM083144
6 · The paper itself

Abstract

The Golgi apparatus is a central hub for both protein and lipid trafficking/sorting and is also a major site for glycosylation in the cell. This organelle employs a cohort of peripheral membrane proteins and protein complexes to keep its structural and functional organization. The conserved oligomeric Golgi (COG) complex is an evolutionary conserved peripheral membrane protein complex that is proposed to act as a retrograde vesicle tethering factor in intra-Golgi trafficking. The COG protein complex consists of eight subunits, distributed in two lobes, Lobe A (Cog1-4) and Lobe B (Cog5-8). Malfunctions in the COG complex have a significant impact on processes such as protein sorting, glycosylation, and Golgi integrity. A deletion of Lobe A COG subunits in yeasts causes severe growth defects while mutations in COG1, COG7, and COG8 in humans cause novel types of congenital disorders of glycosylation. These pathologies involve a change in structural Golgi phenotype and function. Recent results indicate that down-regulation of COG function results in the resident Golgi glycosyltransferases/glycosidases to be mislocalized or degraded.

Indexed as

GlycosylationAdaptor Proteins, Vesicular TransportAnimalsCarbohydrate Metabolism, Inborn ErrorsGolgi ApparatusHumansProteinsSaccharomyces cerevisiaeAdaptor Proteins, Vesicular TransportCOG8 protein, humanProteins

Identifiers

PMID18353293
PMCPMC2773262
OpenAlexW1982264399

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.