Phosphate-sensing and regulatory mechanism of FGF23 production

Mutation of the mouse klotho gene leads to a syndrome resembling ageing

Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837 · see citing works

Cloning and characterization of an extracellular Ca2+-sensing receptor from bovine parathyroid

Brown, E. M., Gamba, G., Riccardi, D., Lombardi, M. J., Butters, R. R., Kifor, O., Sun, A. M., Hediger, M. A., Lytton, J., & Hébert, S. (1993) · Nature · doi:10.1038/366575a0 · Cited by 2,635 · see citing works

The Fibroblast Growth Factor signaling pathway

Ornitz, D. M., & Itoh, N. (2015) · WIREs Developmental Biology · doi:10.1002/wdev.176 · Cited by 2,050 · see citing works

FGF-23 Is a Potent Regulator of Vitamin D Metabolism and Phosphate Homeostasis

Shimada, T., Hasegawa, H., Yamazaki, Y., Muto, T., Hino, R., Takeuchi, Y., Fujita, T., Nakahara, K., Fukumoto, S., & Yamashita, T. (2004) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.0301264 · Cited by 1,883 · see citing works

Klotho converts canonical FGF receptor into a specific receptor for FGF23

Urakawa, I., Yamazaki, Y., Shimada, T., Iijima, K., Hasegawa, H., Okawa, K., Fujita, T., Fukumoto, S., & Yamashita, T. (2006) · Nature · doi:10.1038/nature05315 · Cited by 1,846 · see citing works

Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23

White, K., Evans, W. E., O'Riordan, J., Speer, M., Econs, M., Lorenz-Depiereux, B., Grabowski, M., Meitinger, T., & Strom, T. (2000) · Nature Genetics · doi:10.1038/81664 · Cited by 1,467 · see citing works

Phosphate Regulation of Vascular Smooth Muscle Cell Calcification

Jono, S., McKee, M. D., Murry, C. E., Shioi, A., Nishizawà, Y., Mori, K., Morii, H., & Giachelli, C. M. (2000) · Circulation Research · doi:10.1161/01.res.87.7.e10 · Cited by 1,425 · see citing works

Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia

Shimada, T., Mizutani, S., Muto, T., Yoneya, T., Hino, R., Takeda, S., Takeuchi, Y., Fujita, T., Fukumoto, S., & Yamashita, T. (2001) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.101545198 · Cited by 1,391 · see citing works

Regulation of Fibroblast Growth Factor-23 Signaling by Klotho*

Kurosu, H., Ogawa, Y., Miyoshi, M., Yamamoto, M., Nandi, A., Rosenblatt, K., Baum, M., Schiavi, S., Hu, M.-C., Moe, O., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c500457200 · Cited by 1,356 · see citing works

Loss of DMP1 causes rickets and osteomalacia and identifies a role for osteocytes in mineral metabolism

Feng, J. Q., Ward, L. M., Liu, S., Lu, Y., Xie, Y., Yuan, B., Yu, X., Rauch, F., Davis, S. I., Zhang, S., et al. (2006) · Nature Genetics · doi:10.1038/ng1905 · Cited by 1,199 · see citing works

Evolution of the Fgf and Fgfr gene families.

Itoh, N., & Ornitz, D. (2004) · Trends in Genetics · doi:10.1016/j.tig.2004.08.007 · Cited by 1,123 · see citing works

Control of mucin-type O-glycosylation: A classification of the polypeptide GalNAc-transferase gene family

Bennett, E. P., Mandel, U., Clausen, H., Gerken, T. A., Fritz, T. A., & Tabak, L. A. (2012) · Glycobiology · doi:10.1093/glycob/cwr182 · Cited by 876 · see citing works

Integrating signals from RTKs to ERK/MAPK

Mckay, M., & Morrison, D. K. (2007) · Oncogene · doi:10.1038/sj.onc.1210394 · Cited by 616 · see citing works

Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis

Topaz, O., Shurman, D. L., Bergman, R., Indelman, M., Ratajczak, P., Mizrachi-Koren, M., Khamaysi, Z., Behar, D. M., Petronius, D., Friedman, V., et al. (2004) · Nature Genetics · doi:10.1038/ng1358 · Cited by 591 · see citing works

Exploring mechanisms of FGF signalling through the lens of structural biology

Goetz, R., & Mohammadi, M. (2013) · Nature reviews. Molecular cell biology · doi:10.1038/nrm3528 · Cited by 556 · see citing works

Identification of a Novel Fibroblast Growth Factor, FGF-23, Preferentially Expressed in the Ventrolateral Thalamic Nucleus of the Brain

Yamashita, T., Yoshioka, M., & Itoh, N. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3696 · Cited by 553 · see citing works

Phosphate is a specific signal for induction of osteopontin gene expression

Beck, G. R., Zerler, B. R., & Morán, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.140021997 · Cited by 533 · see citing works

Fibroblast Growth Factor-23 Relationship to Dietary Phosphate and Renal Phosphate Handling in Healthy Young Men

Ferrari, S. L., Bonjour, J.-P., & Rizzoli, R. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-1039 · Cited by 518 · see citing works

Pathogenic role of Fgf23 in Hyp mice

Liu, S., Zhou, J., Tang, W., Jiang, X., Rowe, D. W., & Quarles, L. D. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00008.2006 · Cited by 494 · see citing works

α-Klotho is a non-enzymatic molecular scaffold for FGF23 hormone signalling

Chen, G., Yang, L., Goetz, R. M., Fu, L., Jayaraman, S., Hu, M. C., Moe, O. W., Liang, G., Li, X., & Mohammadi, M. (2018) · Nature · doi:10.1038/nature25451 · Cited by 491 · see citing works

Discovery of 3-(2,6-Dichloro-3,5-dimethoxy-phenyl)-1-{6-[4-(4-ethyl-piperazin-1-yl)-phenylamino]-pyrimidin-4-yl}-1-methyl-urea (NVP-BGJ398), A Potent and Selective Inhibitor of the Fibroblast Growth Factor Receptor Family of Receptor Tyrosine Kinase

Guagnano, V., Furet, P., Spanka, C., Bordas, V., Douget, M. L., Stamm, C., Brueggen, J., Jensen, M. R., Schnell, C., SCHMID, H. A., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm2006222 · Cited by 485 · see citing works

Circulating FGF-23 Is Regulated by 1α,25-Dihydroxyvitamin D3 and Phosphorus in Vivo

Saitô, H., Maeda, A., Ohtomo, S., Hirata, M., Kusano, K., Kato, S., Ogata, E., Segawa, H., Miyamoto, K., & Fukushima, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408903200 · Cited by 468 · see citing works

Mutant FGF-23 Responsible for Autosomal Dominant Hypophosphatemic Rickets Is Resistant to Proteolytic Cleavage and Causes Hypophosphatemia in Vivo

Shimada, T., Muto, T., Urakawa, I., Yoneya, T., Yamazaki, Y., Okawa, K., Takeuchi, Y., Fujita, T., Fukumoto, S., & Yamashita, T. (2002) · Endocrinology · doi:10.1210/endo.143.8.8795 · Cited by 439 · see citing works

Dietary and Serum Phosphorus Regulate Fibroblast Growth Factor 23 Expression and 1,25-Dihydroxyvitamin D Metabolism in Mice

Perwad, F., Azam, N., Zhang, M. Y. H., Yamashita, T., Tenenhouse, H. S., & Portale, A. A. (2005) · Endocrinology · doi:10.1210/en.2005-0777 · Cited by 424 · see citing works

Iron deficiency drives an autosomal dominant hypophosphatemic rickets (ADHR) phenotype in fibroblast growth factor-23 (Fgf23) knock-in mice

