The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation.
Open accessAbstract
The ligand for osteoprotegerin has been identified, and it is a TNF-related cytokine that replaces the requirement for stromal cells, vitamin D3, and glucocorticoids in the coculture model of in vitro osteoclastogenesis. OPG ligand (OPGL) binds to a unique hematopoeitic progenitor cell that is committed to the osteoclast lineage and stimulates the rapid induction of genes that typify osteoclast development. OPGL directly activates isolated mature osteoclasts in vitro, and short-term administration into normal adult mice results in osteoclast activation associated with systemic hypercalcemia. These data suggest that OPGL is an osteoclast differentiation and activation factor. The effects of OPGL are blocked in vitro and in vivo by OPG, suggesting that OPGL and OPG are key extracellular regulators of osteoclast development.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“RANKL was implicated in the fusion of osteoclast precursors into multinucleated cells (39), their differentiation into mature osteoclasts (39), their attachment to bone surfaces (12), their activation to resorb bone (9,39), and their continued survival by avoiding apoptosis (11).”
From Receptor Activator of Nuclear Factor κB Ligand and Osteoprotegerin Regulation of Bone Remodeling in Health and Disease (2008) · cites this paper as [39]
In the citing paper
“OCs differentiate from monocyte/macrophage progenitors following M-CSF [5] and RANKL [6] stimulation.”
From PU.1 target genes undergo Tet2-coupled demethylation and DNMT3b-mediated methylation in monocyte-to-osteoclast differentiation (2013) · cites this paper as [6]
Citations
Cites
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
Self-citationIdentification and characterization of a new member of the TNF family that induces apoptosis
Wiley, S. R., Schooley, K., Smolak, P. J., Din, W. S., Huang, C.-P., Nicholl, J. K., Sutherland, G. R., Smith, T. D., Rauch, C., Smith, C. A., et al. (1995) · Immunity · doi:10.1016/1074-7613(95)90057-8 · Cited by 2,900
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
Induction of Apoptosis by Apo-2 Ligand, a New Member of the Tumor Necrosis Factor Cytokine Family
Pitti, R. M., Marsters, S. A., Ruppert, S., Donahue, C. J., Moore, A., & Ashkenazi, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.12687 · Cited by 1,777
Banner, D. W., D'Arcy, A., Janes, W., Gentz, R., Schönfeld, H., Broger, C., Loetscher, H., & Lesslauer, W. (1993) · Cell · doi:10.1016/0092-8674(93)90132-a · Cited by 1,097
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
Modulation of Osteoclast Differentiation
Suda, T., Takahashi, N., & Martin, T. J. (1992) · Endocrine Reviews · doi:10.1210/edrv-13-1-66 · Cited by 1,004
Takahashi, N., Yamana, H., Yoshiki, S., Roodman, G. D., Mundy, G. R., Jones, S. J., BOYDE, A., & Suda, T. (1988) · Endocrinology · doi:10.1210/endo-122-4-1373 · Cited by 731
Signal Transduction by DR3, a Death Domain-Containing Receptor Related to TNFR-1 and CD95
Chinnaiyan, A. M., O’Rourke, K. M., Yu, G.-L., Lyons, R. H., Garg, M., Duan, D. R., Xing, L., Gentz, R., Ni, J., & Dixit, V. M. (1996) · Science · doi:10.1126/science.274.5289.990 · Cited by 653
Bone resorbing activity in supernatant fluid from cultured human peripheral blood leukocytes
Horton, J. E., Raisz, L. G., Simmons, H. A., Oppenheim, J. J., & Mergenhagen, S. E. (1972) · Science · doi:10.1126/science.177.4051.793 · Cited by 565
Effect of pH on Bone Resorption by Rat Osteoclastsin Vitro
Arnett, T. R., & Dempster, D. W. (1986) · Endocrinology · doi:10.1210/endo-119-1-119 · Cited by 349
Fundamental principles of in situ hybridization.
