Evidence map›Paper›PMID 18064415›Full record

ReviewHandbook of experimental pharmacology2008

alpha-Latrotoxin and its receptors.

Yuri A Ushkaryov, Alexis Rohou, Shuzo Sugita

Open access · greenAbstract readReview
In one paragraph

Review in Handbook of experimental pharmacology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
10.5field-weighted citation impact, top 2% 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

44 citing papers in PubMed, 112 citations in OpenAlex.

  1. Review
  2. The Mechanism of LTXInternational journal of molecular sciences · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Pain-related toxins in scorpion and spider venoms: a face to face with ion channels.The journal of venomous animals and toxins including tropical diseases · 2021
    Review
  17. Widow spiders in the New World: a review onThe journal of venomous animals and toxins including tropical diseases · 2021
    Article
  18. Spider bites of medical significance in the Mediterranean area: misdiagnosis, clinical features and management.The journal of venomous animals and toxins including tropical diseases · 2020
    Review
  19. Review
  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 2 institutions in 2 countries.

Yuri A UshkaryovDivision of Cell and Molecular Biology, Imperial College London, London, SW7 2AY, UK. y.ushkaryov@imperial.ac.uk
Alexis Rohou
Shuzo Sugita
Imperial College London · GBToronto Western Hospital · CA

Funding

Biotechnology and Biological Sciences Research Council BB/D523078/1Wellcome Trust 074359
6 · The paper itself

Abstract

alpha-Latrotoxin (alpha-LTX) from black widow spider venom induces exhaustive release of neurotransmitters from vertebrate nerve terminals and endocrine cells. This 130-kDa protein has been employed for many years as a molecular tool to study exocytosis. However, its action is complex: in neurons, alpha-LTX induces massive secretion both in the presence of extracellular Ca(2+) (Ca(2+) (e)) and in its absence; in endocrine cells, it usually requires Ca(2+) (e). To use this toxin for further dissection of secretory mechanisms, one needs an in-depth understanding of its functions. One such function that explains some alpha-LTX effects is its ability to form cation-permeable channels in artificial lipid bilayers. The mechanism of alpha-LTX pore formation, revealed by cryo-electron microscopy, involves toxin assembly into homotetrameric complexes which harbor a central channel and can insert into lipid membranes. However, in biological membranes, alpha-LTX cannot exert its actions without binding to specific receptors of the plasma membrane. Three proteins with distinct structures have been found to bind alpha-LTX: neurexin Ialpha, latrophilin 1, and receptor-like protein tyrosine phosphatase sigma. Upon binding a receptor, alpha-LTX forms channels permeable to cations and small molecules; the toxin may also activate the receptor. To distinguish between the pore- and receptor-mediated effects, and to study structure-function relationships in the toxin, alpha-LTX mutants have been used.

Indexed as

AnimalsCalciumCell MembraneHumansModels, MolecularMolecular ConformationNeurotransmitter AgentsReceptor-Like Protein Tyrosine Phosphatases, Class 3Receptors, DrugReceptors, PeptideRecombinant ProteinsSignal TransductionSpider Venomsalpha-latrotoxinalpha-latrotoxin receptorCalciumNeurotransmitter AgentsReceptor-Like Protein Tyrosine Phosphatases, Class 3Receptors, DrugReceptors, PeptideRecombinant ProteinsSpider Venoms

Identifiers

PMID18064415
PMCPMC2519134
OpenAlexW147969435

What Socratic 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 Socratic graph.