Farrow, E., Yu, X., Summers, L. J., Davis, S. I., Fleet, J. C., Allen, M. R., Robling, A. G., Stayrook, K. R., Jideonwo, V. N., Magers, M. J., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110905108 · Cited by 380 · see citing works

Dynamic regulation of FGF23 by Fam20C phosphorylation, GalNAc-T3 glycosylation, and furin proteolysis

Tagliabracci, V. S., Engel, J. D., Wiley, S. E., Xiao, J., Gonzalez, D. J., Appaiah, H. N., Koller, A. A., Nizet, V., White, K. E., & Dixon, J. E. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402218111 · Cited by 329 · see citing works

Mutations that cause osteoglophonic dysplasia define novel roles for FGFR1 in bone elongation.

White, K., Cabral, J., Davis, S. I., Fishburn, T., Evans, W. E., Ichikawa, S., Fields, J., Yu, X.-J., Shaw, N., McLellan, N., et al. (2005) · American Journal of Human Genetics · doi:10.1086/427956 · Cited by 320 · see citing works

Bone as an endocrine organ

Fukumoto, S., & Martin, T. J. (2009) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2009.02.001 · Cited by 311 · see citing works

Iron Modifies Plasma FGF23 Differently in Autosomal Dominant Hypophosphatemic Rickets and Healthy Humans

Imel, E. A., Peacock, M., Gray, A. K., Padgett, L. R., Hui, S. L., & Econs, M. J. (2011) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2011-1239 · Cited by 305 · see citing works

Phosphate transporters: a tale of two solute carrier families

Virkki, L. V., Biber, J., Murer, H., et al. (2007) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00228.2007 · Cited by 262 · see citing works

Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction.

Furdui, C., Lew, E., Schlessinger, J., & Anderson, K. (2006) · Molecules and Cells · doi:10.1016/j.molcel.2006.01.022 · Cited by 259 · see citing works

Phosphate as a Signaling Molecule and Its Sensing Mechanism

Michigami, T., Kawai, M., Yamazaki, M., & Ozono, K. (2018) · Physiological Reviews · doi:10.1152/physrev.00022.2017 · Cited by 181 · see citing works

Osteopontin Regulation by Inorganic Phosphate Is ERK1/2-, Protein Kinase C-, and Proteasome-dependent

Beck, G. R., & Knecht, N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304470200 · Cited by 180 · see citing works

Regulation of FGF23 expression in IDG-SW3 osteocytes and human bone by pro-inflammatory stimuli

Ito, N., Wijenayaka, A. R., Prideaux, M., Kogawa, M., Ormsby, R. T., Evdokiou, A., Bonewald, L. F., Findlay, D. M., & Atkins, G. J. (2014) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2014.10.007 · Cited by 169 · see citing works

The Precise Sequence of FGF Receptor Autophosphorylation Is Kinetically Driven and Is Disrupted by Oncogenic Mutations

Lew, E., Furdui, C., Anderson, K., & Schlessinger, J. (2009) · Science Signaling · doi:10.1126/scisignal.2000021 · Cited by 163 · see citing works

Hyperostosis–Hyperphosphatemia Syndrome: A Congenital Disorder of O-Glycosylation Associated With Augmented Processing of Fibroblast Growth Factor 23

Frishberg, Y., Ito, N., Rinat, C., et al. (2006) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.061105 · Cited by 163 · see citing works

Activation of unliganded FGF receptor by extracellular phosphate potentiates proteolytic protection of FGF23 by its O-glycosylation

Takashi, Y., Kosako, H., Sawatsubashi, S., Kinoshita, Y., Ito, N., Tsoumpra, M. K., Nangaku, M., Abe, M., Matsuhisa, M., Kato, S., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1815166116 · Cited by 149 · see citing works

X-Linked Hypophosphatemia and FGF23-Related Hypophosphatemic Diseases: Prospect for New Treatment

