Heparin-binding domain of bovid herpesvirus 1 glycoprotein gIII
Archives of Virology, ISSN: 0304-8608, Vol: 134, Issue: 3-4, Page: 413-419
1994
- 24Citations
- 9Captures
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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
- Citations24
- Citation Indexes24
- 24
- CrossRef15
- Captures9
- Readers9
Article Description
Bovid herpesvirus 1 (BHV-1) glycoprotein gIII functions as a major virus attachment protein through binding to a heparinlike moiety on the host cells. To identify the functional domain, a panel of gIII deletion mutants was constructed, expressed in COS-7 cells, and examined for heparin-binding activity. Mutants with deletion of amino acid residues 103-173 and 324-443 bound to heparin as well as full-length gIII, whereas a mutant with residues 172-337 deleted showed no binding to heparin. In another mutant, with residues 172-211 deleted, the activity was reduced by one-third. These data suggest that the amino acid sequence between residues 172 and 323 contains the functional domain of BHV-1 gIII for heparin-binding and that especially the sequence between residues 212-323 includes a critical site for the activity. © 1994 Springer-Verlag.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0028139556&origin=inward; http://dx.doi.org/10.1007/bf01310578; http://www.ncbi.nlm.nih.gov/pubmed/8129625; http://link.springer.com/10.1007/BF01310578; https://dx.doi.org/10.1007/bf01310578; https://link.springer.com/article/10.1007/BF01310578; http://www.springerlink.com/index/10.1007/BF01310578; http://www.springerlink.com/index/pdf/10.1007/BF01310578
Springer Science and Business Media LLC
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