Matrix Extracellular Phosphoglycoprotein (MEPE) Is a New Bone Renal Hormone and Vascularization Modulator

Endocrine regulation of energy metabolism by the skeleton

Lee, N. K., Sowa, H., Hinoi, E., Ferron, M., Ahn, J. D., Confavreux, C., Dacquin, R., Mee, P. J., McKee, M. D., Jung, D. Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.05.047 · Cited by 2,554

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

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

MEPE, a New Gene Expressed in Bone Marrow and Tumors Causing Osteomalacia

Rowe, P. S., de Zoysa, P. A., Dong, R., Wang, H. R., White, K. E., Econs, M. J., & Oudet, C. L. (2000) · Genomics · doi:10.1006/geno.2000.6235 · Cited by 360

Aldosterone impairs vascular reactivity by decreasing glucose-6-phosphate dehydrogenase activity

Leopold, J. A., Dam, A., Maron, B. A., Scribner, A. W., Liao, R., Handy, D. E., Stanton, R. C., Pitt, B., & Loscalzo, J. (2007) · Nature Medicine · doi:10.1038/nm1545 · Cited by 346

Effects of Aldosterone on the Vasculature

Schiffrin, E. L. (2006) · Hypertension · doi:10.1161/01.hyp.0000201443.63240.a7 · Cited by 302

Mouse α1(I)‐collagen promoter is the best known promoter to drive efficient Cre recombinase expression in osteoblast

Dacquin, R., Starbuck, M. W., Schinke, T., & Karsenty, G. (2002) · Developmental Dynamics · doi:10.1002/dvdy.10100 · Cited by 295

Targeted Disruption of the Osteoblast/Osteocyte Factor 45 Gene (OF45) Results in Increased Bone Formation and Bone Mass

Gowen, L. C., Petersen, D. N., Mansolf, A. L., Qi, H., Stock, J. L., Tkalcevic, G. T., Simmons, H. A., Crawford, D. T., Chidsey-Frink, K. L., Ke, H. Z., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m203250200 · Cited by 295

Angiotensin II accelerates osteoporosis by activating osteoclasts

Shimizu, H., Nakagami, H., Osako, M. K., Hanayama, R., Kunugiza, Y., Kizawa, T., Tomita, T., Yoshikawa, H., Ogihara, T., & Morishita, R. (2008) · The FASEB Journal · doi:10.1096/fj.07-098954 · Cited by 294

MEPE has the properties of an osteoblastic phosphatonin and minhibin

Rowe, P. S., Kumagai, Y., Gutierrez, G., Garrett, I. R., Blacher, R. W., Rosen, D., Cundy, J., Navvab, S., Chen, D., Drezner, M. K., et al. (2003) · Bone · doi:10.1016/j.bone.2003.10.005 · Cited by 268

The Osteocyte: An Endocrine Cell … and More

Dallas, S. L., Prideaux, M., & Bonewald, L. F. (2013) · Endocrine Reviews · doi:10.1210/er.2012-1026 · Cited by 1,042

Inflammation and functional iron deficiency regulate fibroblast growth factor 23 production

David, V., Martin, A., Isakova, T., Spaulding, C., Qi, L., Ramirez, V., Zumbrennen‐Bullough, K. B., Sun, C. C., Lin, H. Y.-F., Babitt, J. L., et al. (2015) · Kidney International · doi:10.1038/ki.2015.290 · Cited by 495

Bone proteins PHEX and DMP1 regulate fibroblastic growth factor Fgf23 expression in osteocytes through a common pathway involving FGF receptor (FGFR) signaling

Martin, A., Liu, S., David, V., Li, H., Karydis, A., Feng, J. Q., & Quarles, L. D. (2011) · The FASEB Journal · doi:10.1096/fj.10-177816 · Cited by 254

The importance of the SIBLING family of proteins on skeletal mineralisation and bone remodelling

Staines, K. A., MacRae, V. E., & Farquharson, C. (2012) · Journal of Endocrinology · doi:10.1530/joe-12-0143 · Cited by 249

A Comparative Transcriptome Analysis Identifying FGF23 Regulated Genes in the Kidney of a Mouse CKD Model

