{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T20:16:42Z","timestamp":1791231402906,"version":"4.1.0"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"2","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1990,1]]},"abstract":"<jats:p>The envelope (env) glycoprotein of human immunodeficiency virus type 1 (HIV-1) consists of two noncovalently associated subunits, gp120 and gp41, that are formed gradient sedimentation, polyacrylamide gel electrophoresis, gradient sedimentation, polyacrylamide gel electrophoresis, and chemical cross-linking, we show that gp160 is synthesized as a monomer and subsequently forms stable homodimers. The molecule remains dimeric after cleavage to gp120\/gp41 but is less stable to detergent solubilization and centrifugation. Analysis of wild-type and mutated env proteins indicated that interactions between the ectodomain regions of adjoining gp41 subunits are important for dimer formation and stability. A higher-order oligomeric form was also recovered, probably a tetramer consisting of two noncovalently associated dimers. The proposed subunit composition of the HIV-1 env protein is identical to that previously observed for the paramyxovirus envelope proteins F and HN.<\/jats:p>","DOI":"10.1073\/pnas.87.2.648","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T07:27:49Z","timestamp":1149060469000},"page":"648-652","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":278,"title":["Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein."],"prefix":"10.1073","volume":"87","author":[{"given":"P L","family":"Earl","sequence":"first","affiliation":[{"name":"Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R W","family":"Doms","sequence":"additional","affiliation":[{"name":"Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B","family":"Moss","sequence":"additional","affiliation":[{"name":"Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1990,1]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.87.2.648","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T13:13:57Z","timestamp":1649855637000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.87.2.648"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1990,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1990,1]]}},"alternative-id":["10.1073\/pnas.87.2.648"],"URL":"https:\/\/doi.org\/10.1073\/pnas.87.2.648","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1990,1]]},"assertion":[{"value":"1990-01-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}