Evidence map›Paper›PMID 17458635›Full record

ReviewProtoplasma2007

Annexins: putative linkers in dynamic membrane-cytoskeleton interactions in plant cells.

D Konopka-Postupolska

Abstract readReview
PubMed Publisher
In one paragraph

Review in Protoplasma, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Annexins as Overlooked Regulators of Membrane Trafficking in Plant Cells.International journal of molecular sciences · 2017
    Review
  5. Characterization of a Secretory Annexin in Echinococcus granulosus.The American journal of tropical medicine and hygiene · 2016
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

1 author at 1 institution in 1 country.

D Konopka-PostupolskaLaboratory of Plant Pathogenesis, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Institute of Biochemistry and Biophysics, Polish Academy of Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The plasma membrane, the most external cellular structure, is at the forefront between the plant cell and its environment. Hence, it is naturally adapted to function in detection of external signals, their transduction throughout the cell, and finally, in cell reactions. Membrane lipids and the cytoskeleton, once regarded as simple and static structures, have recently been recognized as significant players in signal transduction. Proteins involved in signal detection and transduction are organised in specific domains at the plasma membrane. Their aggregation allows to bring together and orient the downstream and upstream members of signalling pathways. The cortical cytoskeleton provides a structural framework for rapid signal transduction from the cell periphery into the nucleus. It leads to intracellular reorganisation and wide-scale modulation of cellular metabolism which results in accumulation of newly synthesised proteins and/or secondary metabolites which, in turn, have to be distributed to the appropriate cell compartments. And again, in plant cells, the secretory vesicles that govern polar cellular transport are delivered to their target membranes by interaction with actin microfilaments. In search for factors that could govern subsequent steps of the cell response delineated above we focused on an evolutionary conserved protein family, the annexins, that bind in a calcium-dependent manner to membrane phospholipids. Annexins were proposed to regulate dynamic changes in membrane architecture and to organise the interface between secretory vesicles and the membrane. Certain proteins from this family were also identified as actin binding, making them ideal mediators in cell membrane and cytoskeleton interactions.

Indexed as

Actin CytoskeletonAnnexinsCell MembraneCytoskeletonMembrane LipidsMolecular Sequence DataPlant ProteinsPlantsProtein TransportSequence Homology, Amino AcidSignal TransductionAnnexinsMembrane LipidsPlant Proteins

Identifiers

PMID17458635
OpenAlexW1966189858

What Socratic 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 Socratic graph.