Investigating the effect of VEGF glycosylation on glycosaminoglycan binding and protein unfolding
Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 340, Issue: 3, Page: 836-839
2006
- 31Citations
- 35Captures
Metric Options: Counts1 Year3 YearSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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.
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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
- Citations31
- Citation Indexes31
- 31
- CrossRef27
- Captures35
- Readers35
- 35
Article Description
VEGF 165 binding to endothelial cells is potentiated by glycosaminoglycans (GAGs). Here, we have investigated the impact of VEGF 165 N-glycosylation on GAG binding. Although glycosylated VEGF 165 bound to heparin with only slightly higher affinity than non-glycosylated VEGF 165, the natural ligand heparan sulfate induced a conformational change only in the glycosylated protein. Unfolding studies of the VEGF proteins indicated a stabilising effect of heparin on the growth factor structure.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006291X05028329; http://dx.doi.org/10.1016/j.bbrc.2005.12.079; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=30144438744&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/16386708; https://linkinghub.elsevier.com/retrieve/pii/S0006291X05028329; https://dx.doi.org/10.1016/j.bbrc.2005.12.079
Elsevier BV
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