The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
Glycine receptors: recent insights into their structural organization and functional diversity
Abstract
Strychnine‐sensitive glycine receptors (GlyRs) are known to mediate synaptic inhibition in spinal cord, brainstem and other regions of the CNS. During the past 5 years, considerable progress has been made in delineating structural determinants of ligand binding and channel activation in recombinant GlyRs. Furthermore, immunohistochemical and gene inactivation studies have disclosed distinct distributions and functions of differentially expressed GlyR subtypes in retina, hippocampus and the dorsal horn of the spinal cord. Accordingly, GlyRs regulate not only the excitability of motor and sensory neurones, but are also essential for the processing of photoreceptor signals, neuronal development and inflammatory pain sensitization. Hence, these receptors constitute promising targets for the development of clinically useful compounds.
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Cites
The K+/Cl− co-transporter KCC2 renders GABA hyperpolarizing during neuronal maturation
Rivera, C., Voipio, J., Payne, J. A., Ruusuvuori, E., Lahtinen, H., Lamsa, K., Pirvola, U., Saarma, M., & Kaila, K. (1999) · Nature · doi:10.1038/16697 · Cited by 2,152
Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
Brejc, K., van Dijk, W. J., Klaassen, R. V., Schuurmans, M., van der Oost, J., Smit, A. B., & Sixma, T. K. (2001) · Nature · doi:10.1038/35077011 · Cited by 1,759
Refined Structure of the Nicotinic Acetylcholine Receptor at 4Å Resolution
Unwin, N. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.12.031 · Cited by 1,659
Diffusion Dynamics of Glycine Receptors Revealed by Single-Quantum Dot Tracking
Dahan, M., Lévi, S., Luccardini, C., Rostaing, P., Riveau, B., & Triller, A. (2003) · Science · doi:10.1126/science.1088525 · Cited by 1,474
Structure and gating mechanism of the acetylcholine receptor pore
Miyazawa, A., Fujiyoshi, Y., & Unwin, N. (2003) · Nature · doi:10.1038/nature01748 · Cited by 1,270
Parallel processing in the mammalian retina
Wässle, H. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1497 · Cited by 1,252
Nicotinic Receptors at the Amino Acid Level
Corringer, P.-J., Novère, N. L., & Changeux, J.-P. (2000) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.40.1.431 · Cited by 820
Molecular Structure and Function of the Glycine Receptor Chloride Channel
Lynch, J. W. (2004) · Physiological Reviews · doi:10.1152/physrev.00042.2003 · Cited by 778
GlyR α3: An Essential Target for Spinal PGE 2 -Mediated Inflammatory Pain Sensitization
Harvey, R. J., Depner, U. B., Wässle, H., Ahmadi, S., Heindl, C., Reinold, H., Smart, T. G., Harvey, K., Schütz, B., Abo-Salem, O. M., et al. (2004) · Science · doi:10.1126/science.1094925 · Cited by 598
Self-citationWidespread expression of glycine receptor subunit mRNAs in the adult and developing rat brain.
Malosio, M. L., Marquèze-Pouey, B., Kuhse, J., & Betz, H. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07779.x · Cited by 552
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Cited by
Molecular Targets of the Phytocannabinoids: A Complex Picture
Morales, P., Hurst, D. P., & Reggio, P. H. (2017) · Progress in the Chemistry of Organic Natural Products · doi:10.1007/978-3-319-45541-9_4 · Cited by 454
Ubiquitination in postsynaptic function and plasticity
Mabb, A. M., & Ehlers, M. D. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100109-104129 · Cited by 255
Mechanisms of Inhibition within the Telencephalon: “Where the Wild Things Are”
Fishell, G., & Rudy, B. (2011) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-061010-113717 · Cited by 233
Glycine transporters and synaptic function
Zafra, F., & Giménez, C. (2008) · IUBMB Life · doi:10.1002/iub.128 · Cited by 73
Metadata
- Authors
- Betz, H., & Laube, B.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2006-06
- Volume
- 97
- Issue
- 6
- Pages
- 1600-1610
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2101630258
- Cited by
- 288
- References
- 65
- FWCI
- 9.60
- Type
- journal article
- Language
- en
- Open access
- closed
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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.