Evidence map›Paper›PMID 15649133›Full record

ReviewBiochemical Society symposium2005

Dynamin I phosphorylation and the control of synaptic vesicle endocytosis.

Karen J Smillie, Michael A Cousin

Open access · greenAbstract readReview
In one paragraph

Review in Biochemical Society symposium, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

23 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Regulation of Clathrin-Mediated Endocytosis.Annual review of biochemistry · 2018
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Differential curvature sensing and generating activities of dynamin isoforms provide opportunities for tissue-specific regulation.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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 at 1 institution in 1 country.

Karen J SmillieMembrane Biology Group, Division of Biomedical Sciences, University of Edinburgh, George Square, Edinburgh EH8 9XD, U.K.
Michael A Cousin
University of Edinburgh · GB

Funding

Wellcome Trust 070569
6 · The paper itself

Abstract

The GTPase dynamin I is essential for synaptic vesicle endocytosis in nerve terminals. It is a nerve terminal phosphoprotein that is dephosphorylated on nerve terminal stimulation by the calcium-dependent protein phosphatase calcineurin and then rephosphorylated by cyclin-dependent kinase 5 on termination of the stimulus. Because of its unusual phosphorylation profile, the phosphorylation status of dynamin I was assumed to be inexorably linked to synaptic vesicle endocytosis; however, direct proof of this link has been elusive until very recently. This review will describe current knowledge regarding dynamin I phosphorylation in nerve terminals and how this regulates its biological function with respect to synaptic vesicle endocytosis.

Indexed as

Amino Acid SequenceAnimalsCalcineurinCyclin-Dependent Kinase 5Cyclin-Dependent KinasesDynamin IEndocytosisHumansModels, NeurologicalMolecular Sequence DataMolecular StructurePhosphorylationProtein Structure, TertiarySynaptic VesiclesCalcineurinCDK5 protein, humanCyclin-Dependent Kinase 5Cyclin-Dependent KinasesDynamin I

Identifiers

PMID15649133
PMCPMC2077358
OpenAlexW1212078

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.