The origins and formation of bone-resorbing osteoclasts

Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation.

Lacey, D. L., Timms, E., Tan, H.-L., Kelley, M. J., Dunstan, C. R., Burgess, T., Elliott, R., Colombero, A., Elliott, G., Scully, S., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81569-x · Cited by 5,439

Osteoprotegerin: a novel secreted protein involved in the regulation of bone density.

Simonet, W. S., Lacey, D. L., Dunstan, C. R., Kelley, M., Chang, M.-S., Lüthy, R., Nguyen, H. Q., Wooden, S., Bennett, L., Boone, T., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)80209-3 · Cited by 5,130

Osteoclast differentiation factor is a ligand for osteoprotegerin/osteoclastogenesis-inhibitory factor and is identical to TRANCE/RANKL

Yasuda, H., Shima, N., Nakagawa, N., Yamaguchi, K., Kinosaki, M., Mochizuki, S.-I., Tomoyasu, A., Yano, K., Goto, M., Murakami, A., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3597 · Cited by 4,224

OPGL is a key regulator of osteoclastogenesis, lymphocyte development and lymph node organogenesis.

Kong, Y.-Y., Yoshida, H., Sarosi, I., Tan, H.-L., Timms, E., Capparelli, C., Morony, S., Oliveira-dos-Santos, A. J., Van, G., Itie, A., et al. (1999) · Nature · doi:10.1038/16852 · Cited by 3,351

Induction and Activation of the Transcription Factor NFATc1 (NFAT2) Integrate RANKL Signaling in Terminal Differentiation of Osteoclasts

Takayanagi, H., Kim, S., Koga, T., Nishina, H., Isshiki, M., Yoshida, H., Saiura, A., Isobe, M., Yokochi, T., Inoue, J.-I., et al. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00369-6 · Cited by 2,701

Osteoprotegerin-deficient mice develop early onset osteoporosis and arterial calcification.

Bucay, N., Sarosi, I., Dunstan, C. R., Morony, S., Tarpley, J., Capparelli, C., Scully, S., Tan, H. L., Xu, W., Lacey, D. L., et al. (1998) · Genes & Development · doi:10.1101/gad.12.9.1260 · Cited by 2,483

Osteoporosis

Compston, J. E., McClung, M. R., & Leslie, W. D. (2019) · The Lancet · doi:10.1016/s0140-6736(18)32112-3 · Cited by 2,449

A homologue of the TNF receptor and its ligand enhance T-cell growth and dendritic-cell function.

Anderson, D. M., Maraskovsky, E., Billingsley, W. L., Dougall, W. C., Tometsko, M. E., Roux, E. R., Teepe, M. C., DuBose, R. F., Cosman, D., & Galibert, L. (1997) · Nature · doi:10.1038/36593 · Cited by 2,290

The murine mutation osteopetrosis is in the coding region of the macrophage colony stimulating factor gene

Yoshida, H., Hayashi, S.-I., Kunisada, T., Ogawa, M., Nishikawa, S., Okamura, H., Sudo, T., Shultz, L. D., & Nishikawa, S.-I. (1990) · Nature · doi:10.1038/345442a0 · Cited by 1,789

Therapeutic Approaches to Bone Diseases

Rodan, G. A., & Martin, T. J. (2000) · Science · doi:10.1126/science.289.5484.1508 · Cited by 1,767

Syncytin is a captive retroviral envelope protein involved in human placental morphogenesis

Mi, S., Lee, X., Li, X., Veldman, G. M., Finnerty, H. F., Collins‐Racie, L. A., LaVallie, E. R., Tang, X.-Y., Edouard, P., Howes, S., et al. (2000) · Nature · doi:10.1038/35001608 · Cited by 1,711

Tumor necrosis factor receptor family member RANK mediates osteoclast differentiation and activation induced by osteoprotegerin ligand.

Hsu, H., Lacey, D. L., Dunstan, C. R., Solovyev, I., Colombero, A., Timms, E., Tan, H.-L., Elliott, G., Kelley, M. J., Sarosi, I., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3540 · Cited by 1,636

RANK is essential for osteoclast and lymph node development.

Dougall, W. C., Glaccum, M., Charrier, K., Rohrbach, K., Brasel, K., De Smedt, T., Daro, E., Smith, J., Tometsko, M. E., Maliszewski, C. R., et al. (1999) · Genes & Development · doi:10.1101/gad.13.18.2412 · Cited by 1,478

c-Fos: a Key Regulator of Osteoclast-Macrophage Lineage Determination and Bone Remodeling

Grigoriadis, A. E., Wang, Z., Cecchini, M. G., Hofstetter, W., Felix, R., Fleisch, H. A., & Wagner, E. F. (1994) · Science · doi:10.1126/science.7939685 · Cited by 1,264

RANKL–RANK signaling in osteoclastogenesis and bone disease

Wada, T., Nakashima, T., Nishina, H., & Penninger, J. M. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.11.007 · Cited by 1,230

RANK is the intrinsic hematopoietic cell surface receptor that controls osteoclastogenesis, and regulation of bone mass and calcium metabolism.

Li, J., Sarosi, I., Yan, X.-Q., Morony, S., Capparelli, C., Tan, H.-L., McCabe, S., Elliott, R., Scully, S., Van, G., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1566 · Cited by 1,119

Origin of osteoclasts: mature monocytes and macrophages are capable of differentiating into osteoclasts under a suitable microenvironment prepared by bone marrow-derived stromal cells.

Udagawa, N., Takahashi, N., Akatsu, T., Tanaka, H., Sasaki, T., Nishihara, T., Koga, T., Martin, T. J., & Suda, T. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.18.7260 · Cited by 1,048

TRANCE Is a Novel Ligand of the Tumor Necrosis Factor Receptor Family That Activates c-Jun N-terminal Kinase in T Cells

Wong, B. R., Rho, J., Arron, J. R., Robinson, E. A., Orlinick, J. R., Chao, M. V., Kalachikov, S. M., Cayani, E., Bartlett, F. S., Frankel, W. N., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.25190 · Cited by 1,042

Mechanics of membrane fusion

Chernomordik, L. V., & Kozlov, M. M. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1455 · Cited by 1,037

Total absence of colony-stimulating factor 1 in the macrophage-deficient osteopetrotic (op/op) mouse.

