Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

By H. Shimura, N. Hattori, S. Kubo, Y. Mizuno, S. Asakawa, S. Minoshima, N. Shimizu, K. Iwai, T. Chiba, Keiji Tanaka and 1 more. Nature Genetics, 2000

2,122 citations recorded by the source corpus.

Subfields: Epidemiology, Molecular Biology, Neurology

View Paper: https://www.semanticscholar.org/paper/eabf2dde9fc6bc6f6b21f7b83cf2cb5d370e2aab

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Citations in the corpus

Expression of A53T Mutant But Not Wild-Type α-Synuclein in PC12 Cells Induces Alterations of the Ubiquitin-Dependent Degradation System, Loss of Dopamine Release, and Autophagic Cell Death (2001, background): “…ligase, responsible for the attachment of ubiquitin to substrates such as CDCrel-1, Pael receptor, and, possibly, a glycosylated form of -synuclein (Shimura et al., 2000; Zhang et al., 2000; Imai et al., 2001; Shimura et al., 2001), and UCHL-1 is a member of the family of deubiquitinating enzymes,…”
Molecular pathophysiology of Parkinson's disease. (2005, background): “Like many other RING finger–containing proteins, parkin can function as an E3 ubiquitin protein ligase (Shimura et al. 2000, Zhang et al. 2000).”
Mitochondrial Dysfunction in Parkinson's Disease (2011, background): “These proteins have been shown to interact and are also involved in proteasomal functions [160, 161].”
The Roles of PINK1, Parkin and Mitochondrial Fidelity in Parkinson's Disease (2015, background): “Parkin is an E3 ubiquitin ligase with an amino-terminal ubiquitin-like (Ubl) domain and a carboxyl-terminal ubiquitin ligase domain (Hristova et al., 2009; Shimura et al., 2000).”
RING finger proteins: mediators of ubiquitin ligase activity. (2000, background): “RPTKs are ubiquitinated sates, and the nature of the ubiquitinated species now in response to activating stimuli and degraded primarily become of great interest (Shimura et al., 2000). in lysosomes.”
Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences (2012, positive): “The presence of the RBR domain suggested that parkin acts as an E3 ubiquitin ligase, mediating the covalent attachment of ubiquitin moieties to substrate proteins (Shimura et al , 2000; Zhang et al , 2000).”
Parkinson-Like Neurodegeneration Induced by Targeted Overexpression of α-Synuclein in the Nigrostriatal System (2002, background): “(Shimura et al., 2000), and ubiquitin C-terminal-hydroxylase-L1,”