Evidence map›Paper›PMID 28937994›Full record

ArticlePloS one2017

Modeling of annexin A2-Membrane interactions by molecular dynamics simulations.

Davit Hakobyan, Volker Gerke, Andreas Heuer

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.0field-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

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. CaProteins · 2023
    Article
  8. Review
  9. Annexin A7 mediates lysosome repair independently of ESCRT-III.Frontiers in cell and developmental biology · 2023
    Article
  10. Article
  11. Article
  12. Annexin A2 regulatesFrontiers in immunology · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  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

3 authors at 1 institution in 1 country.

Davit HakobyanInstitute of Physical Chemistry, University of Muenster, Muenster, Germany.ORCID http://orcid.org/0000-0001-7898-3260
Volker GerkeInstitute of Medical Biochemistry, Center of Molecular Biology of Inflammation (ZMBE), University of Muenster, Muenster, Germany.
Andreas HeuerInstitute of Physical Chemistry, University of Muenster, Muenster, Germany.
Institute of Molecular Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The annexins are a family of Ca2+-regulated phospholipid binding proteins that are involved in membrane domain organization and membrane trafficking. Although they are widely studied and crystal structures are available for several soluble annexins their mode of membrane association has never been studied at the molecular level. Here we obtained molecular information on the annexin-membrane interaction that could serve as paradigm for the peripheral membrane association of cytosolic proteins by Molecular Dynamics simulations. We analyzed systems containing the monomeric annexin A2 (AnxA2), a membrane with negatively charged phosphatidylserine (POPS) lipids as well as Ca2+ ions. On the atomic level we identify the AnxA2 orientations and the respective residues which display the strongest interaction with Ca2+ ions and the membrane. The simulation results fully agree with earlier experimental findings concerning the positioning of bound Ca2+ ions. Furthermore, we identify for the first time a significant interaction between lysine residues of the protein and POPS lipids that occurs independently of Ca2+ suggesting that AnxA2-membrane interactions can also occur in a low Ca2+ environment. Finally, by varying Ca2+ concentrations and lipid composition in our simulations we observe a calcium-induced negative curvature of the membrane as well as an AnxA2-induced lipid ordering.

Indexed as

Membranes, ArtificialMolecular Dynamics SimulationAnnexin A2CalciumCations, DivalentCytosolDimerizationPhosphatidylserinesProtein BindingSurface Properties1-palmitoyl-2-oleoylglycero-3-phosphoserineAnnexin A2CalciumCations, DivalentMembranes, ArtificialPhosphatidylserines

Identifiers

PMID28937994
PMCPMC5609761
OpenAlexW2758384014

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.