Evidence map›Paper›PMID 21550242›Full record

ReviewTrends in cell biology2011

Fusing a lasting relationship between ER tubules.

Tyler J Moss, Andrea Daga, James A McNew

Open access · greenAbstract readReview
In one paragraph

Review in Trends in cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Membrane fusion byMolecular biology of the cell · 2022
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Dynamin, a membrane-remodelling GTPase.Nature reviews. Molecular cell biology · 2012
    Review
  16. Review
  17. 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

3 authors at 2 institutions in 2 countries.

Tyler J MossDepartment of Biochemistry and Cell Biology, Rice University, MS601, Houston, TX 77005, USA.
Andrea Daga
James A McNew
Rice University · USIRCCS Eugenio Medea · IT

Funding

Functional Reconstitution of Yeast ExocytosisR01GM071832 · NIGMS · RICE UNIVERSITY · PI MCNEW, JAMES A · 2006 to 2010
$1.4M
NIGMS NIH HHS GM071832NIGMS NIH HHS R01 GM071832Telethon TCR08004
6 · The paper itself

Abstract

Atlastin is an integral membrane GTPase localized to the endoplasmic reticulum (ER). In vitro and in vivo analyses indicate that atlastin is a membrane fusogen capable of driving membrane fusion, suggesting a role in ER structure and maintenance. Interestingly, mutations in the human atlastin-1 gene, SPG3A, cause a form of autosomal dominant hereditary spastic paraplegia (HSP). The etiology of HSP is unclear, but two predominant forms of the disorder are caused by mutant proteins that affect ER structure, formation and maintenance in motor neurons. In this review, we describe the current knowledge about the molecular mechanism of atlastin function and its potential role in HSP. Greater understanding of the function of atlastin and associated proteins should provide important insight into normal ER biogenesis and maintenance, as well as the pathology of disease.

Indexed as

AnimalsEndoplasmic ReticulumGTP-Binding ProteinsHumansMembrane FusionMembrane ProteinsSpastic Paraplegia, HereditaryATL1 protein, humanGTP-Binding ProteinsMembrane Proteins

Identifiers

PMID21550242
PMCPMC3128651
OpenAlexW2082732776

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.