Evidence map›Paper›PMID 21436057›Full record

ReviewCold Spring Harbor perspectives in biology2011

The golgin coiled-coil proteins of the Golgi apparatus.

Sean Munro

Abstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
–field-weighted citation impact
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

137 citing papers in PubMed.

  1. Review
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  17. Review
  18. Comparative analysis of new, mScarlet-based red fluorescent tags inbioRxiv : the preprint server for biology · 2024
    Article
  19. Article
  20. Review

77 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

1 author.

Sean MunroMRC Laboratory of Molecular Biology, Cambridge, United Kingdom. sean@mrc-lmb.cam.ac.uk

Funding

Medical Research Council MC_U105178783
6 · The paper itself

Abstract

A number of long coiled-coil proteins are present on the Golgi. Often referred to as "golgins," they are well conserved in evolution and at least five are likely to have been present in the last common ancestor of all eukaryotes. Individual golgins are found in different parts of the Golgi stack, and they are typically anchored to the membrane at their carboxyl termini by a transmembrane domain or by binding a small GTPase. They appear to have roles in membrane traffic and Golgi structure, but their precise function is in most cases unclear. Many have binding sites for Rab family GTPases along their length, and this has led to the suggestion that the golgins act collectively to form a tentacular matrix that surrounds the Golgi to capture Rab-coated membranes in the vicinity of the stack. Such a collective role might explain the lack of cell lethality seen following loss of some of the genes in human familial conditions or mouse models.

Indexed as

Models, MolecularAutoantigensBinding SitesCarrier ProteinsGolgi ApparatusHumansMembrane ProteinsMonomeric GTP-Binding ProteinsProtein Structure, TertiaryProtein Transportrab GTP-Binding ProteinsAutoantigensCarrier ProteinsGolgin subfamily A member 2Membrane ProteinsMonomeric GTP-Binding Proteinsrab GTP-Binding Proteins

Identifiers

PMID21436057
PMCPMC3098672

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.