Wiktor-Jedrzejczak, W., Bartocci, A., Ferrante, A. W., Ahmed-Ansari, A., Sell, K. W., Pollard, J. W., & Stanley, E. R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.12.4828 · Cited by 1,031

IL-34 is a tissue-restricted ligand of CSF1R required for the development of Langerhans cells and microglia

Wang, Y., Szretter, K. J., Vermi, W., Gilfillan, S., Rossini, C., Cella, M., Barrow, A. D., Diamond, M. S., & Colonna, M. (2012) · Nature Immunology · doi:10.1038/ni.2360 · Cited by 1,011

Osteonal and hemi‐osteonal remodeling: The spatial and temporal framework for signal traffic in adult human bone

Parfitt, A. M. (1994) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240550303 · Cited by 1,001

Bone and haematopoietic defects in mice lacking c-fos

Wang, Z., Ovitt, C. E., Grigoriadis, A. E., Möhle-Steinlein, U., Rüther, U., & Wagner, E. F. (1992) · Nature · doi:10.1038/360741a0 · Cited by 932

DC-STAMP is essential for cell–cell fusion in osteoclasts and foreign body giant cells

Yagi, M., Miyamoto, T., Sawatani, Y., Iwamoto, K., Hosogane, N., Fujita, N., Morita, K., Ninomiya, K., Suzuki, T., Miyamoto, K., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050645 · Cited by 890

Discovery of a Cytokine and Its Receptor by Functional Screening of the Extracellular Proteome

Lin, H., Lee, E., Hestir, K., Leo, C., Huang, M., Bosch, E., Halenbeck, R., Wu, G., Zhou, A. J., Behrens, D., et al. (2008) · Science · doi:10.1126/science.1154370 · Cited by 849

Autoamplification of NFATc1 expression determines its essential role in bone homeostasis

Asagiri, M., Sato, K., Usami, T., Ochi, S., Nishina, H., Yoshida, H., Morita, I., Wagner, E. F., Mak, T. W., Serfling, E., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20051150 · Cited by 849

The Interaction Between Signal Regulatory Protein Alpha (SIRPα) and CD47: Structure, Function, and Therapeutic Target

Barclay, A. N., & van den Berg, T. K. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032713-120142 · Cited by 841

CSF-1 receptor signaling in myeloid cells.

Stanley, E. R., & Chitu, V. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021857 · Cited by 825

CSF-1 regulation of the wandering macrophage: complexity in action

Pixley, F. J., & Stanley, E. R. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.09.016 · Cited by 807

Isolation of a novel cytokine from human fibroblasts that specifically inhibits osteoclastogenesis.

Tsuda, E., Goto, M., Mochizuki, S.-I., Yano, K., Kobayashi, F., Morinaga, T., & Higashio, K. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6603 · Cited by 787

Bidirectional ephrinB2-EphB4 signaling controls bone homeostasis

Zhao, C., Irie, N., Takada, Y., Shimoda, K., Miyamoto, T., Nishiwaki, T., Suda, T., & Matsuo, K. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.012 · Cited by 777

Severe osteoporosis in mice lacking osteoclastogenesis inhibitory factor/osteoprotegerin.

Mizuno, A., Amizuka, N., Irie, K., Murakami, A., Fujise, N., Kanno, T., Sato, Y., Nakagawa, N., Yasuda, H., Mochizuki, S.-I., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8697 · Cited by 775

RANK Is the Essential Signaling Receptor for Osteoclast Differentiation Factor in Osteoclastogenesis

Nakagawa, N., Kinosaki, M., Yamaguchi, K., Shima, N., Yasuda, H., Yano, K., Morinaga, T., & Higashio, K. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9788 · Cited by 746

Mechanisms of membrane fusion: disparate players and common principles

Martens, S., & McMahon, H. T. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2417 · Cited by 733

Osteoclasts: What Do They Do and How Do They Do It?

Teitelbaum, S. L. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.060834 · Cited by 730

An Envelope Glycoprotein of the Human Endogenous Retrovirus HERV-W Is Expressed in the Human Placenta and Fuses Cells Expressing the Type D Mammalian Retrovirus Receptor

Blond, J.-L., Lavillette, D., Cheynet, V., Bouton, O., Oriol, G., Chapel‐Fernandes, S., Mandrand, B., Mallet, F., & Cosset, F. (2000) · Journal of Virology · doi:10.1128/jvi.74.7.3321-3329.2000 · Cited by 714

Commitment and differentiation of osteoclast precursor cells by the sequential expression of c-Fms and receptor activator of nuclear factor κB (RANK) receptors.

Arai, F., Miyamoto, T., Ohneda, O., Inada, T., Sudo, T., Brasel, K., Miyata, T., Anderson, D. M., & Suda, T. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.12.1741 · Cited by 693

The ligand for osteoprotegerin (OPGL) directly activates mature osteoclasts.

Burgess, T. L., Qian, Y.-X., Kaufman, S., Ring, B. D., Van, G., Capparelli, C., Kelley, M., Hsu, H., Boyle, W. J., Dunstan, C. R., et al. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.3.527 · Cited by 689

Pleiotropic effects of a null mutation in the c-fos proto-oncogene

Johnson, R. S., Spiegelman, B. M., & Papaioannou, V. E. (1992) · Cell · doi:10.1016/0092-8674(92)90592-z · Cited by 636

Stroma-derived interleukin-34 controls the development and maintenance of Langerhans cells and the maintenance of microglia

Greter, M., Lelios, I., Pelczar, P., Hoeffel, G., Price, J., Leboeuf, M., Kündig, T. M., Frei, K., Ginhoux, F., Merad, M., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.11.001 · Cited by 630

Osteoprotection by semaphorin 3A

Hayashi, M., Nakashima, T., Taniguchi, M., Kodama, T., Kumanogoh, A., & Takayanagi, H. (2012) · Nature · doi:10.1038/nature11000 · Cited by 606

Identification and Characterization of the New Osteoclast Progenitor with Macrophage Phenotypes Being Able to Differentiate into Mature Osteoclasts

Takeshita, S., Kaji, K., & Kudō, A. (2000) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2000.15.8.1477 · Cited by 602

Osteopetrosis: genetics, treatment and new insights into osteoclast function

Sobacchi, C., Schulz, A., Coxon, F. P., Villa, A., & Helfrich, M. H. (2013) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2013.137 · Cited by 580

Osteoclasts: New Insights

Feng, X., & Teitelbaum, S. L. (2013) · Bone Research · doi:10.4248/br201301003 · Cited by 562

Genomewide screening for fusogenic human endogenous retrovirus envelopes identifies syncytin 2, a gene conserved on primate evolution

Blaise, S., de Parseval, N., Benit, L., & Heidmann, T. (2003) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2132646100 · Cited by 557

Regulation of bone formation by osteoclasts involves Wnt/BMP signaling and the chemokine sphingosine-1-phosphate

Pederson, L., Ruan, M., Westendorf, J. J., Khosla, S., & Oursler, M. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805133106 · Cited by 556

v-ATPase V0 subunit d2–deficient mice exhibit impaired osteoclast fusion and increased bone formation

Lee, S.-H., Rho, J., Jeong, D., Sul, J., Kim, T. S., Kim, N., Kang, J.-S., Miyamoto, T. K., Suda, T., Lee, S., et al. (2006) · Nature Medicine · doi:10.1038/nm1514 · Cited by 547

