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Galdeano, C
, Gadd, MS, Soares, P, Scaffidi, S, van Molle, I, Birced, I, Hewitt, S, Dias, DM & Ciulli, A 2014, '
Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von Hippel-Lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities.',
Journal of Medicinal Chemistry, vol. 57, no. 20, pp. 8657-8663.
https://doi.org/10.1021/jm5011258APA
Galdeano, C.
, Gadd, M. S., Soares, P., Scaffidi, S., van Molle, I., Birced, I., Hewitt, S., Dias, D. M., & Ciulli, A. (2014).
Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von Hippel-Lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities. Journal of Medicinal Chemistry,
57(20), 8657-8663.
https://doi.org/10.1021/jm5011258Vancouver
Author
Bibtex
@article{c2de9dda2fb94e7a8f913217d7025f71,
title = "Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von Hippel-Lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities.",
abstract = "E3 ubiquitin ligases are attractive targets in the ubiquitin-proteasome system, however, the development of small-molecule ligands has been rewarded with limited success. The von Hippel-Lindau protein (pVHL) is the substrate recognition subunit of the VHL E3 ligase that targets HIF-1α for degradation. We recently reported inhibitors of the pVHL:HIF-1α interaction, however they exhibited moderate potency. Herein, we report the design and optimization, guided by X-ray crystal structures, of a ligand series with nanomolar binding affinities.",
author = "Carles Galdeano and Gadd, {Morgan Stuart} and Pedro Soares and Salvatore Scaffidi and {van Molle}, Inge and Ipek Birced and Sarah Hewitt and Dias, {David M} and Alessio Ciulli",
year = "2014",
month = oct,
day = "23",
doi = "10.1021/jm5011258",
language = "English",
volume = "57",
pages = "8657--8663",
journal = "Journal of Medicinal Chemistry",
issn = "0022-2623",
publisher = "American Chemical Society",
number = "20",
}
RIS
TY - JOUR
T1 - Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von Hippel-Lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities.
AU - Galdeano, Carles
AU - Gadd, Morgan Stuart
AU - Soares, Pedro
AU - Scaffidi, Salvatore
AU - van Molle, Inge
AU - Birced, Ipek
AU - Hewitt, Sarah
AU - Dias, David M
AU - Ciulli, Alessio
PY - 2014/10/23
Y1 - 2014/10/23
N2 - E3 ubiquitin ligases are attractive targets in the ubiquitin-proteasome system, however, the development of small-molecule ligands has been rewarded with limited success. The von Hippel-Lindau protein (pVHL) is the substrate recognition subunit of the VHL E3 ligase that targets HIF-1α for degradation. We recently reported inhibitors of the pVHL:HIF-1α interaction, however they exhibited moderate potency. Herein, we report the design and optimization, guided by X-ray crystal structures, of a ligand series with nanomolar binding affinities.
AB - E3 ubiquitin ligases are attractive targets in the ubiquitin-proteasome system, however, the development of small-molecule ligands has been rewarded with limited success. The von Hippel-Lindau protein (pVHL) is the substrate recognition subunit of the VHL E3 ligase that targets HIF-1α for degradation. We recently reported inhibitors of the pVHL:HIF-1α interaction, however they exhibited moderate potency. Herein, we report the design and optimization, guided by X-ray crystal structures, of a ligand series with nanomolar binding affinities.
U2 - 10.1021/jm5011258
DO - 10.1021/jm5011258
M3 - Journal article
VL - 57
SP - 8657
EP - 8663
JO - Journal of Medicinal Chemistry
JF - Journal of Medicinal Chemistry
SN - 0022-2623
IS - 20
ER -