Kinoshita, Y., & Fukumoto, S. (2018) · Endocrine Reviews · doi:10.1210/er.2017-00220 · Cited by 148 · see citing works

Phosphate (Pi)-regulated heterodimerization of the high-affinity sodium-dependent Pi transporters PiT1/Slc20a1 and PiT2/Slc20a2 underlies extracellular Pi sensing independently of Pi uptake

Bon, N., Couasnay, G., Bourgine, A., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.807339 · Cited by 112 · see citing works

Phosphate-dependent FGF23 secretion is modulated by PiT2/Slc20a2

Bon, N., Frangi, G., Sourice, S., Guicheux, J., Beck-Cormier, S., & Beck, L. (2018) · Molecular Metabolism · doi:10.1016/j.molmet.2018.02.007 · Cited by 87 · see citing works

Both FGF23 and extracellular phosphate activate Raf/MEK/ERK pathway via FGF receptors in HEK293 cells

Yamazaki, M., Ozono, K., Okada, T., Tachikawa, K., Kondou, H., Ohata, Y., & Michigami, T. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22842 · Cited by 82 · see citing works

Signaling of extracellular inorganic phosphate up-regulates cyclin D1 expression in proliferating chondrocytes via the Na+/Pi cotransporter Pit-1 and Raf/MEK/ERK pathway

Kimata, M., Michigami, T., Tachikawa, K., et al. (2010) · Bone · doi:10.1016/j.bone.2010.08.006 · Cited by 82 · see citing works

Small Molecule Inhibitors of Mucin-Type O-Linked Glycosylation from a Uridine-Based Library

Hang, H. C., Yu, C., Hagen, K. G. T., Tian, E., Winans, K. A., Tabak, L. A., & Bertozzi, C. R. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.02.023 · Cited by 72 · see citing works

FGF23 beyond Phosphotropic Hormone

Takashi, Y., & Fukumoto, S. (2018) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2018.08.006 · Cited by 58 · see citing works

Extracellular Phosphate Induces the Expression of Dentin Matrix Protein 1 Through the FGF Receptor in Osteoblasts

Nishino, J., Yamazaki, M., Kawai, M., Tachikawa, K., Yamamoto, K., Miyagawa, K., Kogo, M., Ozono, K., & Michigami, T. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25742 · Cited by 55 · see citing works

Bone remodeling: an operational process ensuring survival and bone mechanical competence

Bolamperti, S., Villa, I., & Rubinacci, A. (2022) · Bone Research · doi:10.1038/s41413-022-00219-8 · Cited by 482 · see citing works

FGF23 signalling and physiology

Ho, B. B., & Bergwitz, C. (2021) · Journal of Molecular Endocrinology · doi:10.1530/jme-20-0178 · Cited by 180 · see citing works

Abstract 364: Klotho Gene Deficiency Causes Heart Failure via Disruption of Phosphate Metabolism

Chen, K., & Sun, Z. (2019) · Circulation Research · doi:10.1161/res.125.suppl_1.364

[Sevelamer hydrochloride prevents ectopic calcification of blood vessels].

Fukushima, N., & Nagano, N. (2004) · PubMed

Dietary Phosphorus and FGF23: Is More Restriction Better?

Gallant, K. M. H. (2019) · PMC

A Case of Hyperphosphatemia and Elevated Fibroblast Growth Factor 23: A Brief Review of Hyperphosphatemia and Fibroblast Growth Factor 23 Pathway

Wang, J., Vogt, B. A., Sethi, S. K., et al. (2017) · Kidney International Reports · doi:10.1016/j.ekir.2017.05.006

Circulating concentration of FGF-23 increases as renal function declines in patients with chronic kidney disease, but does not change in response to variation in phosphate intake in healthy volunteers

Larsson, T., Nisbeth, U. L. F., Ljunggren, Ö., Jüppner, H., & Jonsson, K. B. (2003) · Kidney International · doi:10.1046/j.1523-1755.2003.00328.x · Cited by 689 · see citing works