The Osteocyte: New Insights

Robling, A. G., & Bonewald, L. F. (2020) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021119-034332 · Cited by 539

Protein Expression and Functional Difference of Membrane-Bound and Soluble Receptor Activator of NF-κB Ligand: Modulation of the Expression by Osteotropic Factors and Cytokines

Nakashima, T., Kobayashi, Y., Yamasaki, S., Kawakami, A., Eguchi, K., Sasaki, H., & Sakai, H. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3379 · Cited by 508

Suppression of bone formation by osteoclastic expression of semaphorin 4D

Negishi-Koga, T., Shinohara, M., Komatsu, N., Bito, H., Kodama, T., Friedel, R. H., & Takayanagi, H. (2011) · Nature Medicine · doi:10.1038/nm.2489 · Cited by 498

Developmental origin, functional maintenance and genetic rescue of osteoclasts

Jacome-Galarza, C. E., Percin, G. I., Muller, J. T., Mass, E., Lazarov, T., Eitler, J., Rauner, M., Yadav, V. K., Crozet, L., Bohm, M., et al. (2019) · Nature · doi:10.1038/s41586-019-1105-7 · Cited by 475

NFATc1 Induces Osteoclast Fusion Via Up-Regulation of Atp6v0d2 and the Dendritic Cell-Specific Transmembrane Protein (DC-STAMP)

Kim, K., Lee, S., Kim, J. H., Choi, Y., & Kim, N. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0237 · Cited by 448

A Novel Membrane Glycoprotein, SHPS-1, That Binds the SH2-Domain-Containing Protein Tyrosine Phosphatase SHP-2 in Response to Mitogens and Cell Adhesion

Fujioka, Y., Matozaki, T., Noguchi, T., Iwamatsu, A., Yamao, T., Takahashi, N., Tsuda, M., Takada, T., & Kasuga, M. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.12.6887 · Cited by 447

Osteoclasts recycle via osteomorphs during RANKL-stimulated bone resorption

McDonald, M. M., Khoo, W. H., Ng, P. Y., Xiao, Y., Zamerli, J., Thatcher, P., Kyaw, W., Pathmanandavel, K., Grootveld, A. K., Moran, I., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.002 · Cited by 433

Removal of Osteoclast Bone Resorption Products by Transcytosis

Salo, J., Lehenkari, P. P., Mulari, M. T. K., Metsikkö, K., & Väänänen, H. K. (1997) · Science · doi:10.1126/science.276.5310.270 · Cited by 427

A combination of osteoclast differentiation factor and macrophage-colony stimulating factor is sufficient for both human and mouse osteoclast formation in vitro.

Quinn, J. M. W., Elliott, J., Gillespie, M. T., & Martin, T. J. (1998) · Endocrinology · doi:10.1210/endo.139.10.6331 · Cited by 407

MMP-7 promotes prostate cancer-induced osteolysis via the solubilization of RANKL

Lynch, C. C., Hikosaka, A., Acuff, H. B., Martin, M. D., Kawai, N., Singh, R. K., Vargo-Gogola, T. C., Begtrup, J. L., Peterson, T. E., Fingleton, B., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.04.013 · Cited by 402

The Osteoclast: Friend or Foe?

Novack, D. V., & Teitelbaum, S. L. (2007) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.3.121806.151431 · Cited by 402

Syncytin-A and syncytin-B, two fusogenic placenta-specific murine envelope genes of retroviral origin conserved in Muridae

Dupressoír, A., Marceau, G., Vernochet, C., Bénit, L., Kanellopoulos‐Langevin, C., Sapin, V., & Heidmann, T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406509102 · Cited by 384

Trafficking of Matrix Collagens Through Bone-Resorbing Osteoclasts

Nesbitt, S. A., & Horton, M. A. (1997) · Science · doi:10.1126/science.276.5310.266 · Cited by 378

Membrane Hemifusion: Crossing a Chasm in Two Leaps

Chernomordik, L. V., & Kozlov, M. M. (2005) · Cell · doi:10.1016/j.cell.2005.10.015 · Cited by 376

Functional overlap but differential expression of CSF-1 and IL-34 in their CSF-1 receptor-mediated regulation of myeloid cells

Wei, S., Nandi, S., Chitu, V., Yeung, Y.-G., Yu, W., Huang, M., Williams, L. T., Lin, H., & Stanley, E. R. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.1209822 · Cited by 370

RANKL-induced DC-STAMP Is Essential for Osteoclastogenesis

Kukita, T., Wada, N., Kukita, A., Kakimoto, T., Sandra, F., Toh, K., Nagata, K., Iijima, T., Horiuchi, M., Matsusaki, H., et al. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20040518 · Cited by 357

NFATc1 in mice represses osteoprotegerin during osteoclastogenesis and dissociates systemic osteopenia from inflammation in cherubism

Aliprantis, A. O., Ueki, Y., Sulyanto, R. M., Park, A., Sigrist, K. S., Sharma, S. M., Ostrowski, M. C., Olsen, B. R., & Glimcher, L. H. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35711 · Cited by 350

Osteoclast Differentiation Factor (ODF) Induces Osteoclast-like Cell Formation in Human Peripheral Blood Mononuclear Cell Cultures

Matsuzaki, K., Udagawa, N., Takahashi, N., Yamaguchi, K., Yasuda, H., Shima, N., Morinaga, T., Toyama, Y., Yabe, Y., Higashio, K., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8586 · Cited by 337

Sphingosine 1‐phosphate as a regulator of osteoclast differentiation and osteoclast–osteoblast coupling

Ryu, J., Kim, H. J., Chang, E., Huang, H., Banno, Y., & Hong‐Hee, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601430 · Cited by 332

Molecular mediators of macrophage fusion

Helming, L., & Gordon, S. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.07.005 · Cited by 326

Immature dendritic cell transdifferentiation into osteoclasts: a novel pathway sustained by the rheumatoid arthritis microenvironment

Rivollier, A., Mazzorana, M., Tebib, J. G., Piperno, M., Aitsiselmi, T., Rabourdin‐Combe, C., Jurdic, P., & Delprat, C. (2004) · Blood · doi:10.1182/blood-2004-01-0041 · Cited by 323

αvβ3and macrophage colony‐stimulating factor: partners in osteoclast biology

Ross, F. P., & Teitelbaum, S. L. (2005) · Immunological Reviews · doi:10.1111/j.0105-2896.2005.00331.x · Cited by 312

Interleukin-4 induces foreign body giant cells from human monocytes/macrophages. Differential lymphokine regulation of macrophage fusion leads to morphological variants of multinucleated giant cells.

