Evidence map›Paper›PMID 22840778›Full record

ArticleChemistry & biology2012

Fluorescent saxitoxins for live cell imaging of single voltage-gated sodium ion channels beyond the optical diffraction limit.

Alison E Ondrus, Hsiao-lu D Lee, Shigeki Iwanaga, William H Parsons, Brian M Andresen, W E Moerner, J Du Bois

Abstract read
In one paragraph

Article in Chemistry & biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Article
  2. Saxiphilin is a broad-spectrum toxin sponge for C13-modified saxitoxins.bioRxiv : the preprint server for biology · 2026
    Article
  3. The Chemistry and Biology of the Tetrodotoxin Natural Product Family.Angewandte Chemie (International ed. in English) · 2025
    Review
  4. Article
  5. Trifunctional Saxitoxin Conjugates for Covalent Labeling of Voltage-Gated Sodium Channels.Chembiochem : a European journal of chemical biology · 2023
    Article
  6. Review
  7. Article
  8. Review
  9. Definition of a saxitoxin (STX) binding code enables discovery and characterization of the anuran saxiphilin family.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Review
  11. Review
  12. Article
  13. Taming unruly chloride channel inhibitors with rational design.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Article
  16. Review
  17. Dark dyes-bright complexes: fluorogenic protein labeling.Current opinion in chemical biology · 2015
    Review
  18. Article
  19. Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Alison E OndrusDepartment of Chemistry, Stanford University, 333 Campus Drive, Stanford, CA 94305-5080, USA.
Hsiao-lu D Lee
Shigeki Iwanaga
William H Parsons
Brian M Andresen
W E Moerner
J Du Bois

Funding

Subcellular architecture of regulatory protein complexes at the bacterial poleR01GM086196 · NIGMS · STANFORD UNIVERSITY · PI MOERNER, WILLIAM E, SHAPIRO, LUCILLE · 2008 to 2015
$4.7M
Reaction Design for the Synthesis of Neuroactive AgentsR01NS045684 · NINDS · STANFORD UNIVERSITY · PI DU BOIS, JUSTIN · 2003 to 2011
$3.0M
Guanidinium Toxins as Tools for Ion Channel StudyR56NS045684 · NINDS · STANFORD UNIVERSITY · PI DU BOIS, JUSTIN · 2012 to 2012
$511k
NIGMS NIH HHS R01 GM086196NIGMS NIH HHS R01-GM086196NINDS NIH HHS R01 NS045684NINDS NIH HHS R01-NS45684NINDS NIH HHS R56 NS045684
6 · The paper itself

Abstract

A desire to better understand the role of voltage-gated sodium channels (Na(V)s) in signal conduction and their dysregulation in specific disease states motivates the development of high precision tools for their study. Nature has evolved a collection of small molecule agents, including the shellfish poison (+)-saxitoxin, that bind to the extracellular pore of select Na(V) isoforms. As described in this report, de novo chemical synthesis has enabled the preparation of fluorescently labeled derivatives of (+)-saxitoxin, STX-Cy5, and STX-DCDHF, which display reversible binding to Na(V)s in live cells. Electrophysiology and confocal fluorescence microscopy studies confirm that these STX-based dyes function as potent and selective Na(V) labels. The utility of these probes is underscored in single-molecule and super-resolution imaging experiments, which reveal Na(V) distributions well beyond the optical diffraction limit in subcellular features such as neuritic spines and filopodia.

Indexed as

FluorescenceAnimalsDose-Response Relationship, DrugElectrophysiologyFluorescent DyesMicroscopy, ConfocalModels, MolecularMolecular StructurePC12 CellsRatsSaxitoxinSodium ChannelsStructure-Activity RelationshipFluorescent DyesSaxitoxinSodium Channels

Identifiers

PMID22840778
PMCPMC3731772

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.