Dai, B., David, V., Martin, A., Huang, J., Li, H., Jiao, Y., Gu, W., & Quarles, L. D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044161 · Cited by 195

Regulation of bone-renal mineral and energy metabolism: the PHEX, FGF23, DMP1, MEPE ASARM pathway

Rowe, P. S. N. (2012) · Critical Reviews™ in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v22.i1.50 · Cited by 173

Novel biological markers of bone: from bone metabolism to bone physiology

Chapurlat, R. D., & Confavreux, C. B. (2016) · Rheumatology · doi:10.1093/rheumatology/kev410 · Cited by 131

Endocrine role of bone: recent and emerging perspectives beyond osteocalcin

Oldknow, K. J., MacRae, V. E., & Farquharson, C. (2015) · Journal of Endocrinology · doi:10.1530/joe-14-0584 · Cited by 112

Biomineralization of bone: a fresh view of the roles of non-collagenous proteins

Gorski, J. P. (2011) · Frontiers in bioscience · doi:10.2741/3875 · Cited by 116

Inhibition of Osteoclastogenesis by Mechanically Loaded Osteocytes: Involvement of MEPE

Kulkarni, R. N., Bakker, A. D., Everts, V. E., & Klein‐Nulend, J. (2010) · Calcified Tissue International · doi:10.1007/s00223-010-9407-7 · Cited by 104

Increased Osteopontin Contributes to Inhibition of Bone Mineralization in FGF23-Deficient Mice

Yuan, Q., Jiang, Y., Zhao, X., Sato, T., Densmore, M., Schüler, C., Erben, R. G., McKee, M. D., & Lanske, B. (2013) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2079 · Cited by 104

The role of the SIBLING, Bone Sialoprotein in skeletal biology — Contribution of mouse experimental genetics

Bouleftour, W., Juignet, L., Bouet, G., Granito, R. N., Vanden‐Bossche, A., Laroche, N., Aubin, J. E., Lafage‐Proust, M., Vico, L., & Malaval, L. (2016) · Matrix Biology · doi:10.1016/j.matbio.2015.12.011 · Cited by 99

Microcalcifications in breast cancer: Lessons from physiological mineralization

Cox, R. F., & Morgan, M. P. (2013) · Bone · doi:10.1016/j.bone.2013.01.013 · Cited by 97

Bone mineralization

BONUCCI, E. (2011) · Frontiers in bioscience · doi:10.2741/3918 · Cited by 97

Structure and quantification of microvascularisation within mouse long bones: What and how should we measure?

Roche, B., David, V., Vanden‐Bossche, A., Peyrin, F., Malaval, L., Vico, L., & Lafage‐Proust, M. (2011) · Bone · doi:10.1016/j.bone.2011.09.051 · Cited by 83

RNA sequencing-based analysis of the laying hen uterus revealed the novel genes and biological pathways involved in the eggshell biomineralization

Sah, N., Kuehu, D. L., Khadka, V. S., Deng, Y., Peplowska, K., Jha, R., & Mishra, B. (2018) · Scientific Reports · doi:10.1038/s41598-018-35203-y · Cited by 80

Extracellular matrix mineralization in periodontal tissues: Noncollagenous matrix proteins, enzymes, and relationship to hypophosphatasia and X‐linked hypophosphatemia

McKee, M. D., Hoac, B., Addison, W. N., Barros, N. M. T., Millán, J. L., & Chaussain, C. (2013) · Periodontology 2000 · doi:10.1111/prd.12029 · Cited by 73

MEPE-Derived ASARM Peptide Inhibits Odontogenic Differentiation of Dental Pulp Stem Cells and Impairs Mineralization in Tooth Models of X-Linked Hypophosphatemia

Salmon, B. J. R., Bardet, C., Khaddam, M., Jiar, N., Coyac, B. R., Baroukh, B., Letourneur, F., Lesieur, J., Decup, F., Denmat, D. L., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056749 · Cited by 69

Bmp2 gene in osteoblasts of periosteum and trabecular bone links bone formation to vascularization and mesenchymal stem cells

Yang, W., Guo, D., Harris, M. A., Cui, Y., Gluhak‐Heinrich, J., Wu, J., Chen, X., Skinner, C., Nyman, J. S., Edwards, J., et al. (2013) · Journal of Cell Science · doi:10.1242/jcs.118596 · Cited by 67