(1995) · Europe PMC (PubMed Central) · Cited by 294

Discovery of the RANKL/RANK/OPG system

Yasuda, H. (2021) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-020-01175-1 · Cited by 251

Apoptosis and osteoporosis

Weinstein, R. S., & Manolagas, S. C. (2000) · The American Journal of Medicine · doi:10.1016/s0002-9343(99)00420-9 · Cited by 250

High Expression of Inhibitory Receptor SHPS-1 and Its Association with Protein-tyrosine Phosphatase SHP-1 in Macrophages

Veillette, A., Thibaudeau, E., & Latour, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22719 · Cited by 247

The hematopoietic stem cell niche: from embryo to adult

Gao, X., Xu, C., Asada, N., & Frenette, P. S. (2018) · Development · doi:10.1242/dev.139691 · Cited by 247

CD47, a ligand for the macrophage fusion receptor, participates in macrophage multinucleation

Han, X., Sterling, H., Chen, Y., Saginario, C., Brown, E. J., Frazier, W. A., Lindberg, F. P., & Vignery, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002334200 · Cited by 245

Bone Modeling and Remodeling

Seeman, E. (2009) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v19.i3.40 · Cited by 242

Negative regulation of osteoclastogenesis by ectodomain shedding of receptor activator of NF-κB ligand.

Hikita, A., Yana, I., Wakeyama, H., Nakamura, M., Kadono, Y., Oshima, Y., Nakamura, K., Seiki, M., & Tanaka, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606656200 · Cited by 236

Macrophage fusion

Vignery, A. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20051123 · Cited by 232

Protein-driven membrane stresses in fusion and fission

Kozlov, M. M., McMahon, H. T., & Chernomordik, L. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.06.003 · Cited by 231

Osteoclasts Have Multiple Roles in Bone in Addition to Bone Resorption

Boyce, B. F., Yao, Z., & Xing, L. (2009) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v19.i3.10 · Cited by 214

RANKL/OPG; Critical role in bone physiology

Martin, T. J., & Sims, N. A. (2015) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-014-9308-6 · Cited by 213

The Envelope Glycoprotein of Human Endogenous Retrovirus Type W Uses a Divergent Family of Amino Acid Transporters/Cell Surface Receptors

Lavillette, D., Marin, M., Ruggieri, A., Mallet, F., Cosset, F., & Kabat, D. (2002) · Journal of Virology · doi:10.1128/jvi.76.13.6442-6452.2002 · Cited by 209

Systemic tumor necrosis factor α mediates an increase in peripheral CD11bhigh osteoclast precursors in tumor necrosis factor α–transgenic mice

Li, P., Schwarz, E. M., O’Keefe, R. J., Ma, L., Looney, R. J., Ritchlin, C. T., Boyce, B. F., & Xing, L. (2004) · Arthritis & Rheumatism · doi:10.1002/art.11419 · Cited by 208

The hallmarks of cell-cell fusion

Hernández, J. M., & Podbilewicz, B. (2017) · Development · doi:10.1242/dev.155523 · Cited by 205

Tumor Necrosis Factor-α Increases Circulating Osteoclast Precursor Numbers by Promoting Their Proliferation and Differentiation in the Bone Marrow through Up-regulation of c-Fms Expression

Yao, Z., Li, P., Zhang, Q., Schwarz, E. M., Keng, P., Arbini, A., Boyce, B. F., & Xing, L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512624200 · Cited by 197

How cells fuse

Brukman, N. G., Uygur, B., Podbilewicz, B., & Chernomordik, L. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201901017 · Cited by 195

Cardiotrophin-1 Is an Osteoclast-Derived Stimulus of Bone Formation Required for Normal Bone Remodeling

Walker, E. C., McGregor, N. E., Poulton, I. J., Pompolo, S., Allan, E. H., Quinn, J. M., Gillespie, M. T., Martin, T. J., & Sims, N. A. (2008) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.080706 · Cited by 190

Membrane tension and membrane fusion

Kozlov, M. M., & Chernomordik, L. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.07.010 · Cited by 186

The osteoclast and its unique cytoskeleton

Teitelbaum, S. L. (2011) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2011.06283.x · Cited by 186

Erythromyeloid progenitors give rise to a population of osteoclasts that contribute to bone homeostasis and repair

Yahara, Y., Barrientos, T., Tang, Y. J., Puviindran, V., Nadesan, P., Zhang, H., Gibson, J., Gregory, S. G., Diao, Y., Xiang, Y., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-019-0437-8 · Cited by 185

Transcriptional Program of Mouse Osteoclast Differentiation Governed by the Macrophage Colony-stimulating Factor and the Ligand for the Receptor Activator of NFκB

Cappellen, D., Luong-Nguyen, N.-H., Bongiovanni, S., Grenet, O., Wanke, C., & Šuša, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200434200 · Cited by 184

Podosome organization drives osteoclast-mediated bone resorption

Georgess, D., Machuca‐Gayet, I., Blangy, A., & Jurdic, P. (2014) · Cell Adhesion & Migration · doi:10.4161/cam.27840 · Cited by 181

Molecular regulation of osteoclast activity

Bruzzaniti, A., & Baron, R. (2006) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-006-9009-x · Cited by 181

Osteoclast stimulatory transmembrane protein and dendritic cell–specific transmembrane protein cooperatively modulate cell–cell fusion to form osteoclasts and foreign body giant cells

Miyamoto, H., Suzuki, T., Miyauchi, Y., Iwasaki, R., Kobayashi, T., Sato, Y., Miyamoto, K., Hoshi, H., Hashimoto, K., Yoshida, S., et al. (2012) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.1575 · Cited by 177

The macrophage-specific V-ATPase subunit ATP6V0D2 restricts inflammasome activation and bacterial infection by facilitating autophagosome-lysosome fusion

Xia, Y., Liu, N., Xie, X., Bi, G., Ba, H., Li, L., Zhang, J., Deng, X., Yao, Y., Tang, Z., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1569916 · Cited by 177

Osteoclast Multinucleation: Review of Current Literature

Kodama, J., & Kaito, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165685 · Cited by 177

The RANKL-RANK Story

Nagy, V., & Penninger, J. M. (2015) · Gerontology · doi:10.1159/000371845 · Cited by 175

The CD47-SIRP signalling system: its physiological roles and therapeutic application

Murata, Y., Kotani, T., Ohnishi, H., & Matozaki, T. (2014) · The Journal of Biochemistry · doi:10.1093/jb/mvu017 · Cited by 171

Identification of cell cycle–arrested quiescent osteoclast precursors in vivo

Mizoguchi, T., Muto, A., Udagawa, N., Arai, A., Yamashita, T., Hosoya, A., Ninomiya, T., Nakamura, H., Yamamoto, Y., Kinugawa, S., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200806139 · Cited by 166

The Osteoclast in Bone Metastasis: Player and Target

Maurizi, A., & Rucci, N. (2018) · Cancers · doi:10.3390/cancers10070218 · Cited by 165

