Evidence map›Paper›PMID 21813399›Full record

ReviewCold Spring Harbor perspectives in biology2011

Structure of Golgi transport proteins.

Daniel Kümmel, Karin M Reinisch

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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
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.

Daniel KümmelDepartment of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Karin M Reinisch

Funding

Regulatory Mechanisms in Membrane TraffickingR01GM080616 · NIGMS · YALE UNIVERSITY · PI REINISCH, KARIN M · 2007 to 2018
$4.1M
NIGMS NIH HHS R01 GM080616
6 · The paper itself

Abstract

The function of the Golgi has long been recognized to critically depend on vesicular transport from, to, and within its cisternae, involving constant membrane fission and fusion. These processes are mediated by Arf GTPases and coat proteins, and Rabs, tethers and SNARE proteins, respectively. In this article, we describe structural studies of Golgi coats and tethers and their interactions with SNAREs and GTPases as well as insights regarding membrane traffic processes that these have provided.

Indexed as

Clathrin-Coated VesiclesFungal ProteinsGolgi ApparatusHumansMembrane ProteinsModels, BiologicalProtein Structure, TertiaryProtein TransportVesicular Transport ProteinsFungal ProteinsMembrane ProteinsVesicular Transport Proteins

Identifiers

PMID21813399
PMCPMC3225946

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.