The Structural Biology of the FGF19 Subfamily

Cell Signaling by Receptor Tyrosine Kinases

Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929 · see citing works

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

Cell Signaling by Receptor Tyrosine Kinases

Schlessinger, J. (2000) · Cell · doi:10.1016/s0092-8674(00)00114-8 · Cited by 3,774 · see citing works

Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor

Yayon, A., Klagsbrun, M., Esko, J. D., Leder, P., & Ornitz, D. M. (1991) · Cell · doi:10.1016/0092-8674(91)90512-w · Cited by 2,440 · see citing works

FGF-21 as a novel metabolic regulator

Kharitonenkov, A., Shiyanova, T. L., Koester, A., Ford, A. M., Micanovic, R., Galbreath, E. J., Sandusky, G. E., Hammond, L. J., Moyers, J. S., Owens, R. A., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23606 · Cited by 2,125 · see citing works

Cellular signaling by fibroblast growth factor receptors

Eswarakumar, V. P., Lax, I., & Schlessinger, J. (2005) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2005.01.001 · Cited by 1,923 · see citing works

Fibroblast growth factor 15 functions as an enterohepatic signal to regulate bile acid homeostasis

Inagaki, T., Choi, M., Moschetta, A., Peng, L., Cummins, C. L., McDonald, J. G., Luo, G., Jones, S. A., Goodwin, B., Richardson, J. A., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.09.001 · Cited by 1,865 · 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

Fibroblast Growth Factor 23 and Mortality among Patients Undergoing Hemodialysis

Gutiérrez, O. M., Mannstadt, M., Isakova, T., Rauh‐Hain, J. A., Tamez, H. E., Shah, A., Smith, K. T., Lee, H., Thadhani, R., Jüppner, H., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa0706130 · Cited by 1,729 · see citing works

Requirement of Heparan Sulfate for bFGF-Mediated Fibroblast Growth and Myoblast Differentiation

Rapraeger, A. C., Krufka, A., & Olwin, B. B. (1991) · Science · doi:10.1126/science.1646484 · Cited by 1,508 · see citing works

Endocrine Regulation of the Fasting Response by PPARα-Mediated Induction of Fibroblast Growth Factor 21

Inagaki, T., Dutchak, P., Zhao, G., Ding, X., Gautron, L., Parameswara, V., Li, Y., Goetz, R., Mohammadi, M., Esser, V., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.05.003 · Cited by 1,504 · see citing works

Targeted ablation of Fgf23 demonstrates an essential physiological role of FGF23 in phosphate and vitamin D metabolism.

Shimada, T., Kakitani, M., Yamazaki, Y., Hasegawa, H., Takeuchi, Y., Fujita, T., Fukumoto, S., Tomizuka, K., & Yamashita, T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19081 · Cited by 1,503 · see citing works

Hepatic Fibroblast Growth Factor 21 Is Regulated by PPARα and Is a Key Mediator of Hepatic Lipid Metabolism in Ketotic States

Badman, M. K., Pissios, P., Kennedy, A. R., Koukos, G., Flier, J. S., & Maratos-Flier, E. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.05.002 · Cited by 1,495 · 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

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

Targeted ablation of Fgf23 demonstrates an essential physiological role of FGF23 in phosphate and vitamin D metabolism

Shimada, T., Kakitani, M., Yamazaki, Y., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200419081 · Cited by 1,368 · 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

Fgf10 is essential for limb and lung formation

Sekine, K., Ohuchi, H., Fujiwara, M., Yamasaki, M., Yoshizawa, T., Sato, T., Yagishita, N., Matsui, D., Koga, Y., Itoh, N., et al. (1999) · Nature Genetics · doi:10.1038/5096 · Cited by 1,283 · see citing works

Structural and functional diversity in the FGF receptor multigene family.

Johnson, D. E., & Williams, L. (1993) · Advances in Cancer Research · doi:10.1016/s0065-230x(08)60821-0 · Cited by 1,270 · see citing works

Crystal Structure of a Ternary FGF-FGFR-Heparin Complex Reveals a Dual Role for Heparin in FGFR Binding and Dimerization

Schlessinger, J., Plotnikov, A. N., Ibrahimi, O. A., Eliseenkova, A. V., Yeh, B. K., Yayon, A., Linhardt, R. J., & Mohammadi, M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00073-3 · 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

Fibroblast Growth Factor 21 Corrects Obesity in Mice

Coskun, T., Bina, H. A., Schneider, M. A., Dunbar, J. D., Hu, C. C., Chen, Y., Moller, D. E., & Kharitonenkov, A. (2008) · Endocrinology · doi:10.1210/en.2008-0816 · Cited by 1,031 · see citing works

Fibroblast Growth Factor 10 (FGF10) and branching morphogenesis in the embryonic mouse lung

Bellusci, S., Grindley, J. C., Emoto, H., Itoh, N., & Hogan, B. L. M. (1997) · Development · doi:10.1242/dev.124.23.4867 · Cited by 1,006 · see citing works

A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway.

Kouhara, H., Hadari, Y., Spivak-Kroizman, T., Schilling, J., Bar-Sagi, D., Lax, I., & Schlessinger, J. (1997) · Cell · doi:10.1016/s0092-8674(00)80252-4 · Cited by 908 · see citing works

Fibroblast Growth Factor 23 in Oncogenic Osteomalacia and X-Linked Hypophosphatemia

Jonsson, K. B., Zahradnik, R. J., Larsson, T. E., White, K. E., Sugimoto, T., Imanishi, Y., Yamamoto, T., Hampson, G., Koshiyama, H., Ljunggren, Ö., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa020881 · Cited by 904 · see citing works

Identification of a novel FGF, FGF-21, preferentially expressed in the liver

Nishimura, T., Nakatake, Y., Konishi, M., & Itoh, N. (2000) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(00)00067-1 · Cited by 847 · see citing works

Endothelial cell-derived heparan sulfate binds basic fibroblast growth factor and protects it from proteolytic degradation.

Saksela, O., Moscatelli, D., Sommer, A., & Rifkin, D. B. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.2.743 · Cited by 803 · see citing works

Heparin Structure and Interactions with Basic Fibroblast Growth Factor

Faham, S., Hileman, R. E., Fromm, J. R., Linhardt, R. J., & Rees, D. C. (1996) · Science · doi:10.1126/science.271.5252.1116 · Cited by 798 · see citing works

Determination of ligand-binding specificity by alternative splicing: two distinct growth factor receptors encoded by a single gene.

Miki, T., Bottaro, D., Fleming, T., Smith, C. L., Burgess, W., Chan, A., & Aaronson, S. (1992) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.89.1.246 · Cited by 757 · see citing works

Tissue-specific Expression of βKlotho and Fibroblast Growth Factor (FGF) Receptor Isoforms Determines Metabolic Activity of FGF19 and FGF21

Kurosu, H., Choi, M., Ogawa, Y., Dickson, A. S., Goetz, R., Eliseenkova, A. V., Mohammadi, M., Rosenblatt, K. P., Kliewer, S. A., & Kuro-o, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704165200 · Cited by 748 · see citing works

The metabolic state of diabetic monkeys is regulated by fibroblast growth factor-21

Kharitonenkov, A., Wroblewski, V. J., Koester, A., Chen, Y.-F., Clutinger, C. K., Tigno, X. T., Hansen, B. C., Shanafelt, A. B., & Etgen, G. J. (2007) · Endocrinology · doi:10.1210/en.2006-1168 · Cited by 738 · see citing works

Structural basis for fibroblast growth factor receptor activation

Mohammadi, M., Olsen, S. K., & Ibrahimi, O. A. (2005) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2005.01.008 · Cited by 736 · see citing works

FGF signaling controls somite boundary position and regulates segmentation clock control of spatiotemporal Hox gene activation.

Dubrulle, J., McGrew, M., & Pourquié, O. (2001) · Cell · doi:10.1016/s0092-8674(01)00437-8 · Cited by 713 · see citing works

Mechanisms underlying differential responses to FGF signaling.

