The DOI matches its Crossref record; 107 of the 107 references it cites were found in a registry or an index.
Ubiquitin C-terminal hydrolase L1 (UCH-L1): structure, distribution and roles in brain function and dysfunction
Open accessAbstract
Ubiquitin C-terminal hydrolase L1 (UCH-L1) is an extremely abundant protein in the brain where, remarkably, it is estimated to make up 1–5% of total neuronal protein. Although it comprises only 223 amino acids it has one of the most complicated 3D knotted structures yet discovered. Beyond its expression in neurons UCH-L1 has only very limited expression in other healthy tissues but it is highly expressed in several forms of cancer. Although UCH-L1 is classed as a deubiquitinating enzyme (DUB) the direct functions of UCH-L1 remain enigmatic and a wide array of alternative functions has been proposed. UCH-L1 is not essential for neuronal development but it is absolutely required for the maintenance of axonal integrity and UCH-L1 dysfunction is implicated in neurodegenerative disease. Here we review the properties of UCH-L1, and how understanding its complex structure can provide new insights into its roles in neuronal function and pathology.
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Cites
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Butterfield, D. A., & Boyd‐Kimball, D. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14589 · Cited by 105
Kooij, R., Liu, S., Sapmaz, A., Xin, B.-T., Janssen, G. M. C., van Veelen, P. A., Ovaa, H., Dijke, P. T., & Geurink, P. P. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c07726 · Cited by 82
Metadata
- Authors
- Bishop, P., Rocca, D., & Henley, J. M.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2016-08-11
- Volume
- 473
- Issue
- 16
- Pages
- 2453-2462
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2515462226
- Cited by
- 305
- References
- 107
- FWCI
- 8.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Bishop, P., Rocca, D., & Henley, J. M. (2016). Ubiquitin C-terminal hydrolase L1 (UCH-L1): structure, distribution and roles in brain function and dysfunction. Biochemical Journal. https://doi.org/10.1042/bcj20160082
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
