Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 223

The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.

Molecular and functional properties of P2X receptors—recent progress and persisting challenges

Open access
Kaczmarek-Hájek, Karina, Lörinczi, Éva, Hausmann, Ralf, Nicke, Annette·2012·Purinergic Signalling

Abstract

ATP-gated P2X receptors are trimeric ion channels that assemble as homo- or heteromers from seven cloned subunits. Transcripts and/or proteins of P2X subunits have been found in most, if not all, mammalian tissues and are being discovered in an increasing number of non-vertebrates. Both the first crystal structure of a P2X receptor and the generation of knockout (KO) mice for five of the seven cloned subtypes greatly advanced our understanding of their molecular and physiological function and their validation as drug targets. This review summarizes the current understanding of the structure and function of P2X receptors and gives an update on recent developments in the search for P2X subtype-selective ligands. It also provides an overview about the current knowledge of the regulation and modulation of P2X receptors on the cellular level and finally on their physiological roles as inferred from studies on KO mice.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1007/s11302-012-9314-7

Cites

18 of 18 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 18 references

Cited by

See all 223

Metadata

Authors
Kaczmarek-Hájek, K., Lörinczi, É., Hausmann, R., & Nicke, A.
Venue
Purinergic Signalling
Published
2012-05-01
Volume
8
Issue
3
Pages
375-417
ISSN
  • 1573-9538 (ISSN-L)
  • 1573-9546
OpenAlex
W2036287567
Cited by
223
References
18
FWCI
13.48
Type
journal article
Language
en
Open access
hybrid

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Molecular and functional properties of P2X receptors—recent progress and persisting challenges. https://app.cochat.ai/papers/10.1007/s11302-012-9314-7
The paper
Kaczmarek-Hájek, K., Lörinczi, É., Hausmann, R., & Nicke, A. (2012). Molecular and functional properties of P2X receptors—recent progress and persisting challenges. Purinergic Signalling. https://doi.org/10.1007/s11302-012-9314-7

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.