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- W2120520610 abstract "The mature envelope glycoprotein (Env) spike on the surface of human immunodeficiency virus type 1 (HIV-1) virions is derived by proteolytic cleavage of a trimeric gp160 glycoprotein precursor. Remarkably, proteolytic processing of the HIV-1 Env precursor results in changes in Env antigenicity that resemble those associated with glutaraldehyde fixation. Apparently, proteolytic processing of the HIV-1 Env precursor decreases conformational flexibility of the Env trimeric complex, differentially affecting the integrity/accessibility of epitopes for neutralizing and nonneutralizing antibodies." @default.
- W2120520610 created "2016-06-24" @default.
- W2120520610 creator A5018901631 @default.
- W2120520610 creator A5071476197 @default.
- W2120520610 creator A5075224434 @default.
- W2120520610 date "2013-02-01" @default.
- W2120520610 modified "2023-10-16" @default.
- W2120520610 title "Proteolytic Processing of the Human Immunodeficiency Virus Envelope Glycoprotein Precursor Decreases Conformational Flexibility" @default.
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- W2120520610 doi "https://doi.org/10.1128/jvi.02765-12" @default.
- W2120520610 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3554131" @default.
- W2120520610 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23175369" @default.
- W2120520610 hasPublicationYear "2013" @default.
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