Dailey, L., Ambrosetti, D., Mansukhani, A., & Basilico, C. (2005) · Cytokine & growth factor reviews · doi:10.1016/j.cytogfr.2005.01.007 · Cited by 701 · see citing works

Definition of a novel growth factor-dependent signal cascade for the suppression of bile acid biosynthesisPreprint

Holt, J. A., Luo, G., Billin, A. N., Bisi, J., McNeill, Y. Y., Kozarsky, K., Donahee, M. H., Wang, D. Y., Mansfield, T. A., Kliewer, S. A., et al. (2003) · Genes & Development · doi:10.1101/gad.1083503 · Cited by 698 · see citing works

Heparan sulphate proteoglycans: the sweet side of development

Häcker, U., Nybakken, K. E., & Perrimon, N. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1681 · Cited by 683 · see citing works

Increased Circulatory Level of Biologically Active Full-Length FGF-23 in Patients with Hypophosphatemic Rickets/Osteomalacia

Yamazaki, Y., Okazaki, R., Shibata, M., Hasegawa, Y., Satoh, K., Tajima, T., Takeuchi, Y., Fujita, T., Nakahara, K., Yamashita, T., et al. (2002) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2002-021105 · Cited by 670 · see citing works

FGF-23 in fibrous dysplasia of bone and its relationship to renal phosphate wasting

Riminucci, M., Collins, M. T., Fedarko, N. S., Cherman, N., Corsi, A., White, K. E., Waguespack, S. G., Gupta, A., Hannon, T. S., Econs, M. J., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18399 · Cited by 656 · see citing works

FGF-4 replaces the apical ectodermal ridge and directs outgrowth and patterning of the limb

Niswander, L. A., Tickle, C. A., Vogel, A., Booth, I., & Martin, G. R. (1993) · Cell · doi:10.1016/0092-8674(93)90391-3 · Cited by 651 · see citing works

Heparin Is Required for Cell-Free Binding of Basic Fibroblast Growth Factor to a Soluble Receptor and for Mitogenesis in Whole Cells

Ornitz, D. M., Yayon, A., Flanagan, J. G., Svahn, C. M., Levi, E., & Leder, P. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.1.240 · Cited by 632 · see citing works

βKlotho is required for metabolic activity of fibroblast growth factor 21

Ogawa, Y., Kurosu, H., Yamamoto, M., Nandi, A., Rosenblatt, K. P., Goetz, R., Eliseenkova, A. V., Mohammadi, M., & Kuro-o, M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701600104 · Cited by 617 · see citing works

Structural Basis for FGF Receptor Dimerization and Activation

Plotnikov, A. N., Schlessinger, J., Hubbard, S. R., & Mohammadi, M. (1999) · Cell · doi:10.1016/s0092-8674(00)80051-3 · Cited by 610 · see citing works

Male-to-female sex reversal in mice lacking fibroblast growth factor 9.

Colvin, J. S., Green, R. P., Schmahl, J., Capel, B., & Ornitz, D. (2001) · Cell · doi:10.1016/s0092-8674(01)00284-7 · Cited by 596 · see citing works

Functions of FGF signalling from the apical ectodermal ridge in limb development

Sun, X., Mariani, F. V., & Martin, G. (2002) · Nature · doi:10.1038/nature00902 · Cited by 581 · see citing works

Fibroblast Growth Factor 19 Increases Metabolic Rate and Reverses Dietary and Leptin-Deficient Diabetes

Fu, L., John, L. M., Adams, S. H., Yu, X. X., Tomlinson, E., Renz, M. E., Williams, P. M., Soriano, R. H., Corpuz, R. T., Moffat, B., et al. (2004) · Endocrinology · doi:10.1210/en.2003-1671 · Cited by 580 · see citing works

Transgenic Mice Expressing Human Fibroblast Growth Factor-19 Display Increased Metabolic Rate and Decreased Adiposity

Tomlinson, E., Fu, L., John, L., Hultgren, B., Huang, X., Renz, M., Stephan, J. P., Tsai, S. P., Powell-Braxton, L., French, D., et al. (2002) · Endocrinology · doi:10.1210/endo.143.5.8850 · Cited by 576 · see citing works

Purification and complementary DNA cloning of a receptor for basic fibroblast growth factor.

Lee, P. E., Johnson, D. E., Cousens, L., Fried, V., & Williams, L. (1989) · Science · doi:10.1126/science.2544996 · Cited by 574 · see citing works

Area Patterning of the Mammalian Cortex

O’Leary, D. D. M., Chou, S., & Sahara, S. (2007) · Neuron · doi:10.1016/j.neuron.2007.10.010 · Cited by 574 · see citing works

Phospholipid signaling

Divecha, N., & Irvine, R. F. (1995) · Cell · doi:10.1016/0092-8674(95)90409-3 · Cited by 568 · see citing works

Fibroblast growth factor receptor 2 (FGFR2)-mediated reciprocal regulation loop between FGF8 and FGF10 is essential for limb induction

Xu, X., Weinstein, M. B., Li, C., Naski, M. C., Cohen, R. I., Ornitz, D. M., Leder, P., & Deng, C. (1998) · Development · doi:10.1242/dev.125.4.753 · Cited by 549 · see citing works

Developmental Localization of the Splicing Alternatives of Fibroblast Growth Factor Receptor-2 (FGFR2)

Orr‐Urtreger, A., Bedford, M. T., Burakova, T., Arman, E., Zimmer, Y., Yayon, A., Givol, D., & Lonai, P. (1993) · Developmental Biology · doi:10.1006/dbio.1993.1205 · Cited by 547 · see citing works

Molecular Insights into the Klotho-Dependent, Endocrine Mode of Action of Fibroblast Growth Factor 19 Subfamily Members

Goetz, R., Beenken, A., Ibrahimi, O., Kalinina, J., Olsen, S., Eliseenkova, A. V., Xu, C.-F., Neubert, T., Zhang, F.-M., Linhardt, R., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02249-06 · Cited by 544 · see citing works

The Circulating Metabolic Regulator FGF21 Is Induced by Prolonged Fasting and PPARα Activation in Man

Gälman, C., Lundåsen, T., Kharitonenkov, A., Bina, H. A., Eriksson, M., Hafström, I., Dahlin, M., Åmark, P., Angelin, B., & Rudling, M. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.06.014 · Cited by 512 · see citing works

Regulation of Fibroblastic Growth Factor 23 Expression but Not Degradation by PHEX

Liu, S., Guo, R., Simpson, L. G., Xiao, Z.-S., Burnham, C. E., & Quarles, L. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304544200 · Cited by 505 · see citing works

Fibroblast Growth Factor-21 Improves Pancreatic β-Cell Function and Survival by Activation of Extracellular Signal–Regulated Kinase 1/2 and Akt Signaling Pathways

Wente, W., Efanov, A. M., Brenner, M. B., Kharitonenkov, A., Koster, A. M., Sandusky, G. E., Sewing, S., Treinies, I., Zitzer, H., & Gromada, J. (2006) · Diabetes · doi:10.2337/db05-1435 · Cited by 497 · see citing works

Transgenic Mice Expressing Fibroblast Growth Factor 23 under the Control of the α1(I) Collagen Promoter Exhibit Growth Retardation, Osteomalacia, and Disturbed Phosphate Homeostasis

Larsson, T. E., Marsell, R., Schipani, E., Ohlsson, C., Ljunggren, Ö., Tenenhouse, H. S., Jüppner, H., & Jonsson, K. B. (2004) · Endocrinology · doi:10.1210/en.2003-1768 · Cited by 497 · see citing works

An FGF23 missense mutation causes familial tumoral calcinosis with hyperphosphatemia.

Benet-Pagès, A., Orlik, P., Strom, T., & Lorenz-Depiereux, B. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi034 · Cited by 486 · 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

FGF23 decreases renal NaPi-2a and NaPi-2c expression and induces hypophosphatemia in vivo predominantly via FGF receptor 1

Gattineni, J., Bates, C. M., Twombley, K. E., Dwarakanath, V. N., Robinson, M. L., Goetz, R. M., Mohammadi, M., & Baum, M. G. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90742.2008 · Cited by 439 · see citing works

Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis

Mohammadi, M., Dionne, C. A., Li, W., Li, N., Spivak-Kroizman, T. R., Honegger, A., Jaye, M., & Schlessinger, J. (1992) · Nature · doi:10.1038/358681a0 · Cited by 424 · see citing works

Human Fibroblast Growth Factor-23 Mutants Suppress Na+-dependent Phosphate Co-transport Activity and 1α,25-Dihydroxyvitamin D3 Production

Saitô, H., Kusano, K., Kinosaki, M., Ito, H., Hirata, M., Segawa, H., Miyamoto, K., & Fukushima, N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207872200 · Cited by 412 · see citing works

Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity.

