Evidence map›Paper›PMID 26245303›Full record

ReviewCellular and molecular life sciences : CMLS2015

Complexins: small but capable.

Ralf Mohrmann, Madhurima Dhara, Dieter Bruns

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

45 citing papers in PubMed, 70 citations in OpenAlex.

  1. Postsynaptic Complexin Mediates Constitutive Exocytosis of Nicotinic Acetylcholine Receptor.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Syntaxin 3B: A SNARE Protein Required for Vision.International journal of molecular sciences · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Dynamic Formation of the Protein-Lipid Pre-fusion Complex.bioRxiv : the preprint server for biology · 2024
    Article
  10. Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022
    Review
  18. Review
  19. Article
  20. Stochastic Properties of Spontaneous Synaptic Transmission at Individual Active Zones.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    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.

Ralf MohrmannZentrum für Human- und Molekularbiologie, University of Saarland, CIPMM, 66421, Homburg/Saar, Germany. ralf.mohrmann@uks.eu.
Madhurima DharaMedical Faculty, Department of Physiology, University of Saarland, CIPMM, 66421, Homburg/Saar, Germany.
Dieter BrunsMedical Faculty, Department of Physiology, University of Saarland, CIPMM, 66421, Homburg/Saar, Germany. dieter.bruns@uks.eu.
Saarland University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite intensive research, it is still unclear how an immediate and profound acceleration of exocytosis is triggered by appropriate Ca(2+)-stimuli in presynaptic terminals. This is due to the fact that the molecular mechanisms of "docking" and "priming" reactions, which set up secretory vesicles to fuse at millisecond time scale, are extremely hard to study. Yet, driven by a fruitful combination of in vitro and in vivo analyses, our mechanistic understanding of Ca(2+)-triggered vesicle fusion has certainly advanced in the past few years. In this review, we aim to highlight recent progress and emerging views on the molecular mechanisms, by which constitutively forming SNAREpins are organized in functional, tightly regulated units for synchronized release. In particular, we will focus on the role of the small regulatory factor complexin whose function in Ca(2+)-dependent exocytosis has been controversially discussed for more than a decade. Special emphasis will also be laid on the functional relationship of complexin and synaptotagmin, as both proteins possibly act as allies and/or antagonists to govern SNARE-mediated exocytosis.

Indexed as

ExocytosisAdaptor Proteins, Vesicular TransportCalciumHumansMembrane FusionModels, BiologicalNerve Tissue ProteinsProtein BindingSNARE ProteinsSynaptic VesiclesSynaptotagminsAdaptor Proteins, Vesicular TransportCalciumcomplexin INerve Tissue ProteinsSNARE ProteinsSynaptotagminsCa2+ triggered exocytosisComplexinMembrane fusionSNARE regulatorsSynaptotagmin

Identifiers

PMID26245303
PMCPMC4611016
OpenAlexW1067583755

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.