Associated Papers
Deubiquitinases in muscle physiology and disorders.
Olie CS et al.
Biochemical Society Transactions, 2024
Ubiquitin Carboxyl-Terminal Hydrolase L1 and Its Role in Parkinson's Disease.
Buneeva O et al.
International Journal of Molecular Sciences, 2024
Antibody toolkit reveals N-terminally ubiquitinated substrates of UBE2W.
Davies CW et al.
Nature Communications, 2021
Loss of UCHL1 rescues the defects related to Parkinson's disease by suppressing glycolysis.
Ham SJ et al.
Science Advances, 2021
Cross-over Loop Cysteine C152 Acts as an Antioxidant to Maintain the Folding Stability and Deubiquitinase Activity of UCH-L1 Under Oxidative Stress.
Puri S et al.
Journal of Molecular Biology, 2021
Ubiquitin recognition of BAP1: understanding its enzymatic function.
Hanpude P et al.
Bioscience Reports, 2017
Parkin-mediated K63-polyubiquitination targets ubiquitin C-terminal hydrolase L1 for degradation by the autophagy-lysosome system.
McKeon JE et al.
Cellular and Molecular Life Sciences : Cmls, 2015
Ubiquitin C-terminal hydrolase L1 (UCH-L1) acts as a novel potentiator of cyclin-dependent kinases to enhance cell proliferation independently of its hydrolase activity.
Kabuta T et al.
The Journal of Biological Chemistry, 2013
Recessive loss of function of the neuronal ubiquitin hydrolase UCHL1 leads to early-onset progressive neurodegeneration.
Bilguvar K et al.
Proceedings of the National Academy of Sciences of the United States of America, 2013
Parkinson's disease-associated mutations in α-synuclein and UCH-L1 inhibit the unconventional secretion of UCH-L1.
Konya C et al.
Neurochemistry International, 2011
Ubiquitin vinyl methyl ester binding orients the misaligned active site of the ubiquitin hydrolase UCHL1 into productive conformation.
Boudreaux DA et al.
Proceedings of the National Academy of Sciences of the United States of America, 2010
Regulation of synaptic structure by ubiquitin C-terminal hydrolase L1.
Cartier AE et al.
The Journal of Neuroscience : the Official Journal of the Society for Neuroscience, 2009
Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperone-mediated autophagy.
Kabuta T et al.
The Journal of Biological Chemistry, 2008
Insights into links between familial and sporadic Parkinson's disease: physical relationship between UCH-L1 variants and chaperone-mediated autophagy.
Kabuta T et al.
Autophagy, 2008
The S18Y polymorphic variant of UCH-L1 confers an antioxidant function to neuronal cells.
Kyratzi E et al.
Human Molecular Genetics, 2008
Aberrant molecular properties shared by familial Parkinson's disease-associated mutant UCH-L1 and carbonyl-modified UCH-L1.
Kabuta T et al.
Human Molecular Genetics, 2008
Reversible monoubiquitination regulates the Parkinson disease-associated ubiquitin hydrolase UCH-L1.
Meray RK et al.
The Journal of Biological Chemistry, 2007
Ubiquitin hydrolase Uch-L1 rescues beta-amyloid-induced decreases in synaptic function and contextual memory.
Gong B et al.
Cell, 2006
Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes monoubiquitin in neuron.
Osaka H et al.
Human Molecular Genetics, 2003
Alterations of structure and hydrolase activity of parkinsonism-associated human ubiquitin carboxyl-terminal hydrolase L1 variants.
Nishikawa K et al.
Biochemical and Biophysical Research Communications, 2003