Fibroblast growth factor 23 and its role in phosphate homeostasis

Ramon, I., Kleynen, P., Body, J., & Karmali, R. (2009) · European Journal of Endocrinology · doi:10.1530/eje-09-0597 · Cited by 68

The chicken or the egg: PHEX, FGF23 and SIBLINGs unscrambled

Rowe, P. S. (2012) · Cell Biochemistry and Function · doi:10.1002/cbf.2841 · Cited by 72

MEPE’s Diverse Effects on Mineralization

Boskey, A. L., Chiang, P., Fermanis, A., Brown, J. M., Taleb, H., David, V., & Rowe, P. S. (2009) · Calcified Tissue International · doi:10.1007/s00223-009-9313-z · Cited by 64

ASARM peptides: PHEX-dependent and -independent regulation of serum phosphate

David, V., Martin, A., Hedge, A.-M., Drezner, M. K., & Rowe, P. S. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00304.2010 · Cited by 61

Acute Adaption to Oral or Intravenous Phosphate Requires Parathyroid Hormone

Thomas, L., Bettoni, C., Knöpfel, T., Hernando, N., Biber, J., & Wagner, C. A. (2016) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016010082 · Cited by 59

The Regulatory Role of Matrix Proteins in Mineralization of Bone

Boskey, A. L., & Robey, P. G. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-415853-5.00011-x · Cited by 59

The Osteocyte as the New Discovery of Therapeutic Options in Rare Bone Diseases

Pathak, J. L., Bravenboer, N., & Klein‐Nulend, J. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00405 · Cited by 57

MEPE is a novel regulator of growth plate cartilage mineralization

Staines, K. A., Mackenzie, N. C. W., Clarkin, C. E., Zelenchuk, L. V., Rowe, P. S., MacRae, V. E., & Farquharson, C. (2012) · Bone · doi:10.1016/j.bone.2012.06.022 · Cited by 52

Interactions between osteopontin and vascular endothelial growth factor: Implications for cancer

Ramchandani, D., & Weber, G. F. (2015) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2015.02.003 · Cited by 47

News on Biomarkers in CKD‐MBD

Mazzaferro, S., Tartaglione, L., Rotondi, S., Bover, J., Goldsmith, D. J. A., & Pasquali, M. (2014) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2014.09.006 · Cited by 47

Bone Matrix Proteins and Mineralization Process

Tamma, R., Carbone, C., & Colucci, S. C. (2013) · Springer eBooks · doi:10.1007/978-88-470-5483-7_2 · Cited by 47

The bone–vascular axis in chronic kidney disease

Demer, L. L., & Tintut, Y. (2010) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0b013e32833a3d67 · Cited by 45

Overexpression of the DMP1 C-Terminal Fragment Stimulates FGF23 and Exacerbates the Hypophosphatemic Rickets Phenotype in Hyp Mice

Martin, A., David, V., Li, H., Dai, B., Feng, J. Q., & Quarles, L. D. (2012) · Molecular Endocrinology · doi:10.1210/me.2012-1062 · Cited by 43

FAM20C Overview: Classic and Novel Targets, Pathogenic Variants and Raine Syndrome Phenotypes

Lara, I. P., Pérez-Ramírez, M., Alonso-Themann, P. G., Espinosa-García, A. M., Godínez-Aguilar, R., Bonilla‐Delgado, J., López-Ornelas, A., Victoria-Acosta, G., Olguín‐García, M. G., Moreno, J. G., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158039 · Cited by 40

Regulation and Reconstruction of Cell Phenotype Gradients Along the Tendon‐Bone Interface

Dang, G., Qin, W., Wan, Q., Gu, J., Wang, K., Mu, Z., Gao, B., Jiao, K., Tay, F. R., & Niu, L. (2022) · Advanced Functional Materials · doi:10.1002/adfm.202210275 · Cited by 40

The phosphate transporter NaPi-IIa determines the rapid renal adaptation to dietary phosphate intake in mouse irrespective of persistently high FGF23 levels

