Evidence map›Paper›PMID 19290477›Full record

ReviewCellular and molecular life sciences : CMLS2009

Functions of actin in endocytosis.

Alastair S Robertson, Elizabeth Smythe, Kathryn R Ayscough

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Macropinosomes are a site of HIV-1 entry into primary CD4Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Global Deletome Profile ofFrontiers in microbiology · 2018
    Article
  14. Article
  15. Article
  16. WASP family proteins, more than Arp2/3 activators.Biochemical Society transactions · 2016
    Review
  17. Target shape dependence in a simple model of receptor-mediated endocytosis and phagocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Article
  19. Article
  20. Article

3 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

3 authors at 1 institution in 1 country.

Alastair S RobertsonDepartment of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.
Elizabeth Smythe
Kathryn R Ayscough
University of Sheffield · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0300452Medical Research Council G0601600
6 · The paper itself

Abstract

Endocytosis is a fundamental eukaryotic process required for remodelling plasma-membrane lipids and protein to ensure appropriate membrane composition. Increasing evidence from a number of cell types reveals that actin plays an active, and often essential, role at key endocytic stages. Much of our current mechanistic understanding of the endocytic process has come from studies in budding yeast and has been facilitated by yeast's genetic amenability and by technological advances in live cell imaging. While endocytosis in metazoans is likely to be subject to a greater array of regulatory signals, recent reports indicate that spatiotemporal aspects of vesicle formation requiring actin are likely to be conserved across eukaryotic evolution. In this review we focus on the 'modular' model of endocytosis in yeast before highlighting comparisons with other cell types. Our discussion is limited to endocytosis involving clathrin as other types of endocytosis have not been demonstrated in yeast.

Indexed as

ActinsAdaptor Proteins, Signal TransducingAnimalsCell MembraneClathrinEndocytosisHumansLipid MetabolismMicrofilament ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTransport VesiclesVesicular Transport ProteinsABP1 protein, S cerevisiaeActinsAdaptor Proteins, Signal TransducingClathrinHIP1R protein, humanMicrofilament ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport Proteins

Identifiers

PMID19290477
PMCPMC11115948
OpenAlexW2064681361

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.