Plotnikov, A., Hubbard, S., Schlessinger, J., & Mohammadi, M. (2000) · Cell · doi:10.1016/s0092-8674(00)80851-x · Cited by 412 · see citing works

Heparan Sulfate: A Complex Polymer Charged with Biological Activity

Whitelock, J. M., & Iozzo, R. V. (2005) · Chemical Reviews · doi:10.1021/cr010213m · Cited by 410 · see citing works

Functional evolutionary history of the mouse Fgf gene family

Itoh, N., & Ornitz, D. M. (2007) · Developmental Dynamics · doi:10.1002/dvdy.21388 · Cited by 409 · see citing works

Circulating intestinal fibroblast growth factor 19 has a pronounced diurnal variation and modulates hepatic bile acid synthesis in man

Lundåsen, T., Gälman, C., Angelin, B., & Rudling, M. J. (2006) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2006.01731.x · Cited by 406 · see citing works

The Human Fibroblast Growth Factor Receptor Genes: a Common Structural Arrangement Underlies the Mechanisms for Generating Receptor Forms That Differ in Their Third Immunoglobulin Domain

Johnson, D. E., Lu, J., Chen, H. C., Werner, S., & Williams, L. T. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.9.4627 · Cited by 404 · see citing works

Identification of Six Novel Autophosphorylation Sites on Fibroblast Growth Factor Receptor 1 and Elucidation of Their Importance in Receptor Activation and Signal Transduction

Mohammadi, M., Dikic, I., Sorokin, A., Burgess, W. H., Jaye, M., & Schlessinger, J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.3.977 · Cited by 389 · see citing works

Three-Dimensional Structures of Acidic and Basic Fibroblast Growth Factors

Zhu, X., Komiya, H., Chirino, A. J., Faham, S., Fox, G. M., Arakawa, T., Hsu, B. T., & Rees, D. C. (1991) · Science · doi:10.1126/science.1702556 · Cited by 386 · see citing works

Isolated C-terminal tail of FGF23 alleviates hypophosphatemia by inhibiting FGF23-FGFR-Klotho complex formation

Goetz, R. M., Nakada, Y., Hu, M. C., Kurosu, H., Wang, L., Nakatani, T., Shi, M., Eliseenkova, A. V., Razzaque, M. S., Moe, O. W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902006107 · Cited by 383 · see citing works

Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis

Peters, K., Marie, J., Wilson, E., Ives, H., Escobedo, J., del Rosario, M., Mirda, D., & Williams, L. (1992) · Nature · doi:10.1038/358678a0 · Cited by 375 · see citing works

FRS2 Proteins Recruit Intracellular Signaling Pathways by Binding to Diverse Targets on Fibroblast Growth Factor and Nerve Growth Factor Receptors

Ong, S., Guy, G., Hadari, Y., Laks, S., Gotoh, N., Schlessinger, J., & Lax, I. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.979-989.2000 · Cited by 373 · see citing works

Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development

Lin, X., Buff, E. M., Perrimon, N., & Michelson, A. M. (1999) · Development · doi:10.1242/dev.126.17.3715 · Cited by 368 · see citing works

Structure of a heparin-linked biologically active dimer of fibroblast growth factor

DiGabriele, A. D., Lax, I., Chen, D. I., Svahn, C. M., Jaye, M., Schlessinger, J., & Hendrickson, W. A. (1998) · Nature · doi:10.1038/31741 · Cited by 353 · see citing works

Elevated Cholesterol Metabolism and Bile Acid Synthesis in Mice Lacking Membrane Tyrosine Kinase Receptor FGFR4

Yu, C., Wang, F., Kan, M., Jin, C., Jones, R. B., Weinstein, M. B., Deng, C., & McKeehan, W. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.20.15482 · Cited by 348 · see citing works

βKlotho Is Required for Fibroblast Growth Factor (FGF) 21 Signaling through FGF Receptor (FGFR) 1c and FGFR3c

Suzuki, M., Uehara, Y., Motomura-Matsuzaka, K., Oki, J., Koyama, Y., Kimura, M., Asada, M., Komi-Kuramochi, A., Oka, S., & Toru, T. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0313 · Cited by 345 · see citing works

Lung hypoplasia and neonatal death in Fgf9 -null mice identify this gene as an essential regulator of lung mesenchyme

Colvin, J. S., White, A. C., Pratt, S. J. P., & Ornitz, D. M. (2001) · Development · doi:10.1242/dev.128.11.2095 · Cited by 338 · see citing works

Binding of Shp2 Tyrosine Phosphatase to FRS2 Is Essential for Fibroblast Growth Factor-Induced PC12 Cell Differentiation

Hadari, Y., Kouhara, H., Lax, I., & Schlessinger, J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.3966 · Cited by 333 · see citing works

FGF‐21/FGF‐21 receptor interaction and activation is determined by βKlotho

Kharitonenkov, A., Dunbar, J. D., Bina, H. A., Bright, S. W., Moyers, J. S., Zhang, C., Ding, L., Micanovic, R., Mehrbod, S. F., Knierman, M. D., et al. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21357 · Cited by 329 · see citing works

Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins

Ong, S. H., Hadari, Y. R., Gotoh, N., Guy, G. R., Schlessinger, J., & Lax, I. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111114298 · Cited by 314 · see citing works

Evidence for Selective Advantage of Pathogenic FGFR2 Mutations in the Male Germ Line

Goriely, A., McVean, G., Rojmyr, M., Ingemarsson, B., & Wilkie, A. O. M. (2003) · Science · doi:10.1126/science.1085710 · Cited by 310 · see citing works

Structure of the mouse klotho gene and its two transcripts encoding membrane and secreted protein 1

Shiraki-Iida, T., Aizawa, H., Matsumura, Y., Sekine, S., Iida, A., Anazawa, H., Nagai, R., Kuro‐o, M., & Nabeshima, Y.-I. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00127-6 · Cited by 309 · see citing works

Fgf/MAPK signalling is a crucial positional cue in somite boundary formation

Sawada, A., Shinya, M., Jiang, Y., Kawakami, A., Kuroiwa, A., & Takeda, H. (2001) · Development · doi:10.1242/dev.128.23.4873 · Cited by 304 · see citing works

Characterization of Growth Factor-binding Structures in Heparin/Heparan Sulfate Using an Octasaccharide Library

Ashikari‐Hada, S., Habuchi, H., Kariya, Y., Itoh, N., Reddi, A. H., & Kimata, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313523200 · Cited by 296 · see citing works

Fibroblast Growth Factor (FGF) Homologous Factors Share Structural but Not Functional Homology with FGFs*

Olsen, S., Garbi, M., Zampieri, N., Eliseenkova, A. V., Ornitz, D., Goldfarb, M., & Mohammadi, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303183200 · Cited by 292 · see citing works

A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases.

Chen, H.-B., Ma, J.-H., Li, W., Eliseenkova, A. V., Xu, C.-F., Neubert, T., Miller, W., & Mohammadi, M. (2007) · Molecules and Cells · doi:10.1016/j.molcel.2007.06.028 · Cited by 290 · see citing works

Identification of a hormonal basis for gallbladder filling

Choi, M., Moschetta, A., Bookout, A., Peng, L., Umetani, M., Holmstrom, S. R., Suino-Powell, K., Xu, H. E., Richardson, J., Gerard, R., et al. (2006) · Nature Medicine · doi:10.1038/nm1501 · Cited by 289 · see citing works

Liver-specific Activities of FGF19 Require Klotho beta

Lin, B. C., Wang, M., Blackmore, C. A., & Desnoyers, L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704244200 · Cited by 284 · see citing works

Three-dimensional structure of human basic fibroblast growth factor.

Sauer-Eriksson, A. E., Cousens, L. S., Weaver, L. H., & Matthews, B. W. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.8.3441 · Cited by 284 · see citing works

The Autosomal Dominant Hypophosphatemic Rickets R176Q Mutation in Fibroblast Growth Factor 23 Resists Proteolytic Cleavage and Enhances in Vivo Biological Potency

Bai, X., Miao, D., Goltzman, D., & Karaplis, A. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210490200 · Cited by 274 · 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

Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta.

