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Article: Backbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1
| Title | Backbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1 | ||||
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| Authors | |||||
| Keywords | NMR spectroscopy Parkinson's disease Resonance assignment Ubiquitin Ubiquitin carboxy-terminal hydrolase L1 | ||||
| Issue Date | 2011 | ||||
| Publisher | Springer Netherlands. The Journal's web site is located at http://www.springer.com/physics/biophysics/journal/12104 | ||||
| Citation | Biomolecular Nmr Assignments, 2011, v. 5 n. 2, p. 165-168 How to Cite? | ||||
| Abstract | Ubiquitin carboxy-terminal hydrolase L1 (UCH-L1), also known as PGP9.5, is a protein of 223 amino acids. Although it was originally characterized as a deubiquitinating enzyme, recent studies indicate that it also functions as a ubiquitin (Ub) ligase and a mono-Ub stabilizer. It is highly abundant in brain, constituting up to 2% of total brain proteins. Down-regulation and extensive oxidative modification of UCH-L1 have been observed in the brains of Alzheimer's disease (AD) and Parkinson's disease (PD) patients. Mutations in the UCH-L1 gene have been reported to be linked to Parkinson's disease, in particular, the I93 M variant is associated with a higher susceptibility of PD in contrast to a higher protection against PD for the S18Y variant. Hence, the structure of UCH-L1 and the underlying effects of disease associated mutations on the structure and function of UCH-L1 are of considerable interest. Here, we report the NMR spectral assignments of the S18Y human UCH-L1 mutant with the aim to obtain better understanding about the risk of Parkinson's disease against structural and dynamical changes induced by this mutation on UCH-L1. © 2011 The Author(s). | ||||
| Persistent Identifier | http://hdl.handle.net/10722/144868 | ||||
| ISSN | 2021 Impact Factor: 0.731 2020 SCImago Journal Rankings: 0.359 | ||||
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| ISI Accession Number ID |
Funding Information: This work was supported by the Research Grants Council of Hong Kong (GRF 7755/08 M, 7765/09 M) | ||||
| References | Naito S, Mochizuki H, Yasuda T et al (2006) Characterization of multimetric variants of ubiquitin carboxyl-terminal hydrolase L1 in water by small-angle neutron scattering. Biochem Biophys Res Commun 339:717–725 doi: 10.1016/j.bbrc.2005.11.066 Osaka H, Wang YL, Takada K et al (2003) Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes monoubiquitin in neuron. Hum Mol Genet 12:1945–1958 doi: 10.1093/hmg/ddg211 Wishart DS, Sykes BD (1994) The13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180 doi: 10.1007/BF00175245 |
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Tse, HS | en_HK |
| dc.contributor.author | Hu, HY | en_HK |
| dc.contributor.author | Sze, KH | en_HK |
| dc.date.accessioned | 2012-02-21T05:44:38Z | - |
| dc.date.available | 2012-02-21T05:44:38Z | - |
| dc.date.issued | 2011 | en_HK |
| dc.identifier.citation | Biomolecular Nmr Assignments, 2011, v. 5 n. 2, p. 165-168 | en_HK |
| dc.identifier.issn | 1874-2718 | en_HK |
| dc.identifier.uri | http://hdl.handle.net/10722/144868 | - |
| dc.description.abstract | Ubiquitin carboxy-terminal hydrolase L1 (UCH-L1), also known as PGP9.5, is a protein of 223 amino acids. Although it was originally characterized as a deubiquitinating enzyme, recent studies indicate that it also functions as a ubiquitin (Ub) ligase and a mono-Ub stabilizer. It is highly abundant in brain, constituting up to 2% of total brain proteins. Down-regulation and extensive oxidative modification of UCH-L1 have been observed in the brains of Alzheimer's disease (AD) and Parkinson's disease (PD) patients. Mutations in the UCH-L1 gene have been reported to be linked to Parkinson's disease, in particular, the I93 M variant is associated with a higher susceptibility of PD in contrast to a higher protection against PD for the S18Y variant. Hence, the structure of UCH-L1 and the underlying effects of disease associated mutations on the structure and function of UCH-L1 are of considerable interest. Here, we report the NMR spectral assignments of the S18Y human UCH-L1 mutant with the aim to obtain better understanding about the risk of Parkinson's disease against structural and dynamical changes induced by this mutation on UCH-L1. © 2011 The Author(s). | en_HK |