Bourgeois, S., Capuano, P., Stange, G., Mühlemann, R., Murer, H., Biber, J., & Wagner, C. A. (2013) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-013-1298-9 · Cited by 37

Abnormal Presence of the Matrix Extracellular Phosphoglycoprotein-Derived Acidic Serine- and Aspartate-Rich Motif Peptide in Human Hypophosphatemic Dentin

Boukpessi, T., Gaucher, C., Léger, T., Salmon, B. J. R., Faouder, J. L., Willig, C., Rowe, P. S., Garabédian, M., Meilhac, O., & Chaussain, C. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.091231 · Cited by 39

Age dependent regulation of bone-mass and renal function by the MEPE ASARM-motif

Zelenchuk, L. V., Hedge, A.-M., & Rowe, P. S. (2015) · Bone · doi:10.1016/j.bone.2015.05.030 · Cited by 38

Dietary phosphate restriction suppresses phosphaturia but does not prevent FGF23 elevation in a mouse model of chronic kidney disease

Zhang, S., Gillihan, R., He, N., Fields, T. A., Liu, S., Green, T. M., & Stubbs, J. R. (2013) · Kidney International · doi:10.1038/ki.2013.194 · Cited by 37

Matrix extracellular phosphoglycoprotein is expressed in causative tumors of oncogenic osteomalacia

Imanishi, Y., Hashi­moto, J., Ando, W., Kobayashi, K., Ueda, T., Nagata, Y., Miyauchi, A., Koyano, H. M., Kaji, H., Saito, T., et al. (2011) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-011-0290-8 · Cited by 34

Utility of temporal profiles of new cardio-renal and pulmonary candidate biomarkers in chronic heart failure

Branković, M., Akkerhuis, K. M., Mouthaan, H., Constantinescu, A. A., Çalişkan, K., van Ramshorst, J., Germans, T., Umans, V. A. W. M., & Kardys, I. (2018) · International Journal of Cardiology · doi:10.1016/j.ijcard.2018.08.001 · Cited by 32

MEPE loss-of-function variant associates with decreased bone mineral density and increased fracture risk

Surakka, I. L., Fritsche, L. G., Zhou, W., Backman, J., Kosmicki, J. A., Lu, H., Brumpton, B. M., Nielsen, J. B., Gabrielsen, M. E., Skogholt, A. H., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17315-0 · Cited by 33

Deletion of OPN in BSP knockout mice does not correct bone hypomineralization but results in high bone turnover

Bouleftour, W., Juignet, L., Verdière, L., Machuca‐Gayet, I., Thomas, M., Laroche, N., Vanden‐Bossche, A., Farlay, D., Thomas, C., Gineyts, É., et al. (2018) · Bone · doi:10.1016/j.bone.2018.12.001 · Cited by 30

In vivo impact of Dlx3 conditional inactivation in neural crest‐derived craniofacial bones

Duverger, O., Isaac, J., Zah, A., Hwang, J., Berdal, A., Lian, J. B., & Morasso, M. I. (2012) · Journal of Cellular Physiology · doi:10.1002/jcp.24175 · Cited by 29

A unified model for bone–renal mineral and energy metabolism

Rowe, P. S. (2015) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2015.03.006 · Cited by 27

Direct micropuncture evidence that matrix extracellular phosphoglycoprotein inhibits proximal tubular phosphate reabsorption

Shirley, D. G., Faria, N., Unwin, R. J., & Dobbie, H. (2010) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfq263 · Cited by 27

Variants affecting diverse domains of MEPE are associated with two distinct bone disorders, a craniofacial bone defect and otosclerosis

Schrauwen, I., Valgaeren, H., Tomás‐Roca, L., Sommen, M., Altunoğlu, U., Wesdorp, M., Beyens, M., Fransén, E., Nasır, A., Vandeweyer, G., et al. (2018) · Genetics in Medicine · doi:10.1038/s41436-018-0300-5 · Cited by 23

Surface immobilization of MEPE peptide onto HA/β‐TCP ceramic particles enhances bone regeneration and remodeling

Acharya, B., Chun, S., Kim, S., Moon, C., Shin, H., & Park, E. K. (2012) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.32648 · Cited by 22

Interactions between osteopontin and vascular endothelial growth factor: Implications for skeletal disorders