Regulation of Embryonic and Postnatal Development by the CSF-1 Receptor

Chiţu, V., & Stanley, E. R. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.10.004 · Cited by 163

The Critical Role of IL-34 in Osteoclastogenesis

Chen, Z. J., Büki, K. G., Vääräniemi, J., Gu, G., & Väänänen, H. K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018689 · Cited by 158

Re-thinking the bone remodeling cycle mechanism and the origin of bone loss

Delaisse, J.-M., Andersen, T. L., Kristensen, H. B., Jensen, P. R., Andreasen, C. M., & Søe, K. (2020) · Bone · doi:10.1016/j.bone.2020.115628 · Cited by 152

MFR, a Putative Receptor Mediating the Fusion of Macrophages

Saginario, C., Sterling, H., Beckers, C. J. M., Kobayashi, R., Solimena, M., Ullu, E., & Vignery, A. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.11.6213 · Cited by 151

Atp6v0d2 Is an Essential Component of the Osteoclast-Specific Proton Pump That Mediates Extracellular Acidification in Bone Resorption

Wu, H., Xu, G., & Li, Y. (2008) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.081239 · Cited by 145

Soluble RANKL contributes to osteoclast formation in adult mice but not ovariectomy-induced bone loss

Xiong, J., Cawley, K., Piemontese, M., Fujiwara, Y., Zhao, H., Goellner, J. J., & O’Brien, C. A. (2018) · Nature Communications · doi:10.1038/s41467-018-05244-y · Cited by 144

Stepwise cell fate decision pathways during osteoclastogenesis at single-cell resolution

Tsukasaki, M., Huynh, N. C., Okamoto, K., Muro, R., Terashima, A., Kurikawa, Y., Komatsu, N., Pluemsakunthai, W., Nitta, T., Abe, T., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-00318-y · Cited by 142

Osteoclast Ruffled Border Has Distinct Subdomains for Secretion and Degraded Matrix Uptake

Mulari, M. T. K., Zhao, H., Lakkakorpi, P. T., & Väänänen, H. K. (2003) · Traffic · doi:10.1034/j.1600-0854.2003.40206.x · Cited by 140

Osteoclast stimulatory transmembrane protein (OC‐STAMP), a novel protein induced by RANKL that promotes osteoclast differentiation

Yang, M., Birnbaum, M. J., MacKay, C. A., Mason‐Savas, A., Thompson, B., & Odgren, P. R. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21331 · Cited by 140

Involvement of human endogenous retroviral syncytin-1 in human osteoclast fusion

Søe, K., Andersen, T. L., Hobolt-Pedersen, A.-S., Bjerregaard, B., Larsson, L., & Delaissé, J. (2010) · Bone · doi:10.1016/j.bone.2010.11.011 · Cited by 138

The relationship between the number of nuclei of an osteoclast and its resorptive capability in vitro

Piper, K., BOYDE, A., & Jones, S. (1992) · Anatomy and Embryology · doi:10.1007/bf00185977 · Cited by 137

Genetics of Osteopetrosis

Palagano, E., Menale, C., Sobacchi, C., & VILLA, A. M. (2018) · Current Osteoporosis Reports · doi:10.1007/s11914-018-0415-2 · Cited by 134

Formation and function of the ruffled border in osteoclasts

Stenbeck, G. (2002) · Seminars in Cell and Developmental Biology · doi:10.1016/s1084952102000587 · Cited by 133

An Overview of the Derivation and Function of Multinucleated Giant Cells and Their Role in Pathologic Processes

Brooks, P. J., Glogauer, M., & McCulloch, C. A. (2019) · American Journal Of Pathology · doi:10.1016/j.ajpath.2019.02.006 · Cited by 129

Management of Osteogenesis Imperfecta

Ralston, S. H., & Gaston, M. S. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00924 · Cited by 124

Cell fusion during development

Oren‐Suissa, M., & Podbilewicz, B. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.09.004 · Cited by 123

Discovery of CLC transport proteins: cloning, structure, function and pathophysiology

Jentsch, T. J. (2015) · The Journal of Physiology · doi:10.1113/jp270043 · Cited by 117

New Insights Into Osteoclast Biology

McDonald, M. M., Kim, A. S., Mulholland, B. S., & Rauner, M. (2021) · JBMR Plus · doi:10.1002/jbm4.10539 · Cited by 116

A novel human endogenous retroviral protein inhibits cell-cell fusion

Sugimoto, J., Sugimoto, M., Bernstein, H. B., Jinno, Y., & Schust, D. J. (2013) · Scientific Reports · doi:10.1038/srep01462 · Cited by 115

DC-STAMP: A Key Regulator in Osteoclast Differentiation

Chiu, Y. G., & Ritchlin, C. T. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25389 · Cited by 115

Vacuolar ATPase as a potential therapeutic target and mediator of treatment resistance in cancer

Whitton, B., Okamoto, H., Packham, G., & Crabb, S. J. (2018) · Cancer Medicine · doi:10.1002/cam4.1594 · Cited by 113

The origins and roles of osteoclasts in bone development, homeostasis and repair

Yahara, Y., Nguyen, T., Ishikawa, K., Kamei, K., & Alman, B. A. (2022) · Development · doi:10.1242/dev.199908 · Cited by 111

Meltrin-α, a Fusion Protein Involved in Multinucleated Giant Cell and Osteoclast Formation

Abe, E., Mocharla, H., Yamate, T., Taguchi, Y., & Manolagas, S. C. (1999) · Calcified Tissue International · doi:10.1007/s002239900641 · Cited by 110

The tyrosine phosphatase SHP-1 is a negative regulator of osteoclastogenesis and osteoclast resorbing activity: increased resorption and osteopenia in me/me mutant mice

Aoki, K., DiDomenico, E., Sims, N. A., Mukhopadhyay, K., Neff, L., Houghton, A., Amling, M., Levy, J. B., Horne, W. C., & Baron, R. (1999) · Bone · doi:10.1016/s8756-3282(99)00174-x · Cited by 109

Lineage-committed osteoclast precursors circulate in blood and settle down into bone

Muto, A., Mizoguchi, T., Udagawa, N., Ito, S., Kawahara, I., Abiko, Y., Arai, A., Harada, S., Kobayashi, Y., Nakamichi, Y., et al. (2011) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.490 · Cited by 109

Chemical and Biochemical Basis of Cell-Bone Matrix Interaction in Health and Disease

Xu, F. (2009) · Current Chemical Biology · doi:10.2174/2212796810903020189 · Cited by 109

Colony-stimulating Factor-1 Stimulates the Formation of Multimeric Cytosolic Complexes of Signaling Proteins and Cytoskeletal Components in Macrophages

Yeung, Y.-G., Wang, Y., Einstein, D. B., Lee, P. S. W., & Stanley, E. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.27.17128 · Cited by 108

