ArticleNeurochemical research2001
Implication of the extracellular disulfide bond on myelin protein zero expression.
Article in Neurochemical research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- NADPH oxidase-4 maintains neuropathic pain after peripheral nerve injury.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Tissue distribution of quiescin Q6/sulfhydryl oxidase (QSOX) in developing mouse.Journal of molecular histology · 2008Article
- Myelin P0: new knowledge and new roles.Neurochemical research · 2002Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations in myelin protein zero (P0) are responsible for several peripheral neuropathies. We studied transport and membrane integration of the truncated P0 mutants using transfected oligodendroglial cell line (Oln93). Starting with rat cDNA, we produced two P0 deletions. The first, called P0-Tyr contains a 66 amino acid deletion in the extracellular domain and a tyrosine at the new position 32. In the second, called P0-Cys, the tyrosine 32 is replaced by a cysteine. This replacement restores a disulfide bond in the extracellular domain. Our results show that P0 proteins, truncated or not, were expressed in the plasma membrane of the transfected cells. Transcription rates of both mutants were normal. However, P0-Tyr was detected in only 3-5% of the cells compared to the P0-Cys and the wild type. Thus, the disulfide bond in the extracellular domain is important for stability and correct addressing of the P0 protein.
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