Ramchandani, D., & Weber, G. F. (2015) · Bone · doi:10.1016/j.bone.2015.05.047 · Cited by 21

Antagonism Between PEDF and TGF-β Contributes to Type VI Osteogenesis Imperfecta Bone and Vascular Pathogenesis

Kang, H., C, S. A. A., Barnes, A. M., Martin, A., David, V., Crawford, S. E., & Marini, J. C. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.4540 · Cited by 21

MEPE Localization in the Craniofacial Complex and Function in Tooth Dentin Formation

Gullard, A., Gluhak-Heinrich, J., Papagerakis, S., Sohn, P., Unterbrink, A., Chen, S., & MacDougall, M. (2016) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155416635569 · Cited by 20

Increased Expression of Matrix Extracellular Phosphoglycoprotein (MEPE) in Cortical Bone of the Rat Tibia after Mechanical Loading: Identification by Oligonucleotide Microarray

Reijnders, C. M. A., van Essen, H. W., van Rens, B. T. T. M., van Beek, H., Ylstra, B., Blankenstein, M. A., Lips, P. T. A. M., & Bravenboer, N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079672 · Cited by 20

PHEX Mimetic (SPR4-Peptide) Corrects and Improves HYP and Wild Type Mice Energy-Metabolism

Zelenchuk, L. V., Hedge, A.-M., & Rowe, P. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0097326 · Cited by 18

An in situ hybridization study of perlecan, DMP1, and MEPE in developing condylar cartilage of the fetal mouse mandible and limb bud cartilage

Fujikawa, K., Yokohama‐Tamaki, T., Morita, T., Baba, O., Qin, C., & Shibata, S. (2015) · European Journal of Histochemistry · doi:10.4081/ejh.2015.2553 · Cited by 19

Clinical Disorders of Phosphate Homeostasis

Hansen, K. E., & Drezner, M. K. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-381978-9.10063-0 · Cited by 17

Calcium-dependent activation of PHEX, MEPE and DMP1 in osteocytes

Donmez, B., Karagur, E., Donmez, A., Choi, J., & Akkus, O. (2022) · Molecular Medicine Reports · doi:10.3892/mmr.2022.12876 · Cited by 14

Kidney stone formation in a novel murine model of polycystic kidney disease

Riddle, H. A., Zhang, S., Qian, F., Williams, J. C., Stubbs, J. R., Rowe, P. S., & Parnell, S. C. (2022) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00165.2021 · Cited by 15

Do ASARM peptides play a role in nephrogenic systemic fibrosis?

Rowe, P. S., Zelenchuk, L. V., Laurence, J. S., Lee, P., Brooks, W. M., & McCarthy, E. T. (2015) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00201.2015 · Cited by 15

Two Novel FAM20C Variants in a Family with Raine Syndrome

Hernández‐Zavala, A., Cortés-Camacho, F., Lara, I. P., Godínez-Aguilar, R., Espinosa-García, A. M., Duran, J. P., Villanueva-Ocampo, P., Ugarte-Briones, C., Serrano-Bello, C. A., Sánchez-Santiago, P. J., et al. (2020) · Genes · doi:10.3390/genes11020222 · Cited by 15

Pigment epithelium derived factor regulates human Sost/Sclerostin and other osteocyte gene expression via the receptor and induction of Erk/GSK-3beta/beta-catenin signaling

Feng, L., Cain, J. D., Tombran‐Tink, J., & Niyibizi, C. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.07.034 · Cited by 15

Hypophosphatemia Related to Paraneoplastic Cushing Syndrome in Prostate Cancer: Cure After Bilateral Adrenalectomy

Ramon, I., Kleynen, P., Valsamis, J., Body, J., & Karmali, R. (2011) · Calcified Tissue International · doi:10.1007/s00223-011-9527-8 · Cited by 14

SPR4-peptide alters bone metabolism of normal and HYP mice

Zelenchuk, L. V., Hedge, A.-M., & Rowe, P. S. (2014) · Bone · doi:10.1016/j.bone.2014.11.011 · Cited by 14