Zhang, J. D., Cousens, L. S., Barr, P. J., & Sprang, S. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.8.3446 · Cited by 250 · see citing works

Early Anterior/Posterior Patterning of the Midbrain and Cerebellum

Liu, A., & Joyner, A. L. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.869 · Cited by 248 · see citing works

Impaired negative feedback suppression of bile acid synthesis in mice lacking βKlotho

Ito, S., Fujimori, T., Furuya, A., Satoh, J., Nabeshima, Y., & Nabeshima, Y. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23076 · Cited by 245 · see citing works

Fibroblast growth factor homologous factors: evolution, structure, and function.

Goldfarb, M. (2005) · Cytokine & growth factor reviews · doi:10.1016/j.cytogfr.2005.02.002 · Cited by 234 · see citing works

Structural interactions of fibroblast growth factor receptor with its ligands

Stauber, D. J., DiGabriele, A. D., & Hendrickson, W. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.1.49 · Cited by 233 · see citing works

FGF10 is an inducer and Pax6 a competence factor for lacrimal gland development

Makarenkova, H. P., Ito, M., Govindarajan, V., Faber, S. C., Sun, L., McMahon, G., Overbeek, P. A., & Lang, R. A. (2000) · Development · doi:10.1242/dev.127.12.2563 · Cited by 225 · see citing works

The Fgf Families in Humans, Mice, and Zebrafish: Their Evolutional Processes and Roles in Development, Metabolism, and Disease

Itoh, N. (2007) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.30.1819 · Cited by 224 · see citing works

A Novel Recessive Mutation in Fibroblast Growth Factor-23 Causes Familial Tumoral Calcinosis

Larsson, T. E., Yu, X., Davis, S. I., Draman, M. S., Mooney, S. D., Cullen, M. J., & White, K. E. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-2238 · Cited by 221 · see citing works

Heparan sulfate: lessons from knockout mice

Forsberg, E., & Kjellén, L. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200113561 · Cited by 214 · see citing works

Gene expression profiles of mouse submandibular gland development: FGFR1 regulates branching morphogenesis in vitro through BMP- and FGF-dependent mechanisms

Hoffman, M. P., Kidder, B. L., Steinberg, Z. L., Lakhani, S., Ho, S. W., Kleinman, H. K., & Larsen, M. (2002) · Development · doi:10.1242/dev.00172 · Cited by 212 · see citing works

Insights into the molecular basis for fibroblast growth factor receptor autoinhibition and ligand-binding promiscuity.

Olsen, S., Ibrahimi, O., Raucci, A., Zhang, F.-M., Eliseenkova, A. V., Yayon, A., Basilico, C., Linhardt, R., Schlessinger, J., & Mohammadi, M. (2004) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0307287101 · Cited by 209 · see citing works

A novel mutation in fibroblast growth factor 23 gene as a cause of tumoral calcinosis.

Araya, K., Fukumoto, S., Backenroth, R., Takeuchi, Y., Nakayama, K., Ito, N., Yoshii, N., Yamazaki, Y., Yamashita, T., Silver, J., et al. (2005) · Journal of Clinical Endocrinology and Metabolism · doi:10.1210/jc.2005-0301 · Cited by 209 · see citing works

Activating mutations in FGFR3 and HRAS reveal a shared genetic origin for congenital disorders and testicular tumors

Goriely, A., Hansen, R. M. S., Taylor, I. B., Olesen, I. A., Jacobsen, G. K., McGowan, S. J., Pfeifer, S. P., McVean, G. A. T., Meyts, E. R.-D., & Wilkie, A. O. M. (2009) · Nature Genetics · doi:10.1038/ng.470 · Cited by 205 · see citing works

Structural basis by which alternative splicing modulates the organizer activity of FGF8 in the brainPreprint

Olsen, S. K., Li, J. Y. H., Bromleigh, C., Eliseenkova, A. V., Ibrahimi, O. A., Lao, Z., Zhang, F., Linhardt, R. J., Joyner, A. L., & Mohammadi, M. (2005) · Genes & Development · doi:10.1101/gad.1365406 · Cited by 204 · see citing works

Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors

Yeh, B. K., Igarashi, M., Eliseenkova, A. V., Plotnikov, A., Sher, I., Ron, D., Aaronson, S., & Mohammadi, M. (2003) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0436500100 · Cited by 200 · see citing works

High Resolution X-ray Crystallography Shows That Ascorbate Is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base

Burmeister, W. P., Cottaz, S., Rollin, P., Vasella, A. T., & Henrissat, B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006796200 · Cited by 198 · see citing works

Differential Interactions of FGFs with Heparan Sulfate Control Gradient Formation and Branching Morphogenesis

Makarenkova, H., Hoffman, M., Beenken, A., Eliseenkova, A. V., Meech, R., Tsau, C., Patel, V., Lang, R., & Mohammadi, M. (2009) · Science Signaling · doi:10.1126/scisignal.2000304 · Cited by 194 · see citing works

Heparan sulfate: lessons from knockout mice

Forsberg, E., & Kjellén, L. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13561 · Cited by 190 · see citing works

FGF19-induced Hepatocyte Proliferation Is Mediated through FGFR4 Activation

Wu, X., Ge, H., Lemon, B., Vonderfecht, S., Weiszmann, J., Hecht, R., Gupte, J., Hager, T., Wang, Z.-L., Lindberg, R., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.068783 · Cited by 186 · see citing works

Alternately Spliced NH2-terminal Immunoglobulin-like Loop I in the Ectodomain of the Fibroblast Growth Factor (FGF) Receptor 1 Lowers Affinity for both Heparin and FGF-1(*)

Wang, F., Kan, M., Yan, G.-C., Xu, J.-M., & Mckeehan, W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.10231 · Cited by 157 · see citing works

Crystal Structure of a Fibroblast Growth Factor Homologous Factor (FHF) Defines a Conserved Surface on FHFs for Binding and Modulation of Voltage-gated Sodium Channels*

Goetz, R., Dover, K., Laezza, F., Shtraizent, N., Huang, X., Tchetchik, D., Eliseenkova, A. V., Xu, C.-F., Neubert, T., Ornitz, D., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.001842 · Cited by 157 · see citing works

A protein canyon in the FGF–FGF receptor dimer selects from an à la carte menu of heparan sulfate motifs

Mohammadi, M., Olsen, S. K., & Goetz, R. M. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.09.002 · Cited by 157 · see citing works

Epithelial/mesenchymal interactions and branching morphogenesis of the lung

Hogan, B. L. M., & Yingling, J. M. (1998) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(98)80121-4 · Cited by 152 · see citing works

Oscillations of the Snail Genes in the Presomitic Mesoderm Coordinate Segmental Patterning and Morphogenesis in Vertebrate Somitogenesis

Dale, J. K., Malapert, P., Chal, J., Vilhais-Neto, G. C., Maroto, M., Johnson, T., Jayasinghe, S. M., Trainor, P. A., Herrmann, B. G., & Pourquié, O. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.02.011 · Cited by 151 · see citing works

Effect of hydrolysis-resistant FGF23-R179Q on dietary phosphate regulation of the renal type-II Na/Pi transporter

Segawa, H., Kawakami, E., Kaneko, I., Kuwahata, M., Ito, M., Kusano, K., Saitô, H., Fukushima, N., & Miyamoto, K. (2003) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1084-1 · Cited by 142 · see citing works

Co-receptor Requirements for Fibroblast Growth Factor-19 Signaling

Wu, X., Ge, H., Gupte, J., Weiszmann, J., Shimamoto, G., Stevens, J., Hawkins, N., Lemon, B., Shen, W., Xu, J., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700130200 · Cited by 140 · see citing works

FGF23 and disorders of phosphate homeostasis.

