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From the same journal

Potent and selective activity-based probes for GH27 human retaining α-galactosidases

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Potent and selective activity-based probes for GH27 human retaining α-galactosidases. / Willems, Lianne I.; Beenakker, Thomas J. M.; Murray, Benjamin S.; Scheij, Saskia; Kallemeijn, Wouter W.; Boot, Rolf G.; Verhoek, Marri; Donker-Koopman, Wilma E.; Ferraz, Maria J.; Rijssel, Erwin R. van; Florea, Bogdan I.; Codée, Jeroen D C; Van Der Marel, Gijsbert A.; Aerts, Johannes M F G; Overkleeft, Herman S.

In: Journal of the American Chemical Society, Vol. 136, No. 33, 08.08.2014, p. 11622-11625.

Research output: Contribution to journalArticlepeer-review

Harvard

Willems, LI, Beenakker, TJM, Murray, BS, Scheij, S, Kallemeijn, WW, Boot, RG, Verhoek, M, Donker-Koopman, WE, Ferraz, MJ, Rijssel, ERV, Florea, BI, Codée, JDC, Van Der Marel, GA, Aerts, JMFG & Overkleeft, HS 2014, 'Potent and selective activity-based probes for GH27 human retaining α-galactosidases', Journal of the American Chemical Society, vol. 136, no. 33, pp. 11622-11625. https://doi.org/10.1021/ja507040n

APA

Willems, L. I., Beenakker, T. J. M., Murray, B. S., Scheij, S., Kallemeijn, W. W., Boot, R. G., Verhoek, M., Donker-Koopman, W. E., Ferraz, M. J., Rijssel, E. R. V., Florea, B. I., Codée, J. D. C., Van Der Marel, G. A., Aerts, J. M. F. G., & Overkleeft, H. S. (2014). Potent and selective activity-based probes for GH27 human retaining α-galactosidases. Journal of the American Chemical Society, 136(33), 11622-11625. https://doi.org/10.1021/ja507040n

Vancouver

Willems LI, Beenakker TJM, Murray BS, Scheij S, Kallemeijn WW, Boot RG et al. Potent and selective activity-based probes for GH27 human retaining α-galactosidases. Journal of the American Chemical Society. 2014 Aug 8;136(33):11622-11625. https://doi.org/10.1021/ja507040n

Author

Willems, Lianne I. ; Beenakker, Thomas J. M. ; Murray, Benjamin S. ; Scheij, Saskia ; Kallemeijn, Wouter W. ; Boot, Rolf G. ; Verhoek, Marri ; Donker-Koopman, Wilma E. ; Ferraz, Maria J. ; Rijssel, Erwin R. van ; Florea, Bogdan I. ; Codée, Jeroen D C ; Van Der Marel, Gijsbert A. ; Aerts, Johannes M F G ; Overkleeft, Herman S. / Potent and selective activity-based probes for GH27 human retaining α-galactosidases. In: Journal of the American Chemical Society. 2014 ; Vol. 136, No. 33. pp. 11622-11625.

Bibtex - Download

@article{c82fc85add2842fc86793bc5da84e84d,
title = "Potent and selective activity-based probes for GH27 human retaining α-galactosidases",
abstract = "Lysosomal degradation of glycosphingolipids is mediated by the consecutive action of several glycosidases. Malfunctioning of one of these hydrolases can lead to a lysosomal storage disorder such as Fabry disease, which is caused by a deficiency in α-galactosidase A. Herein we describe the development of potent and selective activity-based probes that target retaining α-galactosidases. The fluorescently labeled aziridine-based probes 3 and 4 inhibit the two human retaining α-galactosidases αGal A and αGal B covalently and with high affinity. Moreover, they enable the visualization of the endogenous activity of both α-galactosidases in cell extracts, thereby providing a means to study the presence and location of active enzyme levels in different cell types, such as healthy cells versus those derived from Fabry patients.",
author = "Willems, {Lianne I.} and Beenakker, {Thomas J. M.} and Murray, {Benjamin S.} and Saskia Scheij and Kallemeijn, {Wouter W.} and Boot, {Rolf G.} and Marri Verhoek and Donker-Koopman, {Wilma E.} and Ferraz, {Maria J.} and Rijssel, {Erwin R. van} and Florea, {Bogdan I.} and Cod{\'e}e, {Jeroen D C} and {Van Der Marel}, {Gijsbert A.} and Aerts, {Johannes M F G} and Overkleeft, {Herman S.}",
year = "2014",
month = aug,
day = "8",
doi = "10.1021/ja507040n",
language = "English",
volume = "136",
pages = "11622--11625",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "33",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Potent and selective activity-based probes for GH27 human retaining α-galactosidases

AU - Willems, Lianne I.

AU - Beenakker, Thomas J. M.

AU - Murray, Benjamin S.

AU - Scheij, Saskia

AU - Kallemeijn, Wouter W.

AU - Boot, Rolf G.

AU - Verhoek, Marri

AU - Donker-Koopman, Wilma E.

AU - Ferraz, Maria J.

AU - Rijssel, Erwin R. van

AU - Florea, Bogdan I.

AU - Codée, Jeroen D C

AU - Van Der Marel, Gijsbert A.

AU - Aerts, Johannes M F G

AU - Overkleeft, Herman S.

PY - 2014/8/8

Y1 - 2014/8/8

N2 - Lysosomal degradation of glycosphingolipids is mediated by the consecutive action of several glycosidases. Malfunctioning of one of these hydrolases can lead to a lysosomal storage disorder such as Fabry disease, which is caused by a deficiency in α-galactosidase A. Herein we describe the development of potent and selective activity-based probes that target retaining α-galactosidases. The fluorescently labeled aziridine-based probes 3 and 4 inhibit the two human retaining α-galactosidases αGal A and αGal B covalently and with high affinity. Moreover, they enable the visualization of the endogenous activity of both α-galactosidases in cell extracts, thereby providing a means to study the presence and location of active enzyme levels in different cell types, such as healthy cells versus those derived from Fabry patients.

AB - Lysosomal degradation of glycosphingolipids is mediated by the consecutive action of several glycosidases. Malfunctioning of one of these hydrolases can lead to a lysosomal storage disorder such as Fabry disease, which is caused by a deficiency in α-galactosidase A. Herein we describe the development of potent and selective activity-based probes that target retaining α-galactosidases. The fluorescently labeled aziridine-based probes 3 and 4 inhibit the two human retaining α-galactosidases αGal A and αGal B covalently and with high affinity. Moreover, they enable the visualization of the endogenous activity of both α-galactosidases in cell extracts, thereby providing a means to study the presence and location of active enzyme levels in different cell types, such as healthy cells versus those derived from Fabry patients.

UR - http://www.scopus.com/inward/record.url?scp=84906351443&partnerID=8YFLogxK

U2 - 10.1021/ja507040n

DO - 10.1021/ja507040n

M3 - Article

C2 - 25105979

AN - SCOPUS:84906351443

VL - 136

SP - 11622

EP - 11625

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 33

ER -