Evidence map›Paper›PMID 11980916›Full record

ArticleThe Journal of cell biology2002

Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function.

Daniel Ungar, Toshihiko Oka, Elizabeth E Brittle, Eliza Vasile, Vladimir V Lupashin, Jon E Chatterton, John E Heuser, Monty Krieger, M Gerard Waters

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
136citing papers in PubMed, 1 pooled it
4.7field-weighted citation impact, top 5% 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

136 citing papers in PubMed, 1 synthesis or guideline pooled it, 290 citations in OpenAlex.

  1. Pooled it
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  5. Article
  6. Article
  7. Review
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  18. Review
  19. Tumor TargetingMicroRNA (Shariqah, United Arab Emirates) · 2024
    Article
  20. Article

76 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

9 authors at 5 institutions in 1 country.

Daniel UngarDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
Toshihiko Oka
Elizabeth E Brittle
Eliza Vasile
Vladimir V Lupashin
Jon E Chatterton
John E Heuser
Monty Krieger
M Gerard Waters
Massachusetts Institute of Technology · USPrinceton University · USBeth Israel Deaconess Medical Center · USUniversity of Arkansas for Medical Sciences · USWashington University in St. Louis · US

Funding

STRUCTURAL ANALYSIS OF CLATHRIN-MEDIATED ENDOCYTOSISR01GM029647 · NIGMS · WASHINGTON UNIVERSITY · PI HEUSER, JOHN EDWARD · 1985 to 2008
$4.8M
GENES CONTROLLING LDL RECEPTOR STRUCTURE AND FUNCTIONR01GM059115 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KRIEGER, MONTY · 2000 to 2003
$1.1M
STRUCTURE/FUNCTION OF GTC, A NOVEL GOLGI PROTEIN COMPLEXR01GM059280 · NIGMS · PRINCETON UNIVERSITY · PI HUGHSON, FREDERICK M · 1999 to 2002
$609k
NIGMS NIH HHS GM29647NIGMS NIH HHS GM59115NIGMS NIH HHS GM59280NIGMS NIH HHS R01 GM029647NIGMS NIH HHS R01 GM059115
6 · The paper itself

Abstract

Multiprotein complexes are key determinants of Golgi apparatus structure and its capacity for intracellular transport and glycoprotein modification. Three complexes that have previously been partially characterized include (a) the Golgi transport complex (GTC), identified in an in vitro membrane transport assay, (b) the ldlCp complex, identified in analyses of CHO cell mutants with defects in Golgi-associated glycosylation reactions, and (c) the mammalian Sec34 complex, identified by homology to yeast Sec34p, implicated in vesicular transport. We show that these three complexes are identical and rename them the conserved oligomeric Golgi (COG) complex. The COG complex comprises four previously characterized proteins (Cog1/ldlBp, Cog2/ldlCp, Cog3/Sec34, and Cog5/GTC-90), three homologues of yeast Sec34/35 complex subunits (Cog4, -6, and -8), and a previously unidentified Golgi-associated protein (Cog7). EM of ldlB and ldlC mutants established that COG is required for normal Golgi morphology. "Deep etch" EM of purified COG revealed an approximately 37-nm-long structure comprised of two similarly sized globular domains connected by smaller extensions. Consideration of biochemical and genetic data for mammalian COG and its yeast homologue suggests a model for the subunit distribution within this complex, which plays critical roles in Golgi structure and function.

Indexed as

Adaptor Proteins, Vesicular TransportAnimalsCarrier ProteinsCell LineCloning, MolecularConserved SequenceGolgi ApparatusHumansMacromolecular SubstancesMembrane ProteinsMultiprotein ComplexesMutationProtein ConformationProteinsProtein SubunitsRatsAdaptor Proteins, Vesicular TransportCarrier ProteinsCOG1 protein, humanCOG2 protein, humanCOG3 protein, humanCOG3 protein, S cerevisiaeMacromolecular SubstancesMembrane ProteinsMultiprotein ComplexesProteinsProtein SubunitsSaccharomyces cerevisiae Proteins

Identifiers

PMID11980916
PMCPMC2173297
OpenAlexW2013702818

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.