Structural and Functional Analysis of the N-Terminal Extracellular Region of β-Dystroglycan
Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 266, Issue: 1, Page: 274-278
1999
- 38Citations
- 14Captures
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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
- Citations38
- Citation Indexes38
- 38
- CrossRef32
- Captures14
- Readers14
- 14
Article Description
A protein fragment corresponding to the mouse β-dystroglycan N-terminal extracellular region from position 654 to 750, β-DG(654–750) was recombinantly expressed in BL21(DE3) Escherichia coli cells. Secondary structure prediction of the protein fragment reveals about 70% of random coil, as confirmed by circular dichroism analysis. Moreover, fluorescence analysis shows that the tryptophan residue in position 659 lays in a solvent-exposed fashion. These data suggest that the β-DG(654–750) is likely to have a quite flexible structure and to be only partially folded. Interestingly, the protein still retains its biological function since using solid-phase assays we have detected binding of biotinylated β-DG(654–750) both to native α-dystroglycan and to a recombinant fragment which spans the C-terminal region of α-dystroglycan.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006291X9991803X; http://dx.doi.org/10.1006/bbrc.1999.1803; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0033539929&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/10581202; https://linkinghub.elsevier.com/retrieve/pii/S0006291X9991803X; https://dx.doi.org/10.1006/bbrc.1999.1803
Elsevier BV
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