Post-translational modifications in the survival motor neuron protein
Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 324, Issue: 1, Page: 288-293
2004
- 9Citations
- 30Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations9
- Citation Indexes9
- CrossRef6
- Captures30
- Readers30
- 30
Article Description
Spinal muscular atrophy (SMA) is an autosomal recessive disease characterized by a progressive loss of the spinal motoneurons. The SMA-determining gene has been termed survival motor neuron (SMN) and is deleted or mutated in over 98% of patients. The encoded gene product is a protein expressed as different isoforms. In particular, we showed that the rat SMN cDNA produces two isoforms with M r of 32 and 35 kDa, both localized in nuclear coiled bodies, but the 32 kDa form is also cytoplasmic, whereas the 35 kDa form is also microsomal. To determine the molecular relationship between these two isoforms and potential post-translational modifications, we performed transfection experiments with a double-tagged rat SMN. Immunoblot and immunostaining studies demonstrated that the 32 kDa SMN isoform derives from the full length 35 kDa, through a proteolytic cleavage at the C-terminal. Furthermore, the 35 kDa SMN isoform is physiologically phosphorylated in vivo. This may modulate its interaction with molecular partners, either proteins or nucleic acids.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006291X0402042X; http://dx.doi.org/10.1016/j.bbrc.2004.09.057; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=4744340679&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/15465016; https://linkinghub.elsevier.com/retrieve/pii/S0006291X0402042X; https://dx.doi.org/10.1016/j.bbrc.2004.09.057
Elsevier BV
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