Yu, X.-J., & White, K. (2005) · Cytokine & growth factor reviews · doi:10.1016/j.cytogfr.2005.01.002 · Cited by 138 · see citing works

A clock and wavefront mechanism for somite formation

Baker, R. E., Schnell, S. D., & Maini, P. K. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.01.018 · Cited by 128 · see citing works

Heparan sulfate–FGF10 interactions during lung morphogenesis

Izvolsky, K. I., Shoykhet, D., Yu, Y., Yu, Q., Nugent, M. A., & Cardoso, W. V. (2003) · Developmental Biology · doi:10.1016/s0012-1606(03)00114-3 · Cited by 126 · see citing works

The Crystal Structure of Fibroblast Growth Factor (FGF) 19 Reveals Novel Features of the FGF Family and Offers a Structural Basis for Its Unusual Receptor Affinity,

Harmer, N. J., Pellegrini, L., Chirgadze, D., Fernández‐Recio, J., & Blundell, T. L. (2003) · Biochemistry · doi:10.1021/bi035320k · Cited by 124 · see citing works

Physiological Regulation and Disorders of Phosphate Metabolism -Pivotal Role of Fibroblast Growth Factor 23-

Fukumoto, S. (2008) · Internal Medicine · doi:10.2169/internalmedicine.47.0730 · Cited by 119 · see citing works

Structural Basis of SNT PTB Domain Interactions with Distinct Neurotrophic Receptors

Dhalluin, C., Yan, K. S., Plotnikova, O., Lee, K., Zeng, L., Kuti, M., Mujtaba, S., Goldfarb, M. P., & Zhou, M.-M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00087-0 · Cited by 107 · see citing works

Genetic Transmission of Tumoral Calcinosis: Autosomal Dominant with Variable Clinical Expressivity*

Lyles, K. W., Burkes, E. J., Ellis, G. J., LUCAS, K. J., Dolan, E. A., & Drezner, M. K. (1985) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-60-6-1093 · Cited by 105 · see citing works

The chick embryo: a leading model in somitogenesis studies

Pourquié, O. (2004) · Mechanisms of Development · doi:10.1016/j.mod.2004.05.002 · Cited by 103 · see citing works

Reduced Activation of RAF-1 and MAP Kinase by a Fibroblast Growth Factor Receptor Mutant Deficient in Stimulation of Phosphatidylinositol Hydrolysis

Huang, J., Mohammadi, M., Rodrigues, G. A., & Schlessinger, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5065 · Cited by 102 · see citing works

Sequential changes in the expression of genes involved in lipid metabolism in adipose tissue and liver in response to fasting

Palou, M., Priego, T., Sánchez, J., Villegas, E., Rodríguez, A. M., Palou, A., & Picó, C. (2008) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-008-0461-1 · Cited by 99 · see citing works

An evolutionary history of the FGF superfamily

Popovici, C., Roubin, R., Coulier, F., & Birnbaum, D. (2005) · BioEssays · doi:10.1002/bies.20261 · Cited by 98 · see citing works

Fibroblast Growth Factor-21 as a Therapeutic Agent for Metabolic Diseases

Kharitonenkov, A., & Shanafelt, A. B. (2008) · BioDrugs · doi:10.2165/00063030-200822010-00004 · Cited by 98 · see citing works

Fgf9 signaling regulates inner ear morphogenesis through epithelial-mesenchymal interactions.

Pirvola, U., Zhang, X.-Q., Mantela, J., Ornitz, D., & Ylikoski, J. (2004) · Developmental Biology · doi:10.1016/j.ydbio.2004.06.010 · Cited by 95 · see citing works

Structural studies of the binding of the anti-ulcer drug sucrose octasulfate to acidic fibroblast growth factor

Zhu, X., Hsu, B. T., & Rees, D. C. (1993) · Structure · doi:10.1016/0969-2126(93)90006-3 · Cited by 89 · see citing works

Fibroblast growth factor (FGF)-4 can induce proliferation of cardiac cushion mesenchymal cells during early valve leaflet formation

Sugi, Y., Ito, N., Szebenyi, G., Myers, K., Fallon, J. F., Mikawa, T., & Markwald, R. R. (2003) · Developmental Biology · doi:10.1016/s0012-1606(03)00099-x · Cited by 80 · see citing works

Reciprocal epithelial-mesenchymal FGF signaling is required for cecal development

Zhang, X.-Q., Stappenbeck, T., White, A. C., Lavine, K. J., Gordon, J., & Ornitz, D. (2006) · Development · doi:10.1242/dev.02175 · Cited by 80 · see citing works

FGF-16 is required for embryonic heart development.

Lu, S.-Y., Sheikh, F., Sheppard, P., Fresnoza, A., Duckworth, M. L., Detillieux, K. A., & Cattini, P. (2008) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2008.06.029 · Cited by 74 · see citing works

Crystal Structure of Fibroblast Growth Factor 9 Reveals Regions Implicated in Dimerization and Autoinhibition

Plotnikov, A. N., Eliseenkova, A. V., Ibrahimi, O. A., Shriver, Z. H., Sasisekharan, R., Lemmon, M. A., & Mohammadi, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006502200 · Cited by 74 · see citing works

A crystallographic snapshot of tyrosine trans -phosphorylation in action

Chen, H., Xu, C., Ma, J., Eliseenkova, A. V., Li, W., Pollock, P. M., Pitteloud, N., Miller, W. T., Neubert, T. A., & Mohammadi, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807752105 · Cited by 68 · see citing works

Identification of Receptor and Heparin Binding Sites in Fibroblast Growth Factor 4 by Structure-Based Mutagenesis

Bellosta, P., Iwahori, A., Plotnikov, A. N., Eliseenkova, A. V., Basilico, C., & Mohammadi, M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.17.5946-5957.2001 · Cited by 66 · see citing works

Directionally Specific Paracrine Communication Mediated by Epithelial FGF9 to Stromal FGFR3 in Two-Compartment Premalignant Prostate Tumors

Jin, C., Wang, F., Wu, X., Yu, C., Luo, Y., & McKeehan, W. L. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3752 · Cited by 59 · see citing works

The Glycine Box: A Determinant of Specificity for Fibroblast Growth Factor

Luo, Y., Lu, W., Mohamedali, K. A., Jang, J.-H., Jones, R. B., Gabriel, J. L., Kan, M., & McKeehan, W. L. (1998) · Biochemistry · doi:10.1021/bi9816599 · Cited by 52 · see citing works

Homodimerization Controls the Fibroblast Growth Factor 9 Subfamily's Receptor Binding and Heparan Sulfate-Dependent Diffusion in the Extracellular Matrix

Kalinina, J., Byron, S. A., Makarenkova, H. P., Olsen, S. K., Eliseenkova, A. V., LaRochelle, W. J., Dhanabal, M., Blais, S. P., Ornitz, D. M., Day, L. A., et al. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01780-08 · Cited by 50 · see citing works

FGF-FGFR signaling in vertebrate organogenesis.

Kato, S., & Sekine, K. (1999) · PubMed · Cited by 50 · see citing works

Lin, X., Buff, E. M., Perrimon, N. & Michelson, A. M. Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development. Development 126, 3715-3723

Xh, L., Buff, E. M., Perrimon, N., & Michelson, A. M. (1999) · Cited by 44 · see citing works

Correlation between the 1.6 Å crystal structure and mutational analysis of keratinocyte growth factor

Osslund, T. D., Syed, R. S., Singer, E., Hsu, E., Nybo, R. E., Harvey, T. S., Arakawa, T., Narhi, L. O., Chirino, A. J., Morris, C. F., et al. (1998) · Protein Science · doi:10.1002/pro.5560070803 · Cited by 41 · see citing works

Structural and Functional Basis of a Role for CRKL in a Fibroblast Growth Factor 8-Induced Feed-Forward Loop

Seo, J.-H., Suenaga, A., Hatakeyama, M., Taiji, M., & Imamoto, A. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01686-08 · Cited by 34 · see citing works

Glu-96 of Basic Fibroblast Growth Factor Is Essential for High Affinity Receptor Binding

Zhu, H., Ramnarayan, K., Anchin, J. M., Miao, W. Y., Sereno, A., Millman, L., Zheng, J., Balaji, V., & Wolff, M. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.37.21869 · Cited by 27 · see citing works

Fibroblast Growth Factor 23 and Klotho: Physiology and Pathophysiology of an Endocrine Network of Mineral Metabolism

Hu, M. C., Shiizaki, K., Kuro-o, M., & Moe, O. W. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-030212-183727 · Cited by 587 · see citing works

Developmental pathways in the pathogenesis of lung fibrosis

Chanda, D., Otoupalova, E., Smith, S. R., Volckaert, T., Langhe, S. D., & Thannickal, V. J. (2018) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2018.08.004 · Cited by 513 · see citing works

Pharmacology of Heparin and Related Drugs

Mulloy, B., Hogwood, J., Gray, E., Lever, R., & Page, C. P. (2015) · Pharmacological Reviews · doi:10.1124/pr.115.011247 · Cited by 341 · see citing works

Metabolic messengers: FGF21

Flippo, K. H., & Potthoff, M. J. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00354-2 · Cited by 311 · see citing works

