Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe

Lenger J, Kaschani F, Lenz T, Dalhoff C, Villamor JG, Köster H, Sewald N, van der Hoorn RAL (2012)
Bioorganic & Medical Chemistry 20(2): 592-596.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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DOI
Autor*in
Lenger, Janina; Kaschani, Farnusch; Lenz, Thomas; Dalhoff, Christian; Villamor, Joji Grace; Köster, Hubert; Sewald, NorbertUniBi ; van der Hoorn, Renier A.L.
Einrichtung
Fakultät für Chemie > Organische Chemie III
Centrum für Biotechnologie > Arbeitsgruppe N. Sewald
Erscheinungsjahr
2012
Zeitschriftentitel
Bioorganic & Medical Chemistry
Band
20
Ausgabe
2
Seite(n)
592-596
ISSN
0968-0896
Page URI
https://pub.uni-bielefeld.de/record/2499568

Zitieren

Lenger J, Kaschani F, Lenz T, et al. Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe. Bioorganic & Medical Chemistry. 2012;20(2):592-596.
Lenger, J., Kaschani, F., Lenz, T., Dalhoff, C., Villamor, J. G., Köster, H., Sewald, N., et al. (2012). Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe. Bioorganic & Medical Chemistry, 20(2), 592-596. doi:10.1016/j.bmc.2011.06.068
Lenger, Janina, Kaschani, Farnusch, Lenz, Thomas, Dalhoff, Christian, Villamor, Joji Grace, Köster, Hubert, Sewald, Norbert, and van der Hoorn, Renier A.L. 2012. “Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe”. Bioorganic & Medical Chemistry 20 (2): 592-596.
Lenger, J., Kaschani, F., Lenz, T., Dalhoff, C., Villamor, J. G., Köster, H., Sewald, N., and van der Hoorn, R. A. L. (2012). Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe. Bioorganic & Medical Chemistry 20, 592-596.
Lenger, J., et al., 2012. Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe. Bioorganic & Medical Chemistry, 20(2), p 592-596.
J. Lenger, et al., “Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe”, Bioorganic & Medical Chemistry, vol. 20, 2012, pp. 592-596.
Lenger, J., Kaschani, F., Lenz, T., Dalhoff, C., Villamor, J.G., Köster, H., Sewald, N., van der Hoorn, R.A.L.: Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe. Bioorganic & Medical Chemistry. 20, 592-596 (2012).
Lenger, Janina, Kaschani, Farnusch, Lenz, Thomas, Dalhoff, Christian, Villamor, Joji Grace, Köster, Hubert, Sewald, Norbert, and van der Hoorn, Renier A.L. “Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe”. Bioorganic & Medical Chemistry 20.2 (2012): 592-596.

9 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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Discovery of Arabidopsis UGT73C1 as a steviol-catalyzing UDP-glycosyltransferase with chemical probes.
Zhou Y, Li W, You W, Di Z, Wang M, Zhou H, Yuan S, Wong NK, Xiao Y., Chem Commun (Camb) 54(52), 2018
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Investigation of the anti-angiogenesis effects induced by deoxypodophyllotoxin-5-FU conjugate C069 against HUVE cells.
Xiang R, Guan XW, Hui L, Jin YX, Chen SW., Bioorg Med Chem Lett 27(4), 2017
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Synthesis of hybrid 4-deoxypodophyllotoxin-5-fluorouracil compounds that inhibit cellular migration and induce cell cycle arrest.
Guan XW, Xu XH, Feng SL, Tang ZB, Chen SW, Hui L., Bioorg Med Chem Lett 26(6), 2016
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The Increasing Impact of Activity-Based Protein Profiling in Plant Science.
Morimoto K, van der Hoorn RA., Plant Cell Physiol 57(3), 2016
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Broad-range glycosidase activity profiling.
Chandrasekar B, Colby T, Emran Khan Emon A, Jiang J, Hong TN, Villamor JG, Harzen A, Overkleeft HS, van der Hoorn RA., Mol Cell Proteomics 13(10), 2014
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Brown LJ, Baranowski M, Wang Y, Schrey AK, Lenz T, Taverna SD, Cole PA, Sefkow M., Anal Biochem 467(), 2014
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Sakurai K, Tawa M, Okada A, Yamada R, Sato N, Inahara M, Inoue M., Chem Asian J 7(7), 2012
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