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Cited by 1,850

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Klotho converts canonical FGF receptor into a specific receptor for FGF23

Urakawa, Itaru, Yamazaki, Yuji, Shimada, Takashi, Iijima, Kousuke, Hasegawa, Hisashi, Okawa, Katsuya, Fujita, Toshiro, Fukumoto, Seiji, Yamashita, Takeyoshi·2006·Nature
DOI 10.1038/nature05315
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Citations

Cites

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Research works printed but not linked: 27

  1. The ADHR Consortium. Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23. Nature Genet. 26, 345–348 (2000) · DOI · Paper page
  2. Shimada, T. et al. Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia. Proc. Natl Acad. Sci. USA 98, 6500–6505 (2001) · DOI · Paper page
  3. Itoh, N. & Ornitz, D. M. Evolution of the Fgf and Fgfr gene families. Trends Genet. 20, 563–569 (2004) · DOI · Paper page
  4. Yamazaki, Y. et al. Increased circulatory level of biologically active full-length FGF-23 in patients with hypophosphatemic rickets/osteomalacia. J. Clin. Endocrinol. Metab. 87, 4957–4960 (2002) · DOI · Paper page
  5. Jonsson, K. B. et al. Fibroblast growth factor 23 in oncogenic osteomalacia and X-linked hypophosphatemia. N. Engl. J. Med. 348, 1656–1663 (2003) · DOI · Paper page
  6. Shimada, T. et al. FGF-23 is a potent regulator of vitamin D metabolism and phosphate homeostasis. J. Bone Miner. Res. 19, 429–435 (2004) · DOI · Paper page
  7. Riminucci, M. et al. FGF-23 in fibrous dysplasia of bone and its relationship to renal phosphate wasting. J. Clin. Invest. 112, 683–692 (2003) · DOI · Paper page
  8. Murer, H., Hernando, N., Forster, I. & Biber, J. Proximal tubular phosphate reabsorption: molecular mechanisms. Physiol. Rev. 80, 1373–1409 (2000) · DOI · Paper page
  9. Wikvall, K. Cytochrome P450 enzymes in the bioactivation of vitamin D to its hormonal form. Int. J. Mol. Med. 7, 201–209 (2001) · doi:10.1007/s008940100035
  10. Gashler, A. & Sukhatme, V. P. Early growth response protein 1 (Egr-1): prototype of a zinc-finger family of transcription factors. Prog. Nucleic Acid Res. Mol. Biol. 50, 191–224 (1995) · DOI · Paper page
  11. Liu, L., Tsai, J. C. & Aird, W. C. Egr-1 gene is induced by the systemic administration of the vascular endothelial growth factor and the epidermal growth factor. Blood 96, 1772–1781 (2000) · DOI
  12. Nabeshima, Y. Klotho: a fundamental regulator of aging. Ageing Res. Rev. 1, 627–638 (2002) · DOI
  13. Imura, A. et al. Secreted Klotho protein in sera and CSF: implication for post-translational cleavage in release of Klotho protein from cell membrane. FEBS Lett. 565, 143–147 (2004) · DOI · Paper page
  14. Yu, X. et al. Analysis of the biochemical mechanisms for the endocrine actions of fibroblast growth factor-23. Endocrinology 146, 4647–4656 (2005) · DOI · Paper page
  15. Yamashita, T., Konishi, M., Miyake, A., Inui, K. & Itoh, N. Fibroblast growth factor (FGF)-23 inhibits renal phosphate reabsorption by activation of the mitogen-activated protein kinase pathway. J. Biol. Chem. 277, 28265–28270 (2002) · DOI
  16. Christy, B. A., Lau, L. F. & Nathans, D. A gene activated in mouse 3T3 cells by serum growth factors encodes a protein with ‘zinc finger’ sequences. Proc. Natl Acad. Sci. USA 85, 7857–7861 (1988) · DOI · Paper page
  17. Shimada, T. et al. Targeted ablation of Fgf23 demonstrates an essential physiological role of FGF23 in phosphate and vitamin D metabolism. J. Clin. Invest. 113, 561–568 (2004) · DOI
  18. Sitara, D. et al. Homozygous ablation of fibroblast growth factor-23 results in hyperphosphatemia and impaired skeletogenesis, and reverses hypophosphatemia in Phex-deficient mice. Matrix Biol. 23, 421–432 (2004) · DOI · Paper page
  19. Yoshida, T., Fujimori, T. & Nabeshima, Y. Mediation of unusually high concentrations of 1,25-dihydroxyvitamin D in homozygous klotho mutant mice by increased expression of renal 1α-hydroxylase gene. Endocrinology 143, 683–689 (2002) · DOI · Paper page
  20. Tsujikawa, H., Kurotaki, Y., Fujimori, T., Fukuda, K. & Nabeshima, Y. Klotho, a gene related to a syndrome resembling human premature aging, functions in a negative regulatory circuit of vitamin D endocrine system. Mol. Endocrinol. 17, 2393–2403 (2003) · DOI · Paper page
  21. Vainikka, S. et al. Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1. J. Biol. Chem. 269, 18320–18326 (1994) · DOI
  22. Ornitz, D. M. & Itoh, N. Fibroblast growth factors. Genome Biol. 2, 3005.1–3005.12 (2001) · DOI
  23. Ito, S. et al. Molecular cloning and expression analyses of mouse betaklotho, which encodes a novel Klotho family protein. Mech. Dev. 98, 115–119 (2000) · DOI · Paper page
  24. Ito, S., Fujimori, T., Hayashizaki, Y. & Nabeshima, Y. Identification of a novel mouse membrane-bound family 1 glycosidase-like protein, which carries an atypical active site structure. Biochim. Biophys. Acta 1576, 341–345 (2002) · DOI
  25. Holt, J. A. et al. Definition of a novel growth factor-dependent signal cascade for the suppression of bile acid biosynthesis. Genes Dev. 17, 1581–1591 (2003) · DOI · Paper page
  26. Ito, S. et al. Impaired negative feedback suppression of bile acid synthesis in mice lacking betaKlotho. J. Clin. Invest. 115, 2202–2208 (2005) · DOI · Paper page
  27. Shimada, T. et al. Mutant FGF-23 responsible for autosomal dominant hypophosphatemic rickets is resistant to proteolytic cleavage and causes hypophosphatemia in vivo.. Endocrinology 143, 3179–3182 (2002) · doi:10.1210/endo.143.8.8795 · Paper page

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Metadata

Authors
Urakawa, I., Yamazaki, Y., Shimada, T., Iijima, K., Hasegawa, H., Okawa, K., Fujita, T., Fukumoto, S., & Yamashita, T.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2006-10-29
Volume
444
Issue
7120
Pages
770-774
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
DOI
10.1038/nature05315
OpenAlex
W2091948921
Cited by
1,850
References
3
FWCI
48.11
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)

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CoChat. (2026). Citation check: Klotho converts canonical FGF receptor into a specific receptor for FGF23. https://app.cochat.ai/papers/10.1038/nature05315
The paper
Urakawa, I., Yamazaki, Y., Shimada, T., Iijima, K., Hasegawa, H., Okawa, K., Fujita, T., Fukumoto, S., & Yamashita, T. (2006). Klotho converts canonical FGF receptor into a specific receptor for FGF23. Nature. https://doi.org/10.1038/nature05315

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