The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2
Open accessAbstract
The inhibition of new blood vessel formation (angiogenesis) is an effective means of limiting both the size and metastasis of solid tumors. The leading anti-angiogenic compound, TNP-470, has proven to be effective in in vitro and in animal model studies, and is currently being tested in phase III antitumor clinical trials. Despite many detailed pharmacological studies, little is known of the molecular mode of action of TNP-470. Using a derivative of the TNP-470 parent compound, the fungal metabolite, fumagillin, we have purified a mammalian protein that is selectively and covalently bound by this natural product. This fumagillin binding protein was found to be a metalloprotease, methionine aminopeptidase (MetAP-2), that is highly conserved between human and Saccharomyces cerevisiae . In the absence of MetAP-1, a distantly related methionine aminopeptidase, MetAP-2 function is essential for vegetative growth in yeast. We demonstrate that fumagillin selectively inhibits the S. cerevisiae MetAP-2 protein in vivo . The binding is highly specific as judged by the failure of fumagillin to inhibit MetAP-1 in vivo . Hence, these results identify MetAP-2 as an important target of study in the analysis of the potent biological activities of fumagillin.
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Kim, K. J., Li, B., Winer, J., Armanini, M., Gillett, N., Phillips, H. S., & Ferrara, N. (1993) · Nature · doi:10.1038/362841a0 · Cited by 3,605
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Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
Cited by
Sakamoto, K. M., Kim, K. B., Kumagai, A., Mercurio, F., Crews, C. M., & Deshaies, R. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.141230798 · Cited by 2,609
Self-citationInduced protein degradation: an emerging drug discovery paradigm
Lai, A. C., & Crews, C. M. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.211 · Cited by 1,486
Self-citationEffects of Angiogenesis Inhibitors on Multistage Carcinogenesis in Mice
Bergers, G., Javaherian, K., Lo, K.-M., Folkman, J., & Hanahan, D. (1999) · Science · doi:10.1126/science.284.5415.808 · Cited by 988
Pathogenesis of Aspergillus fumigatus in Invasive Aspergillosis
Dagenais, T. R. T., & Keller, N. P. (2009) · Clinical Microbiology Reviews · doi:10.1128/cmr.00055-08 · Cited by 993
Moulton, K. S., Heller, E., Konerding, M. A., Flynn, E., Palinski, W., & Folkman, J. (1999) · Circulation · doi:10.1161/01.cir.99.13.1726 · Cited by 688
Metadata
- Authors
- Sin, N., Meng, L., Wang, M. Q. W., Wen, J. J., Bornmann, W. G., & Crews, C. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-06-10
- Volume
- 94
- Issue
- 12
- Pages
- 6099-6103
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2107257265
- Cited by
- 635
- References
- 2
- FWCI
- 10.03
- Type
- journal article
- Language
- en
- Open access
- green
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- Sin, N., Meng, L., Wang, M. Q. W., Wen, J. J., Bornmann, W. G., & Crews, C. M. (1997). The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.94.12.6099
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