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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2010-5-3
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pubmed:abstractText |
UCH-L1 is a member of the family of ubiquitin C-terminal hydrolases whose primary role is to hydrolyze small C-terminal adducts of ubiquitin to generate free ubiquitin monomers. Expression of UCH-L1 is highly specific to neurons and point mutations in this enzyme are associated with a hereditary form of Parkinson's disease. Herein, we present the NMR backbone assignments of human UCH-L1, thus enabling future solution-state NMR spectroscopic studies on the structure and function of this important protein.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1874-270X
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
41-3
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pubmed:meshHeading |
pubmed-meshheading:20012716-Cysteine Endopeptidases,
pubmed-meshheading:20012716-Escherichia coli,
pubmed-meshheading:20012716-Humans,
pubmed-meshheading:20012716-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:20012716-Protein Structure, Secondary,
pubmed-meshheading:20012716-Recombinant Proteins,
pubmed-meshheading:20012716-Structural Homology, Protein,
pubmed-meshheading:20012716-Ubiquitin Thiolesterase
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pubmed:year |
2010
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pubmed:articleTitle |
Backbone assignments of the 26 kDa neuron-specific ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1).
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pubmed:affiliation |
Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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