ADAM8: A Novel Osteoclast Stimulating Factor

Choi, S. J., Han, J.-H., & Roodman, G. D. (2001) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2001.16.5.814 · Cited by 108

Cell-surface phosphatidylserine regulates osteoclast precursor fusion

Verma, S. K., Leikina, E., Melikov, K., Gebert, C. M., Kram, V., Young, M. F., Uygur, B., & Chernomordik, L. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.809681 · Cited by 104

Regulation of human osteoclast development by dendritic cell-specific transmembrane protein (DC-STAMP)

Chiu, Y. G., Mensah, K. A., Schwarz, E. M., Ju, Y., Takahata, M., Feng, C., McMahon, L. A., Hicks, D. G., Panepento, B., Keng, P. C., et al. (2011) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.531 · Cited by 101

Flagging fusion: Phosphatidylserine signaling in cell–cell fusion

Whitlock, J. M., & Chernomordik, L. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100411 · Cited by 101

Growth Hormone Regulation of SIRP and SHP-2 Tyrosyl Phosphorylation and Association

Stofega, M. R., Wang, H., Ullrich, A., & Carter‐Su, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.7112 · Cited by 100

Extracellular annexins and dynamin are important for sequential steps in myoblast fusion

Leikina, E., Melikov, K., Sanyal, S., et al. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201207012 · Cited by 100

RANKL induces heterogeneous DC‐STAMP lo and DC‐STAMP hi osteoclast precursors of which the DC‐STAMP lo precursors are the master fusogens

Mensah, K. A., Ritchlin, C. T., & Schwarz, E. M. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.22012 · Cited by 100

Dendritic Cells at the Osteo‐Immune Interface: Implications for Inflammation‐Induced Bone Loss

Alnaeeli, M., Park, J.-A., Mahamed, D., Penninger, J. M., & Teng, Y. (2007) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.070314 · Cited by 97

Osteoclast Fusion and Fission

Jansen, I. D. C., Vermeer, J. A. F., Bloemen, V., Stap, J., & Everts, V. E. (2012) · Calcified Tissue International · doi:10.1007/s00223-012-9600-y · Cited by 94

Syncytins expressed in human placental trophoblast

Roberts, R. M., Ezashi, T., Schulz, L. C., Sugimoto, J., Schust, D. J., Khan, T., & Zhou, J. (2021) · Placenta · doi:10.1016/j.placenta.2021.01.006 · Cited by 91

Administration of colony stimulating factor-1 corrects some macrophage, dental, and skeletal defects in an osteopetrotic mutation (toothless, tl) in the rat

Marks, S. C., Wójtowicz, A., Szperl, M., Urbanowska, E., MacKay, C. A., Wiktor-Jędrzejczak, W., Stanley, E. R., & Aukerman, S. L. (1992) · Bone · doi:10.1016/8756-3282(92)90365-4 · Cited by 90

Osteoclast formation is strongly reduced both in vivo and in vitro in the absence of CD47/SIRPα-interaction

Lundberg, P., Koskinen, C., Baldock, P. A. J., Löthgren, H., Stenberg, Å., Lerner, U. H., & Oldenborg, P. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.11.057 · Cited by 90

Macrophage Colony Stimulating Factor Increases Bone Resorption in Dispersed Osteoclast Cultures by Increasing Osteoclast Size

Lees, R. L., & Heersche, J. N. M. (1999) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.1999.14.6.937 · Cited by 90

CD47 Regulates Bone Mass and Tumor Metastasis to Bone

Uluçkan, Ö., Becker, S. N., Deng, H., Zou, W., Prior, J. L., Piwnica-Worms, D. R., Frazier, W. A., & Weilbaecher, K. N. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3358 · Cited by 87

Dynamin and endocytosis are required for the fusion of osteoclasts and myoblasts

Shin, N.-Y., Choi, H., Neff, L., Wu, Y., Saito, H., Ferguson, S. M., Camilli, P. V. D., & Baron, R. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201401137 · Cited by 83

V-ATPases and osteoclasts: ambiguous future of V-ATPases inhibitors in osteoporosis

Duan, X., Yang, S., Zhang, L., & Yang, T. (2018) · Theranostics · doi:10.7150/thno.28391 · Cited by 83

Feel the force: Podosomes in mechanosensing

Linder, S., & Wiesner, C. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.11.026 · Cited by 82

Studies of OC-STAMP in Osteoclast Fusion: A New Knockout Mouse Model, Rescue of Cell Fusion, and Transmembrane Topology

Witwicka, H., Hwang, S., Reyes‐Gutierrez, P., Jia, H., Odgren, P. E., Donahue, L. R., Birnbaum, M. J., & Odgren, P. R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0128275 · Cited by 81

Transcriptional Activity of Nuclei in Multinucleated Osteoclasts and Its Modulation by Calcitonin

Boissy, P., Saltel, F., Baly, C., Jurdic, P., & Machuca‐Gayet, I. (2002) · Endocrinology · doi:10.1210/endo.143.5.8813 · Cited by 81

Monocytes from circulating blood fuse in vitro with purified osteoclasts in primary culture

Zallone, A. Z., Teti, A. M., & Primavera, M. V. (1984) · Journal of Cell Science · doi:10.1242/jcs.66.1.335 · Cited by 79

Phosphatidylethanolamine dynamics are required for osteoclast fusion

Irie, A., Yamamoto, K., Miki, Y., & Murakami, M. (2017) · Scientific Reports · doi:10.1038/srep46715 · Cited by 78

One Disease, Many Genes: Implications for the Treatment of Osteopetroses

Penna, S., Capo, V., Palagano, E., Sobacchi, C., & VILLA, A. M. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00085 · Cited by 78

CCN family 2/connective tissue growth factor (CCN2/CTGF) promotes osteoclastogenesis via induction of and interaction with dendritic cell–specific transmembrane protein (DC-STAMP)

Nishida, T., Emura, K., Kubota, S., Lyons, K. M., & Takigawa, M. (2010) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.222 · Cited by 77

Dominant role of CD47–thrombospondin-1 interactions in myeloma-induced fusion of human dendritic cells: implications for bone disease

Kukreja, A., Radfar, S., Sun, B., Insogna, K. L., & Dhodapkar, M. V. (2009) · Blood · doi:10.1182/blood-2009-03-211920 · Cited by 76

Membrane trafficking in osteoclasts and implications for osteoporosis

Ng, P. Y., Ribet, A., & Pavlos, N. J. (2019) · Biochemical Society Transactions · doi:10.1042/bst20180445 · Cited by 75

TGF-β induces the expression of the FLICE-inhibitory protein and inhibits Fas-mediated apoptosis of microglia

Schlapbach, R., Spanaus, K., Malipiero, U., Lens, S. M. A., Tasinato, A., Tschopp, J., & Fontana, A. (2000) · European Journal of Immunology · doi:10.1002/1521-4141(200012)30:12 · Cited by 74

