Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1.

By Yi Zhang, Junqing Gao, Kenny K K Chung, Hui-li Huang, Valina L. Dawson, T. Dawson. Proceedings of the National Academy of Sciences of the United States of America, 2000

989 citations recorded by the source corpus.

Subfields: Epidemiology, Molecular Biology, Neurology

View Paper: https://www.semanticscholar.org/paper/11e5918fd81b276b03b13c6c721a2427a84fe40f

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Epidemiology

In Molecular Biology

In Neurology

Citations in the corpus

Alpha-synuclein and neurodegenerative diseases (2001, background): “Parkin functions as a ubiquitin ligase, and the known mutations are believed to lead to a loss of its functio”
The Role of Oxidative Stress in Parkinson’s Disease (2013, background): “Parkin is a cytoplasmic and nuclear protein that functions as an E3 ubiquitin ligase, and the loss of this activity due to mutations is associated with autosomal recessive early-onset PD [296] [297] [298].”
Genetic Animal Models of Parkinson’s Disease (2010, positive): “Parkin functions as an E3 ubiquitin ligase where it participates in the ubiquitin proteasome system (Figure 2) (Shimura et al., 2000; Zhang et al., 2000).”
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): “…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, which remove…”
The Continuing Challenges of Leprosy (2006, background): “Functionally, the specific locus identified codes for the synthesis of a ligase in the ubiquitin-proteasome pathway of intracellular protein degradation (454).”
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).”
The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. (2002, background): “Parkin ubiquitinates and promotes degradation of several proteins, among them is CDCrel-1, a synaptic vesicle-enriched septin GTPase implicated in the inhibition of exocytosis through its interactions with syntaxin (498).”
Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases (2004, background): “This structure is consistent with parkin functioning as an E3 ubiquitin ligase, and such activity has been demonstrate”
Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences (2012, neutral): “The mechanism underlying the tumour suppressor activity of parkin is not well understood.”
The roles of intracellular protein-degradation pathways in neurodegeneration (2006, background): “These include parkin, an E3 ligase in which autosomal recessive loss-of-function mutations cause P”
Pathogenesis of parkinson's disease: dopamine, vesicles and α-synuclein (2002, background): “This enzyme transfers activated ubiquitin to an E2 ubiquitin-conjugating enzyme, which together with an E3 ubiquitin-ligating enzyme (such as parkin, which is encoded by PARK2”