Purification and characterization of GP90, one of the envelope glycoproteins of respiratory syncytial virus

Clicks: 418
ID: 116657
1984
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Popular

Ranked #7 of 14 articles by views in the journal of general virology

Most read Least read

Bar heights use a square-root scale.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Abstract
The large glycoprotein, GP90, of respiratory syncytial virus (RSV) was purified by affinity chromatography using a monoclonal antibody. Hyperimmune rabbit antiserum directed specifically to the purified GP90 neutralized RSV to high titre but did not inhibit fusion of previously infected cells. 125I- …
Reference Key
ee1984thepurification Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Walsh EE;Schlesinger JJ;Brandriss MW;;
Journal the journal of general virology
Year 1984
DOI
DOI not found
URL
Keywords

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

No comments yet. Be the first to comment on this article.