1H, 13C and 15N backbone resonance assignment for the 40.5 kDa catalytic domain of Ubiquitin Specific Protease 7 (USP7)
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
http://link.springer.com/content/pdf/10.1007/s12104-016-9698-3.pdf
Reference18 articles.
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2. Brown CJ et al (2009) Awakening guardian angels: drugging the p53 pathway. Nat Rev Cancer 9(12):862–873
3. Chauhan D et al (2012) A small molecule inhibitor of ubiquitin-specific protease-7 induces apoptosis in multiple myeloma cells and overcomes bortezomib resistance. Cancer Cell 22(3):345–358
4. Delaglio F et al (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277–293
5. Faesen AC et al (2011) Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase. Mol Cell 44(1):147–159
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1. Dynamic regions allosterically connect the USP14 active site with the proteasome interaction surface;2024-07-02
2. Backbone 1H, 13C and 15N resonance assignment of the ubiquitin specific protease 7 catalytic domain (residues 208–554) in complex with a small molecule ligand;Biomolecular NMR Assignments;2024-03-12
3. Application of Nuclear Magnetic Resonance Spectroscopy for Studying Protein Three-dimensional Structure;PROG BIOCHEM BIOPHYS;2022
4. Discovery of Small-Molecule Inhibitors of Ubiquitin Specific Protease 7 (USP7) Using Integrated NMR and in Silico Techniques;Journal of Medicinal Chemistry;2017-12-08
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