Remodeling process in bone of aged rats in response to resistance training

de Farias, G. C., Neto, I. V. D. S., Guzzoni, V., Pisani, G. F. D., Royer, C., de Lima, C. L., Neves, F. D. A. R., Bogni, F. H., Nonaka, K. O., Durigan, J. L. Q., et al. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118008 · Cited by 15

Effect of organic and inorganic dietary selenium supplementation on gene expression in oviduct tissues and Selenoproteins gene expression in Lohman Brown-classic laying hens

Muhammad, A. I., Dalia, A. M., Loh, T. C., Akit, H., & Samsudin, A. A. (2021) · BMC Veterinary Research · doi:10.1186/s12917-021-02964-0 · Cited by 13

Verbascoside Inhibits/Repairs the Damage of LPS-Induced Inflammation by Regulating Apoptosis, Oxidative Stress, and Bone Remodeling

Akyer, Ş. P., Karagür, E. R., Tunç-Ata, M., Kılıç-Toprak, E., Çört, A., & Dönmez, B. Ö. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45110550 · Cited by 12

Resveratrol prevents ovariectomy-induced bone quality deterioration by improving the microarchitectural and biophysicochemical properties of bone

Öztürk, Ş., Cüneyit, İ., Altıntaş, F., Karagür, E. R., Donmez, A. C., Ocak, M., Ünal, M., Sarıkanat, M., & Dönmez, B. Ö. (2023) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-023-01416-z · Cited by 12

ASARM mineralization hypothesis: A bridge too far?

David, V., & Quarles, L. D. (2010) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.69 · Cited by 9

The Intricacies of Renal Phosphate Reabsorption—An Overview

Walker, V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094684 · Cited by 10

Cross-Species RNA-Seq Study Comparing Transcriptomes of Enriched Osteocyte Populations in the Tibia and Skull

Wang, N., Niger, C., Li, N., Richards, G. O., & Skerry, T. M. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.581002 · Cited by 10

The Bioactive Acidic Serine- and Aspartate-Rich Motif Peptide

Minamizaki, T., & Yoshiko, Y. (2015) · Current Protein and Peptide Science · doi:10.2174/1389203716666150206122839 · Cited by 9

Kbus/Idr, a mutant mouse strain with skeletal abnormalities and hypophosphatemia: Identification as an allele of 'Hyp'

Moriyama, K., Hanai, A., Mekada, K., Yoshiki, A., Ogiwara, K., Kimura, A. P., & Takahashi, T. (2011) · Journal of Biomedical Science · doi:10.1186/1423-0127-18-60 · Cited by 10

Isolation of Primary Avian Osteocytes

Semeins, C. M., Bakker, A. D., & Klein‐Nulend, J. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-415-5_4 · Cited by 9

Pigment epithelium-derived factor (PEDF) reduced expression and synthesis of SOST/sclerostin in bone explant cultures: implication of PEDF-osteocyte gene regulation in vivo

Li, F., Cain, J. D., Tombran‐Tink, J., & Niyibizi, C. (2019) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-018-0982-4 · Cited by 9

High-throughput targeted proteomics discovery approach and spontaneous reperfusion in ST-segment elevation myocardial infarction

Shavadia, J., Granger, C. B., Alemayehu, W. G., Westerhout, C. M., Povsic, T. J., Brener, S. J., van Diepen, S., deFilippi, C. R., & Armstrong, P. W. (2019) · American Heart Journal · doi:10.1016/j.ahj.2019.09.015 · Cited by 9

Active sites of human MEPE-ASARM regulating bone matrix mineralization

Minamizaki, T., Sakurai, K., Hayashi, I., Toshishige, M., Yoshioka, H., Kozai, K., & Yoshiko, Y. (2020) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2020.110931 · Cited by 8

PHEXL222P Mutation Increases Phex Expression in a New ENU Mouse Model for XLH Disease

Hakam, C. E., Parenté, A., Baraige, F., Magnol, L., Forestier, L., Meo, F. D., & Blanquet, V. (2022) · Genes · doi:10.3390/genes13081356 · Cited by 8

Comprehensive phenotyping of cutaneous afferents reveals early-onset alterations in nociceptor response properties, release of CGRP, and hindpaw edema following spinal cord injury