| dc.language | eng | en_US |
| dc.publisher | Springer Netherlands. The Journal's web site is located at http://www.springer.com/physics/biophysics/journal/12104 | en_HK |
| dc.relation.ispartof | Biomolecular NMR Assignments | en_HK |
| dc.rights | The Author(s) | en_US |
| dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | en_US |
| dc.subject | NMR spectroscopy | en_HK |
| dc.subject | Parkinson's disease | en_HK |
| dc.subject | Resonance assignment | en_HK |
| dc.subject | Ubiquitin | en_HK |
| dc.subject | Ubiquitin carboxy-terminal hydrolase L1 | en_HK |
| dc.title | Backbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1 | en_HK |
| dc.type | Article | en_HK |
| dc.identifier.openurl | http://library.hku.hk:4551/resserv?sid=springerlink&genre=article&atitle=Backbone and side-chain <sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1&title=Biomolecular NMR Assignments&issn=18742718&date=2011-10-01&volume=5&issue=2& spage=165&authors=Ho-Sum Tse, Hong-Yu Hu, Kong-Hung Sze | en_US |
| dc.identifier.email | Sze, KH:khsze@hku.hk | en_HK |
| dc.identifier.authority | Sze, KH=rp00785 | en_HK |
| dc.description.nature | published_or_final_version | en_US |
| dc.identifier.doi | 10.1007/s12104-011-9292-7 | en_HK |
| dc.identifier.pmid | 21298373 | - |
| dc.identifier.pmcid | PMC3166605 | - |
| dc.identifier.scopus | eid_2-s2.0-84855371939 | en_HK |
| dc.relation.references | Das C, Hoang QQ, Kreinbring CA, Luchansky SJ, Meray RK, Ray SS, Lansbury PT, Ringe D, Petsko GA (2006) Structural basis for conformational plasticity of the Parkinson’s disease-associated ubiquitin hydrolase UCH-L1. Proc Natl Acad Sci USA 103:4675–4680 | en_US |
| dc.relation.references | Leroy E, Boyer R, Auburger G, Leube B, Ulm G, Mezey E et al (1998) The ubiquitin pathway in Parkinson’s disease. Nature 395:451–452 | en_US |
| dc.relation.references | Naito S, Mochizuki H, Yasuda T et al (2006) Characterization of multimetric variants of ubiquitin carboxyl-terminal hydrolase L1 in water by small-angle neutron scattering. Biochem Biophys Res Commun 339:717–725 | en_US |
| dc.relation.references | doi: 10.1016/j.bbrc.2005.11.066 | en_US |
| dc.relation.references | Osaka H, Wang YL, Takada K et al (2003) Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes monoubiquitin in neuron. Hum Mol Genet 12:1945–1958 | en_US |
| dc.relation.references | doi: 10.1093/hmg/ddg211 | en_US |
| dc.relation.references | Wilkinson KD, Lee KM, Deshpande S, Duerksen-Hughes P, Boss JM, Pohl J (1989) The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase. Science 246:670–673 | en_US |
| dc.relation.references | Wishart DS, Sykes BD (1994) The13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180 | en_US |
| dc.relation.references | doi: 10.1007/BF00175245 | en_US |
| dc.relation.references | Goddard TD, Kneller DG (1993) SPARKY 3. University of California, San Francisco | en_US |
| dc.relation.references | Hibi K, Liu Q, Beaudry GA et al (1998) Serial analysis of gene expression in non-small cell lung cancer. Cancer Res 58:5690–5694 | en_US |
| dc.relation.references | Liu Y, Fallon L, Lashuel HA, Liu Z, Lansbury PT Jr (2002) The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson’s disease susceptibility. Cell 111:209–18 | en_US |
| dc.relation.references | Maraganore DM, Farrer MJ, Hardy JA, McDonnell SK, Lincoln SJ, Rocca WA (1999) Case-control study of the ubiquitin carboxy-terminal hydrolase L1 gene in Parkinson’s disease. Neurology 53:1858–1860 | en_US |
| dc.identifier.volume | 5 | en_US |
| dc.identifier.issue | 2 | en_US |
| dc.identifier.spage | 165 | en_HK |
| dc.identifier.epage | 168 | en_HK |
| dc.identifier.eissn | 1874-270X | en_US |
| dc.identifier.isi | WOS:000294559700010 | - |
| dc.publisher.place | Netherlands | en_HK |
| dc.description.other | Springer Open Choice, 21 Feb 2012 | en_US |
| dc.identifier.scopusauthorid | Tse, HS=36919182700 | en_HK |
| dc.identifier.scopusauthorid | Hu, HY=24344153500 | en_HK |
| dc.identifier.scopusauthorid | Sze, KH=7006735061 | en_HK |
| dc.identifier.citeulike | 8788812 | - |
| dc.identifier.issnl | 1874-270X | - |