FGF23 and its role in X-linked hypophosphatemia-related morbidity

Beck‐Nielsen, S. S., Zulf Mughal, M., Haffner, D., Nilsson, O., Levtchenko, E. N., Ariceta, G., Collantes, C. D. L., Schnabel, D., Jandhyala, R., & Mäkitie, O. (2019) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-019-1014-8 · Cited by 288 · see citing works

Molecular Mechanisms of Fibroblast Growth Factor Signaling in Physiology and PathologyPreprint

Belov, A. A., & Mohammadi, M. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a015958 · Cited by 272 · see citing works

Fibroblast Growth Factor 21: A Versatile Regulator of Metabolic Homeostasis

BonDurant, L. D., & Potthoff, M. J. (2018) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071816-064800 · Cited by 222 · see citing works

Fibroblast growth factors (FGFs) in cancer: FGF traps as a new therapeutic approach

Presta, M., Chiodelli, P., Giacomini, A., Rusnati, M., & Ronca, R. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.05.013 · Cited by 199 · see citing works

Molecular basis of bile acid-FXR-FGF15/19 signaling axis

Katafuchi, T., & Makishima, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116046 · Cited by 193 · see citing works

Separating Tumorigenicity from Bile Acid Regulatory Activity for Endocrine Hormone FGF19

Zhou, M., Wang, X., Phung, V., Lindhout, D. A., Mondal, K., Hsu, J.-Y., Yang, H., Humphrey, M., Ding, X., Arora, T., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0208 · Cited by 183 · see citing works

Fibroblast growth factor signalling in osteoarthritis and cartilage repair

Xie, Y., Zinkle, A., Chen, L., & Mohammadi, M. (2020) · Nature Reviews Rheumatology · doi:10.1038/s41584-020-0469-2 · Cited by 186 · see citing works

Renal and extrarenal effects of fibroblast growth factor 23

Vervloet, M. G. (2018) · Nature Reviews Nephrology · doi:10.1038/s41581-018-0087-2 · Cited by 150 · see citing works

FGF21: A Novel Regulator of Glucose and Lipid Metabolism and Whole-Body Energy Balance

Szczepańska, E., & Gietka‐Czernel, M. (2022) · Hormone and Metabolic Research · doi:10.1055/a-1778-4159 · Cited by 155 · see citing works

Endocrine FGFs: Evolution, Physiology, Pathophysiology, and Pharmacotherapy

Itoh, N., Ohta, H., & Konishi, M. (2015) · Frontiers in Endocrinology · doi:10.3389/fendo.2015.00154 · Cited by 119 · see citing works

Fibroblast Growth Factor 15/19: From Basic Functions to Therapeutic Perspectives

Somm, E., & Jornayvaz, F. R. (2018) · Endocrine Reviews · doi:10.1210/er.2018-00134 · Cited by 118 · see citing works

Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability

Huang, Z., Tan, Y., Gu, J., Liu, Y., Song, L., Niu, J., Zhao, L., Srinivasan, L., Lin, Q., Deng, J., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.063 · Cited by 103 · see citing works

Conversion of a Paracrine Fibroblast Growth Factor into an Endocrine Fibroblast Growth Factor

Goetz, R. M., Ohnishi, M., Kır, S., Kurosu, H., Wang, L., Pastor, J. V., Ma, J., Gai, W., Kuro‐o, M., Razzaque, M. S., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.342980 · Cited by 98 · see citing works

FGF23-αKlotho as a paradigm for a kidney-bone network

Kuro‐o, M., & Moe, O. W. (2016) · Bone · doi:10.1016/j.bone.2016.11.013 · Cited by 92 · see citing works

Roles of FGFs As Paracrine or Endocrine Signals in Liver Development, Health, and Disease

Itoh, N., Nakayama, Y., & Konishi, M. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00030 · Cited by 93 · see citing works

Klotho Coreceptors Inhibit Signaling by Paracrine Fibroblast Growth Factor 8 Subfamily Ligands

Goetz, R., Ohnishi, M., Ding, X., Kurosu, H., Wang, L., Akiyoshi, J., Ma, J.-H., Gai, W.-M., Sidis, Y., Pitteloud, N., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06603-11 · Cited by 76 · see citing works

Biology of Fibroblast Growth Factor 23: From Physiology to PathologyPreprint

Courbebaisse, M., & Lanske, B. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031260 · Cited by 81 · see citing works

β-Klotho gene variation is associated with liver damage in children with NAFLD

Dongiovanni, P., Crudele, A., Panera, N., Romito, I., Meroni, M., Stefanis, C. D., Palma, A., Comparcola, D., Fracanzani, A. L., Miele, L., et al. (2019) · Journal of Hepatology · doi:10.1016/j.jhep.2019.10.011 · Cited by 78 · see citing works

The Saga of Endocrine FGFs

Phan, P., Saikia, B. B., Sonnaila, S., Agrawal, S., Alraawi, Z., Kumar, T. K. S., & Iyer, S. (2021) · Cells · doi:10.3390/cells10092418 · Cited by 67 · see citing works

Decoding FGF/FGFR Signaling: Insights into Biological Functions and Disease Relevance

Edirisinghe, O., Ternier, G., Alraawi, Z., & Kumar, T. K. S. (2024) · Biomolecules · doi:10.3390/biom14121622 · Cited by 60 · see citing works

Is Fibroblast Growth Factor Receptor 4 a Suitable Target of Cancer Therapy?

Heinzle, C. F., Erdem, Z., Paur, J., Grasl‐Kraupp, B., Holzmann, K., Grusch, M., Berger, W., & Marian, B. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113199990594 · Cited by 56 · see citing works

Fibroblast growth factor signaling in macrophage polarization: impact on health and diseases

Shen, L., Li, Y., & Zhao, H. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1390453 · Cited by 54 · see citing works

Role of Fibroblast Growth Factor-23 in Innate Immune Responses

Fitzpatrick, E. A., Han, X., Xiao, Z., & Quarles, L. D. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00320 · Cited by 54 · see citing works

Soluble Expression of Disulfide Bond Containing Proteins FGF15 and FGF19 in the Cytoplasm of Escherichia coli

Kong, B., & Guo, G. L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085890 · Cited by 50 · see citing works

FGF-based drug discovery: advances and challenges

Chen, G., Chen, L., Li, X., & Mohammadi, M. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-01125-w · Cited by 51 · see citing works

The roles of FGF21 in atherosclerosis pathogenesis

Shanehbandpour-Tabari, F., Karimian, A., Parsian, H., Rameshknia, V., Mahmoodpoor, A., Majidinia, M., Maniati, M., & Yousefi, B. (2019) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-019-09488-x · Cited by 41 · see citing works

Fibroblast growth factor 21: An emerging pleiotropic regulator of lipid metabolism and the metabolic network

Li, S., Zou, T., Chen, J., Li, J., & You, J. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.06.033 · Cited by 37 · see citing works

The importance of klotho in phosphate metabolism and kidney disease

Tan, S., Smith, E. R., Hewitson, T. D., Holt, S. G., & Toussaint, N. D. (2014) · Nephrology · doi:10.1111/nep.12268 · Cited by 35 · see citing works

In vitro and in vivo characterization of Recifercept, a soluble fibroblast growth factor receptor 3, as treatment for achondroplasia

Gonçalves, D., Rignol, G., Dellugat, P., Hartmann, G., García, S., Stavenhagen, J. B., Santarelli, L., Gouze, E., & Czech, C. (2020) · PLoS ONE · doi:10.1371/journal.pone.0244368 · Cited by 34 · see citing works

Programmed ageing: decline of stem cell renewal, immunosenescence, and Alzheimer's disease

Lathe, R., & Clair, D. S. (2023) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12959 · Cited by 36 · see citing works

A solid-phase PEGylation strategy for protein therapeutics using a potent FGF21 analog

Song, L., Zhu, Y., Wang, H., Belov, A. A., Niu, J., Shi, L., Xie, Y., Ye, C., Li, X., & Huang, Z. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2014.03.023 · Cited by 32 · see citing works

Paracrine-endocrine FGF chimeras as potent therapeutics for metabolic diseases

Zhao, L., Niu, J., Lin, H., Zhao, J., Liu, Y., Song, Z., Xiang, C., Wang, X., Yang, Y., Li, X., et al. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.09.052 · Cited by 30 · see citing works

Alteration in the serum concentrations of FGF19, FGFR4 and βKlotho in patients with thyroid cancer

