The DOI matches its Crossref record; 79 of the 79 references it cites were found in a registry or an index.
The Claudins: From Tight Junctions to Biological Systems
Open accessAbstract
Claudins are cell-cell adhesion molecules located at the tight junctions (TJs) between cells in epithelial cell sheets. The claudin family in mammals consists of 27 four-transmembrane domain proteins. Claudins are responsible for the paracellular barrier function of TJs, and in some cases confer paracellular channel functions to the paracellular barriers of TJs. Based on recent breakthroughs in the molecular structure of claudins, the hypothetical 'antiparallel double row model' was proposed, which suggests how claudins polymerize in a linear fashion and form TJ strands with paracellular barrier and channel functions. Meanwhile, ongoing studies at the cell and tissue levels are clarifying how the paracellular barrier and/or channel functions of claudin-based TJs, which are both robust and flexible, organize various biological systems.
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Cites
JUNCTIONAL COMPLEXES IN VARIOUS EPITHELIA
Farquhar, M. G., & Palade, G. E. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.17.2.375 · Cited by 3,635
Occludin: a novel integral membrane protein localizing at tight junctions.
Furuse, M., Hirase, T., Itoh, M., Nagafuchi, A., Yonemura, S., Tsukita, S., & Tsukita, S. (1993) · The Journal of cell biology · doi:10.1083/jcb.123.6.1777 · Cited by 2,580
Self-citationMultifunctional strands in tight junctions
Tsukita, S., Furuse, M., & Itoh, M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35067088 · Cited by 2,509
Self-citationFuruse, M., Fujita, K., Hiiragi, T., Fujimoto, K., & Tsukita, S. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.7.1539 · Cited by 2,095
Self-citationClaudin-based tight junctions are crucial for the mammalian epidermal barrier
Furuse, M., Hata, M., Furuse, K., Yoshida, Y., Haratake, A., Sugitani, Y., Noda, T., Kubo, A., & Tsukita, S. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200110122 · Cited by 1,512
Self-citationClaudins and the Modulation of Tight Junction Permeability
Günzel, D., & Yu, A. S. L. (2013) · Physiological Reviews · doi:10.1152/physrev.00019.2012 · Cited by 1,456
Complex Phenotype of Mice Lacking Occludin, a Component of Tight Junction Strands
Saitou, M., Furuse, M., Sasaki, H., Schulzke, J.-D., Fromm, M., Takano, H., Noda, T., & Tsukita, S. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.12.4131 · Cited by 1,195
Self-citationParacellin-1, a Renal Tight Junction Protein Required for Paracellular Mg 2+ Resorption
Simon, D. B., Lu, Y., Choate, K. A., Velazquez, H., Al-Sabban, E., Praga, M., Casari, G., Bettinelli, A., Colussi, G., Rodriguez-Soriano, J., et al. (1999) · Science · doi:10.1126/science.285.5424.103 · Cited by 1,147
FRACTURE FACES OF ZONULAE OCCLUDENTES FROM "TIGHT" AND "LEAKY" EPITHELIA
Claude, P., & Goodenough, D. A. (1973) · The Journal of Cell Biology · doi:10.1083/jcb.58.2.390 · Cited by 1,096
Social stress induces neurovascular pathology promoting depression
Menard, C., Pfau, M. L., Hodes, G. E., Kana, V., Wang, V. X., Bouchard, S., Takahashi, A., Flanigan, M. E., Aleyasin, H., LeClair, K. B., et al. (2017) · Nature Neuroscience · doi:10.1038/s41593-017-0010-3 · Cited by 1,028
Cited by
Tight junctions as targets and effectors of mucosal immune homeostasis
Zuo, L., Kuo, W.-T., & Turner, J. R. (2020) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2020.04.001 · Cited by 191
Do Bacteria Provide an Alternative to Cancer Treatment and What Role Does Lactic Acid Bacteria Play?
Dicks, L. M. T., & Vermeulen, W. (2022) · Microorganisms · doi:10.3390/microorganisms10091733 · Cited by 25
Multi-modal quantification of pathway activity with MAYA
Landais, Y., & Vallot, C. (2023) · Nature Communications · doi:10.1038/s41467-023-37410-2 · Cited by 9
Design principles of a membrane-spanning ubiquitin ligase
Williams, C., Nocka, L. M., Hedger, G., Parashara, P., Pardon, E., Latorraca, N. R., Pusapati, G. V., Sarkar, P., Lartey, D., Gao, L., et al. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.05.001 · Cited by 3
Metadata
- Authors
- Tsukita, S., Tanaka, H., & Tamura, A.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2019-02
- Volume
- 44
- Issue
- 2
- Pages
- 141-152
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2898469163
- Cited by
- 470
- References
- 79
- FWCI
- 3.59
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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