Eller, O. C., Stair, R. N., Neal, C. A., Rowe, P. S., Nelson‐Brantley, J., Young, E. E., & Baumbauer, K. M. (2022) · Neurobiology of Pain · doi:10.1016/j.ynpai.2022.100097 · Cited by 8

Correction of Vascular Calcification and Hyperphosphatemia in CKD Rats Treated with ASARM Peptide

Rowe, P. S., McCarthy, E. M., Yu, A. S. L., & Stubbs, J. R. (2022) · Kidney360 · doi:10.34067/kid.0002782022 · Cited by 7

Radiation activated CHK1/MEPE pathway may contribute to microgravity-induced bone density loss

Zhang, X., Wang, P., & Wang, Y. (2015) · Life Sciences in Space Research · doi:10.1016/j.lssr.2015.08.004 · Cited by 6

Fibroblast Growth Factor-23 and Matrix Extracellular Phosphoglycoprotein Levels in Healthy Children and, Pregnant and Puerperal Women

Ozsen, A., Furman, A., Güran, T., Bereket, A., & Turan, S. (2019) · Hormone Research in Paediatrics · doi:10.1159/000506477 · Cited by 6

The Effects of Inorganic Phosphorus Levels on Phosphorus Utilization, Local Bone-Derived Regulators, and BMP/MAPK Pathway in Primary Cultured Osteoblasts of Broiler Chicks

Li, T., Cao, S., Liao, X., Shao, Y., Zhang, L., Lü, L., Liu, Z., & Luo, X. (2022) · Frontiers in Veterinary Science · doi:10.3389/fvets.2022.855405 · Cited by 5

Bone Shaft Revascularization After Marrow Ablation Is Dramatically Accelerated in BSP‐/‐ Mice, Along With Faster Hematopoietic Recolonization

Bouleftour, W., Granito, R. N., Vanden‐Bossche, A., Sabido, O., Roche, B., Thomas, M., Linossier, M., Aubin, J. E., Lafage‐Proust, M., Vico, L., et al. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25630 · Cited by 5

Low, but Not High, Pulsating Fluid Shear Stress Affects Matrix Extracellular Phosphoglycoprotein Expression, Mainly via Integrin β Subunits in Pre-Osteoblasts

Jin, J., & Zandieh‐Doulabi, B. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46110738 · Cited by 4

Oncogenic osteomalacia associated with phosphaturic mesenchymal tumour, mixed connective tissue type of the knee.

Szumera‐Ciećkiewicz, A., Ptaszyński, K., Pawełas, A., & Rutkowski, P. L. (2009) · PubMed · Cited by 4

FAM20C: A key protein kinase in multiple diseases

Zhang, R., Ren, Y., Ju, Y., Zhang, Y., Zhang, Y., & Wang, Y. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.101179 · Cited by 3

The Role of Non-collagenous Proteins and Other Matrix Molecules in Vertebrate Mineralization

Shapiro, I. M., & Landis, W. J. (2023) · Springer eBooks · doi:10.1007/978-3-031-34304-9_8 · Cited by 4

3D genomic alterations during development of skeletal muscle in chicken

Xu, Z., Wang, T., Zhu, W., Yang, M., Leng, D., Li, Z., Zhang, J., Liu, P., Wu, Z., He, M., et al. (2024) · Journal of Integrative Agriculture · doi:10.1016/j.jia.2024.03.052 · Cited by 3

Heritable Renal Phosphate Wasting Disorders

Drezner, M. K., & Whyte, M. P. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804182-6.00040-x · Cited by 3

Fisiología del tejido óseo

Levasseur, R. (2019) · EMC - Aparato Locomotor · doi:10.1016/s1286-935x(19)42130-8 · Cited by 2

Fisiología del tejido óseo

Levasseur, R. (2019) · EMC - Podología · doi:10.1016/s1762-827x(19)42712-0 · Cited by 1

Gene Polymorphisms Associated with Osteoarthritis: Potential Implications for Nutrigenetics and Precision Nutrition

Mariano, A., d’Abusco, A. S., & Ammendola, S. (2026) · Nutrients · doi:10.3390/nu18061003 · Cited by 1

Heritable Renal Phosphate Wasting Disorders

Drezner, M. K. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-387829-8.00032-9 · Cited by 1