Wilcox, J. N. (1993) · Journal of Histochemistry & Cytochemistry · doi:10.1177/41.12.8245419 · Cited by 246
B61 is a ligand for the ECK receptor protein-tyrosine kinase
Bartley, T. D., Hunt, R. W., Welcher, A. A., et al. (1994) · Nature · doi:10.1038/368558a0 · Cited by 246
Wilson, C., Payton, M. N., Elliott, G., Buaas, F. W., Cajulis, E. E., Grosshans, D. R., Ramos, L., Reese, D., Slamon, D. J., & Calzone, F. J. (1997) · Oncogene · doi:10.1038/sj.onc.1200924 · Cited by 193
Self-citationATAR, a Novel Tumor Necrosis Factor Receptor Family Member, Signals through TRAF2 and TRAF5
Hsu, H., Solovyev, I., Colombero, A. M., Elliott, R., Kelley, M. J., & Boyle, W. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.21.13471 · Cited by 180
Self-citationAbe, E., Tanaka, H., Ishimi, Y., Miyaura, C., Hayashi, T., Nagasawa, H. T., Tomida, M., Yamaguchi, Y., Hozumi, M., & Suda, T. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.16.5958 · Cited by 126
Lacey, D. L., Erdmann, J. M., Teitelbaum, S. L., Tan, H., Ohara, J., & Shioi, A. (1995) · Endocrinology · doi:10.1210/endo.136.6.7750457 · Cited by 87
Self-citationMapping the Domain(s) Critical for the Binding of Human Tumor Necrosis Factor-α to Its Two Receptors
Chen, P. C.-H., DuBois, G. C., & Chen, M.-J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2874 · Cited by 58
Fuller, K., Gallagher, A. C., & Chambers, T. J. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81382-8 · Cited by 52
Isolation of a murine osteoclast colony-stimulating factor.
Lee, M. Y., Eyre, D. R., & Osborne, W. R. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8500 · Cited by 41
Osteoclast recruiting activity in bone matrix
Hentunen, T. A., Cunningham, N. S., Vuolteenaho, O. J., Reddi, A. H., & Väänänen, H. K. (1994) · Bone and Mineral · doi:10.1016/s0169-6009(08)80238-3 · Cited by 25
A novel cytokine with osteoclastopoietic activity
Yoneda, T., Kato, I., Bonewald, L. F., Burgess, W. H., & Mundy, G. R. (1993) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.1993.tb02117.x · Cited by 9
Research works printed but not linked: 1
- Evans, 1979, Histochemical identification of osteoclasts in undecalcified sections of human bone, Mineral Electolyte Metab., 2, 179
Cited by
Sorted by citations
Osteoclast differentiation and activation
Boyle, W. J., Simonet, W. S., & Lacey, D. L. (2003) · Nature · doi:10.1038/nature01658 · Cited by 6,670
Self-citationOPGL 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
Self-citationSignalling pathways of the TNF superfamily: a double-edged sword
Aggarwal, B. B. (2003) · Nature Reviews Immunology · doi:10.1038/nri1184 · Cited by 2,793
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
Leptin Inhibits Bone Formation through a Hypothalamic Relay
Ducy, P., Amling, M., Takeda, S., Priemel, M., Schilling, A. F., Beil, F. T., Shen, J., Vinson, C., Rueger, J. M., & Karsenty, G. (2000) · Cell · doi:10.1016/s0092-8674(00)81558-5 · Cited by 2,077
Metadata
- Authors
- Lacey, D. L., Timms, E., Tan, H.-L., Kelley, M. J., Dunstan, C. R., Burgess, T., Elliott, R., Colombero, A., Elliott, G., Scully, S., Hsu, H., Sullivan, J., Hawkins, N., Davy, E., Capparelli, C., Eli, A., Qian, Y.-X., Kaufman, S., Sarosi, I., Shalhoub, V, Senaldi, G., Guo, J., Delaney, J., & Boyle, W. J.
- Affiliations
- Amgen (United States) (US)
- Corresponding author
- Boyle, W.J
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1998-04
- Volume
- 93
- Issue
- 2
- Pages
- 165-176
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2048299560
- Cited by
- 5,439
- References
- 23
- Citations by year
- 2026: 74 · 2025: 86 · 2024: 96 · 2023: 97 · 2022: 125 · 2021: 171 · 2020: 167 · 2019: 174 · 2018: 174 · 2017: 201 · 2016: 147 · 2015: 211 · 2014: 225 · 2013: 234 · 2012: 272
- FWCI
- 61.29
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Amgen
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
- Health Sciences › Medicine › Rheumatology › Rheumatoid Arthritis Research and Therapies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
- Keywords
- osteoprotegerin ligand, osteoprotegerin, osteoclastogenesis, osteoclast activation, hypercalcemia, bone remodeling
- MeSH terms
- Amino Acid Sequence, Animals, Bone Resorption, Carrier Proteins, Cell Differentiation, Cells, Cultured, Cloning, Molecular, Glycoproteins, Hematopoietic Stem Cells, Humans, Hypercalcemia, Ligands, Membrane Glycoproteins, Molecular Sequence Data, Organ Specificity, Osteoclasts, Protein Binding, Recombinant Fusion Proteins, RNA, Messenger, Macrophage Colony-Stimulating Factor, Cytokines, Receptors, Tumor Necrosis Factor, Receptors, Cytoplasmic and Nuclear, Gene Expression Regulation, Developmental, Coculture Techniques, Mice, Rats, Osteoprotegerin, RANK Ligand, Receptor Activator of Nuclear Factor-kappa B
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
