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Nafizul Kazi on Muck Rack

Nafizul Kazi

As seen in: Nature, ACS Publications, BioRxiv
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Articles

Chimeric deubiquitinase engineering reveals structural basis for specific inhibition of the mitophagy regulator USP30 - Nature Structural & Molecular Biology

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By Nafizul Kazi, Nikolas Klink, Kai Gallant, Gian-Marvin Kipka
| Nature Verified
Abstract The mitochondrial deubiquitinase ubiquitin-specific protease (USP) 30 negatively regulates PINK1–parkin-driven mitophagy. Whether enhanced mitochondrial quality control through inhibition of USP30 can protect dopaminergic neurons is currently being explored in a clinical trial for Parkinson’s disease. However, the molecular basis for specific inhibition of USP30 by small molecules has remained elusive.
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Discovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53 - Nature Chemical Biology

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By Kim Wendrich, Kai Gallant, Stavroula Petroulia, Nafizul Kazi, Rachel O’Dea, Jeroen A. Demmers, Jan André Hane, Siska Führer
| Nature Verified
Abstract Ubiquitin-specific proteases (USPs) represent the largest class of human deubiquitinases (DUBs) and comprise its phylogenetically most distant members USP53 and USP54, which are annotated as catalytically inactive pseudoenzymes. Conspicuously, mutations within the USP domain of USP53 cause progressive familial intrahepatic cholestasis. Here, we report the discovery that USP53 and USP54 are active DUBs with high specificity for K63-linked polyubiquitin.
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Chimeric deubiquitinase engineering reveals structural basis for specific inhibition of USP30 and a framework for DUB ligandability

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By Nafizul Kazi, Kai Gallant, Gian-Marvin Kipka, Nikolas Klink
| BioRxiv
Abstract The mitochondrial deubiquitinase USP30 negatively regulates Pink1/Parkin-driven mitophagy. Whether enhanced mitochondrial quality control through inhibition of USP30 can protect dopaminergic neurons is currently explored in a clinical trial for Parkinson's disease. However, the molecular basis for specific inhibition of USP30 by small molecules has remained elusive.
Open in Who Shared Issue with article?
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