Biomarkers Associated with Worsening Renal Function and Progression in Chronic Kidney Disease among Patients Hospitalized for Acute Heart Failure

Ohlsson, M. A., Molvin, J., Isholth, H. H., Nezami, Z., Laučytė-Cibulskienė, A., Christensson, A. G., Jujić, A., & Magnusson, M. (2025) · Cardiorenal Medicine · doi:10.1159/000546236 · Cited by 1

A Synopsis of Phosphate Disorders in the Nursing Home

Xing, X. S., Yamaguchi, D. T., & Weintraub, N. T. (2010) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2009.10.007 · Cited by 1

Bone Cell Function: A Review

Nguyen, H. N., & Kampa, N. (2013) · The Thai Journal of Veterinary Medicine · doi:10.56808/2985-1130.2488 · Cited by 1

Sex-specific gene expression signatures of calcific aortic valve stenosis in a large collection of human tissues

Houessou, U., Zamani, P., Manikpurage, H. D., Li, Z., Gaudreault, N., Dahmene, M., Dagenais, F., Couture, C., Clavel, M.-A., Pibarot, P., et al. (2026) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2026.120791 · Cited by 1

Comparação das características clínicas, bioquímicas e da análise histomorfométrica de biópsias ósseas de pacientes com doença renal crônica em diálise com e sem fratura

Santos, M. F. P. (2017) · doi:10.11606/d.5.2017.tde-22092017-153920

Efeitos da paratireoidectomia na biologia do tecido ósseo de pacientes com doença renal crônica e hiperparatireoidismo secundário

Pires, G. O. (2018) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.5.2018.tde-08052018-114855

Raine Syndrome and FAM20C Variants in a Mexican Family

Palacios‐Reyes, C., Espinosa-García, A. M., Lara, I. P., Godínez-Aguilar, R., Duran, J. P., Alonso-Themann, P. G., Hernández‐Zavala, A., Cortés-Camacho, F., Villanueva-Ocampo, P., Ugarte-Briones, C., et al. (2020) · Vide Leaf, Hyderabad eBooks · doi:10.37247/pag.1.2020.9

Effect of Organic and Inorganic Dietary Selenium Supplementation on Gene Expression in Oviduct Tissues and, Antioxidant Capacity of Laying HensPreprint

Muhammad, A. I., Dalia, A. M., Loh, T. C., Akit, H., & Samsudin, A. A. (2020) · Research Square · doi:10.21203/rs.3.rs-127962/v1

Comprehensive Phenotyping of Cutaneous Afferents Reveals Rapid-Onset Alterations in Nociceptor Response Properties Following Spinal Cord InjuryPreprint

Eller, O. C., Stair, R. N., Neal, C. A., Rowe, P. S., Nelson‐Brantley, J., Young, E. E., & Baumbauer, K. M. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.15.448577

MEPE has the properties of an osteoblastic phosphatonin and minhibin

Rowe, P. S., Kumagai, Y., Gutierrez, G., Garrett, I. R., Blacher, R. W., Rosen, D., Cundy, J., Navvab, S., Chen, D., Drezner, M. K., et al. (2003) · Bone · doi:10.1016/j.bone.2003.10.005 · Cited by 268

Age dependent regulation of bone-mass and renal function by the MEPE ASARM-motif

Zelenchuk, L. V., Hedge, A.-M., & Rowe, P. S. (2015) · Bone · doi:10.1016/j.bone.2015.05.030 · Cited by 38

Gingko biloba extract (EGb 761): Pharmacological activities and clinical applications

Stewart, A. G. (1992) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(92)90102-c · Cited by 15

Molecular Regulation of Matrix Extracellular Phosphoglycoprotein Expression by Bone Morphogenetic Protein-2

Cho, Y., Yoon, W., Woo, K. M., Baek, J., Lee, G., Cho, J., & Ryoo, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.008391 · Cited by 38

A Synthetic Peptide Fragment of Human MEPE Stimulates New Bone Formation In Vitro and In Vivo

Hayashibara, T., Hiraga, T., Yi, B., Nomizu, M., Kumagai, Y., Nishimura, R., & Yoneda, T. (2004) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.0301263 · Cited by 70