Evidence map›Paper›PMID 11823417›Full record

ArticleThe EMBO journal2002

The dynamin A ring complex: molecular organization and nucleotide-dependent conformational changes.

Boris Klockow, Willem Tichelaar, Dean R Madden, Hartmut H Niemann, Toshihiko Akiba, Keiko Hirose, Dietmar J Manstein

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Frontiers in cell and developmental biology · 2021
    Review
  3. Article
  4. Review
  5. Nucleotide-dependent farnesyl switch orchestrates polymerization and membrane binding of human guanylate-binding protein 1.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. ARC5, a cytosolic dynamin-like protein from plants, is part of the chloroplast division machinery.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  17. Mitochondrial membrane dynamics are altered in cluA- mutants of Dictyostelium.Journal of muscle research and cell motility · 2002
    Article
  18. Neurotransmission and the synaptic vesicle cycle.The Yale journal of biology and medicine
    Review
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

7 authors at 2 institutions in 3 countries.

Boris KlockowDepartment of Biophysics, Max-Planck-Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany.
Willem Tichelaar
Dean R Madden
Hartmut H Niemann
Toshihiko Akiba
Keiko Hirose
Dietmar J Manstein
Max Planck Institute for Medical Research · DENational Institute of Advanced Industrial Science and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here we show that Dictyostelium discoideum dynamin A is a fast GTPase, binds to negatively charged lipids, and self-assembles into rings and helices in a nucleotide-dependent manner, similar to human dynamin-1. Chemical modification of two cysteine residues, positioned in the middle domain and GTPase effector domain (GED), leads to altered assembly properties and the stabilization of a highly regular ring complex. Single particle analysis of this dynamin A* ring complex led to a three-dimensional map, which shows that the nucleotide-free complex consists of two layers with 11-fold symmetry. Our results reveal the molecular organization of the complex and indicate the importance of the middle domain and GED for the assembly of dynamin family proteins. Nucleotide-dependent changes observed with the unmodified and modified protein support a mechanochemical action of dynamin, in which tightening and stretching of a helix contribute to membrane fission.

Indexed as

DynaminsGTP PhosphohydrolasesProtozoan ProteinsAnimalsDictyosteliumDimerizationHumansProtein Conformationdynamin A protein, Dictyostelium discoideumDynaminsGTP PhosphohydrolasesProtozoan Proteins

Identifiers

PMID11823417
PMCPMC125838
OpenAlexW1993846936

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.