Osteoclast Fusion: Time‐Lapse Reveals Involvement of CD47 and Syncytin‐1 at Different Stages of Nuclearity

Møller, A. M. J., Delaissé, J., & Søe, K. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25633 · Cited by 74

RANKL and RANK in sex hormone-induced breast cancer and breast cancer metastasis

Schramek, D., Sigl, V., & Penninger, J. M. (2011) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2011.02.007 · Cited by 73

Role of OSCAR Signaling in Osteoclastogenesis and Bone Disease

Nedeva, I. R., Vitale, M., Elson, A., Hoyland, J. A., & Bella, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.641162 · Cited by 72

Osteoclast fusion is initiated by a small subset of RANKL-stimulated monocyte progenitors, which can fuse to RANKL-unstimulated progenitors

Levaot, N., Ottolenghi, A., Mann, M., Ram, G. G., Kam, Z., & Geiger, B. (2015) · Bone · doi:10.1016/j.bone.2015.05.021 · Cited by 68

Two novel genes FIND and LIND differentially expressed in deactivated and Listeria -infected human macrophages

Staege, H., Brauchlin, A. E., Schoedon, G., & Schaffner, A. (2001) · Immunogenetics · doi:10.1007/s002510100306 · Cited by 68

Oxysterols and EBI2 promote osteoclast precursor migration to bone surfaces and regulate bone mass homeostasis

Nevius, E., Pinho, F. O., Dhodapkar, M. M., Jin, H., Nadrah, K., Horowitz, M. C., Kikuta, J., Ishii, M., & Pereira, J. P. (2015) · The Journal of Experimental Medicine · doi:10.1084/jem.20150088 · Cited by 68

Thrombospondin-1 Regulates Bone Homeostasis Through Effects on Bone Matrix Integrity and Nitric Oxide Signaling in Osteoclasts

Amend, S. R., Uluçkan, Ö., Hurchla, M. A., Leib, D. J., Novack, D. V., Silva, M. J., Frazier, W. A., & Weilbaecher, K. N. (2014) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2308 · Cited by 65

The RANKL-RANK Axis: A Bone to Thymus Round Trip

Sobacchi, C., Menale, C., & VILLA, A. M. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00629 · Cited by 65

Osteoclast Fusion: Physiological Regulation of Multinucleation through Heterogeneity—Potential Implications for Drug Sensitivity

Søe, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207717 · Cited by 62

Osteoclast Fusion is Based on Heterogeneity Between Fusion Partners

Hobolt-Pedersen, A.-S., Delaissé, J., & Søe, K. (2014) · Calcified Tissue International · doi:10.1007/s00223-014-9864-5 · Cited by 61

Macrophage Fusion

Vignery, A. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-250-2_9 · Cited by 59

Circulating monocytes: an appropriate model for bone-related study

Zhou, Y. G., Deng, H., & Shen, H. (2015) · Osteoporosis International · doi:10.1007/s00198-015-3250-7 · Cited by 58

Cell fusion in osteoclasts plays a critical role in controlling bone mass and osteoblastic activity

Iwasaki, R., Ninomiya, K., Miyamoto, K., Suzuki, T., Sato, Y., Kawana, H., Nakagawa, T., Suda, T., & Miyamoto, T. K. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.076 · Cited by 57

The elementary fusion modalities of osteoclasts

Søe, K., Hobolt-Pedersen, A.-S., & Delaissé, J. (2014) · Bone · doi:10.1016/j.bone.2014.12.010 · Cited by 57

Effects of surface microtopography on the assembly of the osteoclast resorption apparatus

Geblinger, D., Zink, C., Spencer, N. D., Addadi, L., & Geiger, B. (2011) · Journal of The Royal Society Interface · doi:10.1098/rsif.2011.0659 · Cited by 57

Identification of an inducible surface molecule specific to fusing macrophages.

Saginario, C., Qian, H. Y., & Vignery, A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.26.12210 · Cited by 55

The fusogenic synapse at a glance

Kim, J. H., & Chen, E. H. (2019) · Journal of Cell Science · doi:10.1242/jcs.213124 · Cited by 55

Dendritic-cell-derived osteoclasts: a new game changer in bone-resorption-associated diseases

Lapérine, O., Blin‐Wakkach, C., Guicheux, J., Beck-Cormier, S., & Lesclous, P. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.04.022 · Cited by 54

A CSF-1 Receptor Phosphotyrosine 559 Signaling Pathway Regulates Receptor Ubiquitination and Tyrosine Phosphorylation

Xiong, Y., Song, D., Cai, Y., Yu, W., Yeung, Y.-G., & Stanley, E. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.166702 · Cited by 53

Positive and negative regulators of osteoclast apoptosis

Soysa, N. S., & Alles, N. (2019) · Bone Reports · doi:10.1016/j.bonr.2019.100225 · Cited by 53

Negative Feedback Control of Osteoclast Formation through Ubiquitin-mediated Down-regulation of NFATc1

Kim, J. H., Kim, K., Jin, H. M., Song, I., Youn, B. U., Lee, S., Choi, Y., & Kim, N. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.042812 · Cited by 52

Immature dendritic cells in multiple myeloma are prone to osteoclast‐like differentiation through interleukin‐17 A stimulation

Tucci, M., Stucci, L. S., Savonarola, A., Ciavarella, S., Cafforio, P., Dammacco, F., & Silvestris, F. (2013) · British Journal of Haematology · doi:10.1111/bjh.12333 · Cited by 50

Absence of Dap12 and the αvβ3 integrin causes severe osteopetrosis

Zou, W., & Teitelbaum, S. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201410123 · Cited by 50

Late stages of the synchronized macrophage fusion in osteoclast formation depend on dynamin

Verma, S. K., Leikina, E., Melikov, K., & Chernomordik, L. (2014) · Biochemical Journal · doi:10.1042/bj20141233 · Cited by 50

Formation of osteoclasts from blood monocytes during 1 alpha-OH Vit D-stimulated bone resorption in mice.