Motylewska, E., Stępień, T., Borkowska, M., Kuzdak, K., Siejka, A., Komorowski, J., Stepien, H., & Ławnicka, H. (2018) · Cytokine · doi:10.1016/j.cyto.2018.02.013 · Cited by 27 · see citing works

Advances of Fibroblast Growth Factor/Receptor Signaling Pathway in Hepatocellular Carcinoma and its Pharmacotherapeutic Targets

Wang, H., Yang, J., Zhang, K., Liu, J., Li, Y., Su, W., & Song, N. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.650388 · Cited by 28 · see citing works

Unliganded Fibroblast Growth Factor Receptor 1 Forms Density-independent Dimers

Comps‐Agrar, L., Dunshee, D. R., Eaton, D., & Sonoda, J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.681395 · Cited by 27 · see citing works

Dynamic folding modulation generates FGF21 variant against diabetes

Zhu, L., Zhao, H., Liu, J., Cai, H., Wu, B., Liu, Z., Zhou, S., Liu, Q., Li, X., Bao, B., et al. (2020) · EMBO Reports · doi:10.15252/embr.202051352 · Cited by 23 · see citing works

Fibroblast growth factor 9 subfamily and the heart

Wang, S., Li, Y., Jiang, C., & Tian, H. (2017) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-017-8652-3 · Cited by 23 · see citing works

Differential receptor selectivity of the FGF15/FGF19 orthologues determines distinct metabolic activities in db/db mice

Hansen, A. M. K., Vienberg, S. G., Lykkegaard, K., Zhao, X., Tingqing, G., Han, D., Zhang, X., Thøgersen, H., Sass‐Ørum, K., Tagmose, T. M., et al. (2018) · Biochemical Journal · doi:10.1042/bcj20180555 · Cited by 23 · see citing works

The autocrine role of FGF21 in cultured adipocytes

Justesen, S., Haugegaard, K. V., Hansen, J. B., Hansen, H. S., & Andersen, B. (2020) · Biochemical Journal · doi:10.1042/bcj20200220 · Cited by 23 · see citing works

Is Cerebrospinal Fluid Fibroblast Growth Factor 19 (FGF19) a mood regulator?

Liu, Y., Yu, D., Wang, X., Tan, X., Luo, X., Fan, H., Kang, Y., Xiao, J., Li, X., & Wang, F. (2017) · Neuropsychiatry · doi:10.4172/neuropsychiatry.1000187 · Cited by 22 · see citing works

Regulation of Hormone-Sensitive Renal Phosphate Transport

Gattineni, J., & Friedman, P. A. (2015) · Vitamins and hormones · doi:10.1016/bs.vh.2015.01.002 · Cited by 22 · see citing works

The interoceptive hippocampus: Mouse brain endocrine receptor expression highlights a dentate gyrus (DG)–cornu ammonis (CA) challenge–sufficiency axis

Lathe, R., Singadia, S., Jordan, C. Y., & Riedel, G. (2020) · PLoS ONE · doi:10.1371/journal.pone.0227575 · Cited by 21 · see citing works

Biological role of heparan sulfate in osteogenesis: A review

Xu, Z., Chen, S., Feng, D., Liu, Y., Wang, Q., Gao, T., Liu, Z., Zhang, Y., Chen, J., & Qiu, L. (2021) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2021.118490 · Cited by 21 · see citing works

FGF21 decreases food intake and body weight in obese Göttingen minipigs

Christoffersen, B. Ø., Straarup, E. M., Lykkegaard, K., Fels, J. J., Sass‐Ørum, K., Zhang, X., Raun, K., & Andersen, B. (2018) · Diabetes Obesity and Metabolism · doi:10.1111/dom.13560 · Cited by 19 · see citing works

HDAC Inhibitors Alleviate Uric Acid–Induced Vascular Endothelial Cell Injury by Way of the HDAC6/FGF21/PI3K/AKT Pathway

Wang, K., Zhang, Y., Zhou, M., Du, Y., Li, P., Guan, C., & Huang, Z. (2023) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001372 · Cited by 15 · see citing works

Pegozafermin Is a Potential Master Therapeutic Regulator in Metabolic Disorders: A Review

Bailey, N., Peterson, S. J., Parikh, M. A., Jackson, K. A., & Frishman, W. H. (2023) · Cardiology in Review · doi:10.1097/crd.0000000000000625 · Cited by 15 · see citing works

Exploring endocrine FGFs - structures, functions and biomedical applications

Phan, P. (2024) · International Journal of Biochemistry and Molecular Biology · doi:10.62347/palk2137 · Cited by 15 · see citing works

FGF23 associated bone diseases

Liao, E. (2013) · Frontiers of Medicine · doi:10.1007/s11684-013-0254-6 · Cited by 14 · see citing works

Characterization of FGF21 Sites of Production and Signaling in Mice

Sullivan, A. I., Jensen-Cody, S. O., Claflin, K. E., Vorhies, K., Flippo, K. H., & Potthoff, M. J. (2024) · Endocrinology · doi:10.1210/endocr/bqae120 · Cited by 11 · see citing works

Advances in FGFs for diabetes care applications

Liu, Y., Chen, Q., Li, Y., Bi, L., He, Z., Shao, C., Jin, L., Peng, R., & Zhang, X. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.121015 · Cited by 12 · see citing works

Growth factors and female reproduction in vertebrates

Uju, C. N., & Unniappan, S. (2023) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2023.112091 · Cited by 12 · see citing works

Role of fibroblast growth factor 19 in maintaining nutrient homeostasis and disease.

Zhang, J., Li, H. T., Fang, Q. C., & Jia, W. (2014) · PubMed · doi:10.3967/bes2014.056 · Cited by 11 · see citing works

The Gly385(388)Arg Polymorphism of the FGFR4 Receptor Regulates Hepatic Lipogenesis Under Healthy Diet

Lutz, S. Z., Hennige, A. M., Peter, A., Kovářová, M., Totsikas, C., Machann, J., Kröber, S. M., Sperl, B., Schleicher, E. D., Schick, F., et al. (2018) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2018-01573 · Cited by 8 · see citing works

Lysine tRNA fragments and miR-194-5p co-regulate hepatic steatosis via β-Klotho and perilipin 2

Tzur, Y., Winek, K., Madrer, N., Dubnov, S., Bennett, E. R., Greenberg, D., Hanin, G., Gammal, A., Tam, J., Arkin, I. T., et al. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101856 · Cited by 10 · see citing works

The Role of the FGF19 Family in the Pathogenesis of Gestational Diabetes: A Narrative Review

Sadowska, A., Poniedziałek‐Czajkowska, E., & Mierzyński, R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417298 · Cited by 9 · see citing works

FGFR Aberrations in Solid Tumors: Mechanistic Insights and Clinical Translation of Targeted Therapies

He, Z., Chen, Y., Li, G., Wang, J., Wang, Y., Tu, P., Huang, Y., Zhao, L., Pan, X., Liu, H., et al. (2025) · Cancers · doi:10.3390/cancers18010089 · Cited by 9 · see citing works

Preparation, characterization, and pharmacological study of a novel long-acting FGF21 with a potential therapeutic effect in obesity

Kim, D., Lee, J., Bae, I., Kim, M., Huh, Y., Choi, J., Bae, S., Choi, I. Y., Kim, H. H., & Kim, D. K. (2020) · Biologicals · doi:10.1016/j.biologicals.2020.11.005 · Cited by 9 · see citing works

FGF-Mediated Axon Guidance: Role of Downstream Signaling Pathways in Cytoskeletal Control

Li, J., Gao, H., & Liu, F. (2025) · Cells · doi:10.3390/cells14110777 · Cited by 9 · see citing works

Growth Factor Signaling in Lens Fiber Differentiation

de Iongh, R. U., & Duncan, M. K. (2014) · Springer eBooks · doi:10.1007/978-4-431-54300-8_5 · Cited by 7 · see citing works

A primer on the pleiotropic endocrine fibroblast growth factor FGF19/FGF15

Bouju, A., Nusse, R., & Wu, P. V. (2024) · Differentiation · doi:10.1016/j.diff.2024.100816 · Cited by 7 · see citing works

Identification of a crucial amino acid responsible for the loss of specifying FGFR1–KLB affinity of the iodinated FGF21

Luo, W., Lin, X., Wang, T., Cai, J., Zeng, X., Zhu, C., Li, R., Wang, H., & Wu, X. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26780 · Cited by 6 · see citing works

Development of A Cell-Based Assay to Identify Small Molecule Inhibitors of FGF23 Signaling

Diener, S., Schorpp, K., Strom, T.-M., Hadian, K., & Lorenz‐Depiereux, B. (2015) · Assay and Drug Development Technologies · doi:10.1089/adt.2015.653 · Cited by 6 · see citing works

Fibroblast Growth Factor 21: Mechanisms, Therapeutic Potential, and Clinical Translation in Metabolic Dysfunction

Rama, K., Jahagirdar, V., & Sanyal, A. J. (2026) · Drug Design Development and Therapy · doi:10.2147/dddt.s560034 · Cited by 6 · see citing works

The role of FGF15/FGF19 in the development of the central nervous system, eyes and inner ears in vertebrates.

