The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
P2X1 and P2X3 receptors form stable trimers: a novel structural motif of ligand-gated ion channels
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Cites
Hollmann, M., & Heinemann, S. (1994) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.17.030194.000335 · Cited by 3,975
Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
Schägger, H., & von Jagow, G. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90094-a · Cited by 2,232
The Cytolytic P 2Z Receptor for Extracellular ATP Identified as a P 2X Receptor (P2X 7 )
Surprenant, A., Rassendren, F., Kawashima, E., North, R. A., & Buell, G. (1996) · Science · doi:10.1126/science.272.5262.735 · Cited by 1,739
Schagger, H., Cramer, W. A., & Vonjagow, G. (1994) · Analytical Biochemistry · doi:10.1006/abio.1994.1112 · Cited by 1,238
Purinoceptors: Are there families of P2X and P2Y purinoceptors?
Abbracchio, M. P., & Burnstock, G. (1994) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(94)00048-4 · Cited by 1,083
A new class of ligand-gated ion channel defined by P2X receptor for extracellular ATP
Valera, S., Hussy, N., Evans, R. J., Adami, N., North, R. A., Surprenant, A., & Buell, G. (1994) · Nature · doi:10.1038/371516a0 · Cited by 1,029
A P2X purinoceptor expressed by a subset of sensory neurons
Chen, C.-C., Akopian, A. N., Sivilottit, L., Colquhoun, D., Burnstock, G., & Wood, J. N. (1995) · Nature · doi:10.1038/377428a0 · Cited by 1,016
Acetylcholine receptor channel imaged in the open state
Unwin, N. (1995) · Nature · doi:10.1038/373037a0 · Cited by 999
Lewis, C., Neidhart, S., Holy, C., North, R. A., Buell, G., & Surprenant, A. (1995) · Nature · doi:10.1038/377432a0 · Cited by 997
Quality control in the secretory pathway
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Cited by
Kettenmann, H., Hanisch, U.-K., Noda, M., & Verkhratsky, A. (2011) · Physiological Reviews · doi:10.1152/physrev.00011.2010 · Cited by 3,547
Molecular Physiology of P2X Receptors
North, R. A. (2002) · Physiological Reviews · doi:10.1152/physrev.00015.2002 · Cited by 2,919
Khakh, B. S., Burnstock, G., Kennedy, C., King, B. F., North, R. A., Séguéla, P., Voigt, M., & Humphrey, P. P. A. (2001) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01482-0 · Cited by 667
Allosteric Receptors after 30 Years
Changeux, J.-P., & Edelstein, S. J. (1998) · Neuron · doi:10.1016/s0896-6273(00)80616-9 · Cited by 431
Molecular physiology of p2x receptors and atp signalling at synapses
Khakh, B. S. (2001) · Nature Reviews Neuroscience · doi:10.1038/35058521 · Cited by 363
Metadata
- Authors
- Nicke, A.
- Venue
- The EMBO Journal
- Published
- 1998-06-01
- Volume
- 17
- Issue
- 11
- Pages
- 3016-3028
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W2136134177
- Cited by
- 554
- References
- 61
- FWCI
- 18.05
- Type
- journal article
- Language
- en
- Open access
- green
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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.
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- CoChat. (2026). Citation check: P2X1 and P2X3 receptors form stable trimers: a novel structural motif of ligand-gated ion channels. https://app.cochat.ai/papers/10.1093/emboj/17.11.3016
- The paper
- Nicke, A. (1998). P2X1 and P2X3 receptors form stable trimers: a novel structural motif of ligand-gated ion channels. The EMBO Journal. https://doi.org/10.1093/emboj/17.11.3016
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.