Tinkler, S. M., Linder, J. E., Williams, D. M., & Johnson, N. W. (1981) · Europe PMC (PubMed Central) · Cited by 48

OC‐STAMP promotes osteoclast fusion for pathogenic bone resorption in periodontitis via up‐regulation of permissive fusogen CD9

Ishii, T., Ruiz‐Torruella, M., Ikeda, A., Shindo, S., Movilă, A., Mawardi, H. H., Albassam, A., Kayal, R. A., Al-Dharrab, A. A., Egashira, K., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201701424r · Cited by 47

Characterization of the Bone Phenotype in ClC-7-Deficient Mice

Neutzsky-Wulff, A. V., Karsdal, M. A., & Henriksen, K. (2008) · Calcified Tissue International · doi:10.1007/s00223-008-9185-7 · Cited by 46

The contribution of cross-talk between the cell-surface proteins CD36 and CD47–TSP-1 in osteoclast formation and function

Koduru, S. V., Sun, B.-H., Walker, J. M., Zhu, M., Simpson, C. A., Dhodapkar, M. V., & Insogna, K. L. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000633 · Cited by 46

An essential role for the association of CD47 to SHPS-1 in skeletal remodeling

Maile, L. A., DeMambro, V., Wai, C., Aday, A. W., Capps, B. E., Beamer, W. G., Rosen, C. J., & Clemmons, D. R. (2011) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.441 · Cited by 45

Sexual Dimorphism in Differentiating Osteoclast Precursors Demonstrates Enhanced Inflammatory Pathway Activation in Female Cells

Mun, S. H., Jastrzebski, S. L., Kalinowski, J., Zeng, S. L., Oh, B., Bae, S., Eugenia, G., Khan, N. M., Drissi, H., Zhou, P., et al. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.4270 · Cited by 45

Fusogens

Segev, N., Avinoam, O., & Podbilewicz, B. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.024 · Cited by 45

Novel techniques in the development of osteoporosis drug therapy: the osteoclast ruffled-border vacuolar H+-ATPase as an emerging target

Kartner, N., & Manolson, M. F. (2014) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2014.902155 · Cited by 43

RAB-5- and DYNAMIN-1-Mediated Endocytosis of EFF-1 Fusogen Controls Cell-Cell Fusion

Smurova, K., & Podbilewicz, B. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.01.027 · Cited by 43

State of the Art in Cell–Cell Fusion

Willkomm, L., & Bloch, W. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2703-6_1 · Cited by 43

Pin1 Regulates Osteoclast Fusion Through Suppression of the Master Regulator of Cell Fusion DC‐STAMP

Islam, R., Bae, H., Yoon, W., Woo, K. M., Baek, J., Kim, H., Uchida, T., & Ryoo, H. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24679 · Cited by 42

The lifespan of osteoclasts: Experimental studies using the giant granule cytoplasmic marker characteristic of beige mice

Marks, S. C., & Seifert, M. F. (1985) · Bone · doi:10.1016/8756-3282(85)90223-6 · Cited by 38

Quantitative relationship between osteoclasts, osteoclast nuclei and the extent of the resorbing surface in hamster periodontal disease

Makris, G., & Jl, S. (1982) · Archives of Oral Biology · doi:10.1016/0003-9969(82)90104-2 · Cited by 37

The Gene of Retroviral Origin Syncytin 1 is Specific to Hominoids and is Inactive in Old World Monkeys

Cáceres, M., & Thomas, J. W. (2006) · Journal of Heredity · doi:10.1093/jhered/esj011 · Cited by 37

Evolution of programmed cell fusion: Common mechanisms and distinct functions

Oren‐Suissa, M., & Podbilewicz, B. (2010) · Developmental Dynamics · doi:10.1002/dvdy.22284 · Cited by 35

Lack of CD47 Impairs Bone Cell Differentiation and Results in an Osteopenic Phenotype in Vivo due to Impaired Signal Regulatory Protein α (SIRPα) Signaling

Koskinen, C., Persson, E., Baldock, P. A. J., Stenberg, Å., Boström, I. M., Matozaki, T., Oldenborg, P., & Lundberg, P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.494591 · Cited by 34

Comprehensive profiling analysis of actively resorbing osteoclasts identifies critical signaling pathways regulated by bone substrate

Purdue, P. E., Crotti, T. N., Shen, Z., Swantek, J. L., Li, J., Hill, J. A., Hanidu, A., Dimock, J., Nabozny, G. H., Goldring, S. R., et al. (2014) · Scientific Reports · doi:10.1038/srep07595 · Cited by 29

Integrating Phosphoproteome and Transcriptome Reveals New Determinants of Macrophage Multinucleation

Rotival, M., Ko, J., Srivastava, P. K., Kerloc’h, A., Montoya, A., Mauro, C., Faull, P. A., Cutillas, P. R., Petretto, E. G., & Behmoaras, J. V. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.043836 · Cited by 28

Ostm1 Bifunctional Roles in Osteoclast Maturation: Insights From a Mouse Model Mimicking a Human OSTM1 Mutation

Pata, M., & Vacher, J. (2018) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3378 · Cited by 27

Interaction between the integrin Mac-1 and signal regulatory protein α (SIRPα) mediates fusion in heterologous cells

Podolnikova, N. P., Hlaváčková, M., Wu, Y., Yakubenko, V. P., Faust, J. J., Balabiyev, A., Wang, X., & Ugarova, T. P. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006314 · Cited by 26

Adrm1 interacts with Atp6v0d2 and regulates osteoclast differentiation

Kim, T. S., Ha, H., Kim, N., Yi, O., Lee, S. H., & Choi, Y. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.10.010 · Cited by 23

Surface microtopography modulates sealing zone development in osteoclasts cultured on bone

Shemesh, M., Addadi, L., & Geiger, B. (2017) · Journal of The Royal Society Interface · doi:10.1098/rsif.2016.0958 · Cited by 23

Mechanisms of RANKL delivery to the osteoclast precursor cell surface

Honma, M., Ikebuchi, Y., & Suzuki, H. (2020) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-020-01157-3 · Cited by 23

Targeting Msx2 as a brake in the fusion fate of osteoclasts and an anabolic therapy in pre-clinical models of osteoporosis

Ma, Q., Wang, S., Xue, H., Ni, L., Yuan, P., Shen, Y., Zheng, B., Wang, Q., Zhang, J., Wang, H., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61938-0 · Cited by 16

Μελέτη RANKL-επαγόμενων παθογενετικών μηχανισμών σε γενετικά ζωικά πρότυπα και νέες θεραπευτικές προσεγγίσεις

Ρηνώτας, Ε. (2014) · doi:10.12681/eadd/38366

[Partial purification and properties of proteases of bitoxibacillin].

Kuchera, M., & Nm, B. (1980) · PubMed

ANALYSIS OF PROTEASE KINDS AND ACTIVITIES IN SEVEN KINDS OF TISSUES AND ORGANS OF ANDRIAS DAVIDIANUS

Ze-hua, X. (2004) · Chieh P'ou Hsueh Pao

Detection of RANKL-producing cells and osteoclastic activation by the addition of exogenous RANKL in the regenerating scales of goldfish

Yamamoto, T., Ikegame, M., Kawago, U., Tabuchi, Y., Hirayama, J., Sekiguchi, T., Furusawa, Y., Yachiguchi, K., Matsubara, H., Urata, M., et al. (2020) · Biological Sciences in Space · doi:10.2187/bss.34.34 · Cited by 7

In search of partners: linking extracellular proteases to substrates

Overall, C. M., & Blobel, C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2120 · Cited by 353