Phosphorylation of Recombinant N -Syndecan (Syndecan 3) Core Protein
Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 240, Issue: 2, Page: 502-506
1997
- 22Citations
- 4Captures
- 3Mentions
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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
- Citations22
- Citation Indexes22
- 22
- CrossRef17
- Captures4
- Readers4
- Mentions3
- References3
- Wikipedia3
Article Description
The cytoplasmic domain of the syndecan family of heparan sulfate proteoglycans is punctuated by the presence of four regularly spaced tyrosine residues. In this report, we explore the possibility of whether the four tyrosine residues in the cytoplasmic domain of N-syndecan (Syndecan 3) are potential substrates for phosphorylation by a tyrosine kinase. Bacterially expressed elk kinase was used to phosphorylate a series of bacterially expressed N-syndecan fusion proteins. Our results clearly demonstrate that the tyrosine residues in the cytoplasmic domain of N-syndecan can be phosphorylated by a tyrosine-specific kinase, and that all four tyrosine residues are capable of being phosphorylated.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006291X97976841; http://dx.doi.org/10.1006/bbrc.1997.7684; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0031576407&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9388509; https://linkinghub.elsevier.com/retrieve/pii/S0006291X97976841; https://dx.doi.org/10.1006/bbrc.1997.7684
Elsevier BV
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