Hidalgo-Sánchez, M., Sánchez-Guardado, L., Rodríguez-León, J., & Francisco-Morcillo, J. (2024) · Tissue & Cell · doi:10.1016/j.tice.2024.102619 · Cited by 5 · see citing works

One-step metal affinity purification of recombinant hFGF19 without using tags.

Choi, H.-J., Cheong, D., Yoo, S.-K., & Kim, G.-J. (2022) · Protein Expression and Purification · doi:10.1016/j.pep.2022.106186 · Cited by 5 · see citing works

Prediction of the structural interface between fibroblast growth factor23 and Burosumab using alanine scanning and molecular docking

Kanhasut, K., Tharakaraman, K., Ruchirawat, M., Satayavivad, J., Fuangthong, M., & Sasisekharan, R. (2022) · Scientific Reports · doi:10.1038/s41598-022-18580-3 · Cited by 5 · see citing works

FGF21 Is Released During Increased Lipogenesis State Following Rapid-Onset Radioiodine-Induced Hypothyroidism

Szczepańska, E., Glinicki, P., Zgliczyński, W., Slowinska-Srzednicka, J., Jastrzębska, H., & Gietka‐Czernel, M. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.900034 · Cited by 3 · see citing works

Белок Klotho и фактор роста фибробластов FGF23 как маркеры хронической болезни почек

Мельник, А. А. (2017) · KIDNEYS · doi:10.22141/2307-1257.6.3.2017.109027 · Cited by 3 · see citing works

Hormonal Regulation of Epithelial Sodium Channel (ENaC) and Other Nonneuronal Epithelial Ion Channels

Litwack, G. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813814-4.00012-2 · Cited by 3 · see citing works

Growth Factors

Norman, A. W., & Henry, H. L. (2014) · Elsevier eBooks · doi:10.1016/b978-0-08-091906-5.00017-3 · Cited by 3 · see citing works

FGF19 and muscle architecture in older patients

Bres, É., Bouvier, J., Courtay, A., Delaire, L., Humblot, J., Cuerq, C., Tripoz-dit-Masson, S., Fauvernier, M., Gilbert, T., & Bonnefoy, M. (2023) · Experimental Gerontology · doi:10.1016/j.exger.2023.112120 · Cited by 4 · see citing works

The PTH/Vitamin D/FGF23 Axis

Goltzman, D., & Karaplis, A. C. (2015) · Springer eBooks · doi:10.1007/978-88-470-5376-2_8 · Cited by 3 · see citing works

Pharmacology of Gut Hormone Mimetics for Obesity and Diabetes

Lafferty, R. A., O'Harte, F. P. M., Irwin, N., Flatt, P. R., & Gault, V. A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00035-9 · Cited by 3 · see citing works

Structure and modification

Li, X. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15793-6.00004-4 · Cited by 2 · see citing works

The Role of The βklotho Gene, Fgf21 and Fgfr1 in Cancerogenesis

Wójcik‐Krowiranda, K., Szczepaniec, S., & Bieńkiewicz, A. (2018) · Women Health Care and Issues · doi:10.31579/2642-9756/003 · Cited by 1 · see citing works

FGF-FGFR Signaling in Cancer

Mohammadi, M., & Beenken, A. (2017) · Springer eBooks · doi:10.1007/978-1-4419-0717-2_19 · Cited by 1 · see citing works

Study of Molecular Docking and Evolutionary Dynamics of the FGF Gene Family in Nile Tilapia

Khan, M. F., Parveen, S., Manan, M., Latif, F., Haditomo, A. H. C., Xu, Y.-H., Zhu, P., & Shafique, L. (2025) · Marine Biotechnology · doi:10.1007/s10126-025-10546-6 · Cited by 1 · see citing works

The role of FGF23/Klotho in mineral metabolism and chronic kidney disease

Olauson, H. (2013)

FGF-FGFR Signaling in Cancer

Mohammadi, M., & Beenken, A. (2014) · Springer eBooks · doi:10.1007/978-1-4614-6613-0_19-4

Molecular description of fibroblast growth factor and mechanisms by which fibroblast growth factor-21 mediating biological actions and acting as a biologic biomarker of cardiovascular diseases

Melaku, L. S., & Debela, N. (2020) · Indian Journal of Health Sciences and Biomedical Research (KLEU) · doi:10.4103/kleuhsj.kleuhsj_92_20

Structural basis of FGF23 hormone signaling

Zinkle, A., Goetz, R. M., Chen, L., & Mohammadi, M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-818036-5.00002-1

The developing link of metabolic growth factors in insulin resistance

Gao, R., Hassan, W., Shahzadi, A., din, F. U., & Rasheed, H. M. F. (2017) · Journal of Contemporary Pharmacy · doi:10.56770/jcp201705

Research advances in purification, expression, and function of fibroblast growth factor 9

He, X., Zhang, B., Qi, R., Lei, M., & Xu, X. (2025) · Regenesis repair rehabilitation. · doi:10.1016/j.rerere.2025.07.002

Targeting the FGF19/FGFR4 positive feedback loop to disrupt ERK-mediated tumor progression in head and neck cancer

Yang, Y., Yu, P.-L., Chou, C.-Y., & Lin, Y. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07999-1

Cytokines and insulin sensitivity

Khan, F., Akhtar, S., & Kumar, A. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-33590-7.00008-3

Positive actions of fibroblast growth factor 21 on female zebrafish reproductive axis

Uju, C. N., & Unniappan, S. (2026) · Theriogenology · doi:10.1016/j.theriogenology.2026.118106

Canonical and Non-Canonical Regulators of Lipid Metabolism in the Liver and the “Liver–Other Organs” Axes

Kotlyarov, S. N., Котлярова, А. А., Catanzaro, R., & Marotta, F. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27198614

The gastrointestinal KATP-ERK signaling axis: Molecular mechanisms, pharmacological opportunities, and emerging translational technologies

Denora, M., Turi, A. D., Maqoud, F., Antonacci, M., Orlando, A., Drago, S., Malerba, E., Russo, F., & Tricarico, D. (2026) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2026.119986

Fibroblast growth factor 19/15-mediated metabolic regulation supports its drug development potential: a narrative review

Bai, L., Bai, D., Han, L., & Yang, Q. (2026) · Metabolism and Target Organ Damage · doi:10.20517/mtod.2026.128

Molecular Insights into the Klotho-Dependent, Endocrine Mode of Action of Fibroblast Growth Factor 19 Subfamily Members

Goetz, R., Beenken, A., Ibrahimi, O., Kalinina, J., Olsen, S., Eliseenkova, A. V., Xu, C.-F., Neubert, T., Zhang, F.-M., Linhardt, R., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02249-06 · Cited by 544 · see citing works

Molecular Insights into the Klotho-Dependent, Endocrine Mode

Razzaque, M. S., & Mohammadi, M. (2006)

Enabling Endocrine Action of Fibroblast Growth Factors

Ray, L. B. (2007) · Science s STKE · doi:10.1126/stke.3822007tw133 · Cited by 1 · see citing works

Structures of ligand-occupied β-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity

Kuzina, E. S., Ung, P. M. U., Mohanty, J., Tomé, F., Choi, J., Pardon, E., Steyaert, J., Lax, I., Schlessinger, A., Schlessinger, J., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1822055116 · Cited by 41 · see citing works

C-terminal Tail of FGF19 Determines Its Specificity toward Klotho Co-receptors

Wu, X., Lemon, B. D., Li, X., Gupte, J., Weiszmann, J., Stevens, J. L., Hawkins, N., Shen, W. D., Lindberg, R. A., Chen, J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803319200 · Cited by 86 · see citing works