The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
ADAM 12-S Cleaves IGFBP-3 and IGFBP-5 and Is Inhibited by TIMP-3
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Citations
Cites
Tissue inhibitors of metalloproteinases: evolution, structure and function
Brew, K., Dinakarpandian, D., & Nagase, H. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00279-4 · Cited by 1,908
Tissue inhibitors of metalloproteinases: structure, regulation and biological functions.
Gomez, D. E., Alonso, D. F., Yoshiji, H., & Thorgeirsson, U. P. (1997) · PubMed · Cited by 1,508
Lawrence, J. B., Oxvig, C., Overgaard, M. T., Sottrup-Jensen, L., Gleich, G. J., Hays, L. G., Yates, J. R., & Conover, C. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3149 · Cited by 706
TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3
Amour, A., Slocombe, P. M., Webster, A., Butler, M., Knight, C. G., Smith, B. J., Stephens, P. E., Shelley, C., Hutton, M., Knäuper, V., et al. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01031-x · Cited by 609
Self-citationThe ADAM gene family: surface proteins with adhesion and protease activity
Primakoff, P., & Myles, D. G. (2000) · Trends in Genetics · doi:10.1016/s0168-9525(99)01926-5 · Cited by 582
Schlöndorff, J., & Blobel, C. P. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.21.3603 · Cited by 550
A metalloprotease-disintegrin participating in myoblast fusion
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ADAMs: focus on the protease domain
Black, R. A., & White, J. M. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80042-2 · Cited by 467
The in vitro activity of ADAM‐10 is inhibited by TIMP‐1 and TIMP‐3
Amour, A., Knight, C. G., Webster, A., Slocombe, P. M., Stephens, P. E., Knäuper, V., Docherty, A. J. P., & Murphy, G. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01528-3 · Cited by 404
Self-citationA Novel, Secreted Form of Human ADAM 12 (Meltrin α) Provokes Myogenesis in Vivo
Gilpin, B. J., Loechel, F., Mattei, M.-G., Engvall, E., Albrechtsen, R., & Wewer, U. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.157 · Cited by 315
Self-citationIba, K., Albrechtsen, R., Gilpin, B., Fröhlich, C., Loechel, F., Zolkiewska, A., Ishiguro, K., Kojima, T., Liu, W., Langford, J. K., et al. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.5.1143 · Cited by 248
Self-citationWillenbrock, F., Crabbe, T., Slocombe, P. M., Sutton, C. W., Docherty, A. J. P., Cockett, M. I., O'Shea, M., Brocklehurst, K., Phillips, I. R., & Murphy, G. (1993) · Biochemistry · doi:10.1021/bi00067a023 · Cited by 237
Self-citationInsulin-Like Growth Factor Binding Proteins: New Proteins, New Functions
Ferry Jr., R. J., Cerri, R. W., & Cohen, P. (1999) · Hormone Research in Paediatrics · doi:10.1159/000023315 · Cited by 205
Cysteine-Rich Domain of Human ADAM 12 (Meltrin α) Supports Tumor Cell Adhesion
Iba, K., Albrechtsen, R., Gilpin, B. J., Loechel, F., & Wewer, U. M. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65403-x · Cited by 204
Self-citationHuman ADAM 12 (Meltrin α) Is an Active Metalloprotease
Loechel, F., Gilpin, B. J., Engvall, E., Albrechtsen, R., & Wewer, U. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.27.16993 · Cited by 187
Self-citationADAM 12, a Disintegrin Metalloprotease, Interacts with Insulin-like Growth Factor-binding Protein-3
Shi, Z., Xu, W., Loechel, F., Wewer, U. M., & Murphy, L. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002172200 · Cited by 179
Self-citationIntracellular Maturation of the Mouse Metalloprotease Disintegrin MDC15
Lum, L., Reid, M. S., & Blobel, C. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.26236 · Cited by 167
Thrailkill, K. M., Quarles, L. D., Nagase, H., Suzuki, K., SERRA, D. M., & Fowlkes, J. L. (1995) · Endocrinology · doi:10.1210/en.136.8.3527 · Cited by 163
Stone, A. L., Kröger, M., & Sang, Q. A. (1999) · Journal of Protein Chemistry · doi:10.1023/a:1020692710029 · Cited by 161
Regulation of Human ADAM 12 Protease by the Prodomain
Loechel, F., Overgaard, M. T., Oxvig, C., Albrechtsen, R., & Wewer, U. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13427 · Cited by 131
Self-citationInoue, D., Reid, M. S., Lum, L., Krätzschmar, J., Weskamp, G., Myung, Y. M., Baron, R., & Blobel, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.7.4180 · Cited by 105
Kaushal, G. P., & Shah, S. V. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10078 · Cited by 77
Bang, P., & Fielder, P. J. (1997) · Endocrinology · doi:10.1210/endo.138.9.5371 · Cited by 41
Cited by
Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575
Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting
Gialeli, C., Theocharis, A. D., & Karamanos, N. K. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07919.x · Cited by 1,607
EDWARDS, D., HANDSLEY, M., & PENNINGTON, C. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.001 · Cited by 1,161
Metalloproteinases and their inhibitors: Regulators of wound healing
Gill, S. E., & Parks, W. C. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.10.024 · Cited by 742
The role of TIMPs in regulation of extracellular matrix proteolysis
Arpino, V., Brock, M., & Gill, S. E. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.03.005 · Cited by 734
Metadata
- Authors
- Loechel, F., Fox, J. W., Murphy, G., Albrechtsen, R., & Wewer, U. M.
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2000-11
- Volume
- 278
- Issue
- 3
- Pages
- 511-515
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2080673945
- Cited by
- 314
- References
- 23
- FWCI
- 6.24
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
