1982
DOI: 10.1016/s0021-9258(19)45337-4
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Glycosylation and intracellular transport of membrane glycoproteins encoded by murine leukemia viruses. Inhibition by amino acid analogues and by tunicamycin.

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Cited by 65 publications
(1 citation statement)
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“…HIV-1 varies dramatically within a clade and within infected individuals. HIV Env gp120 is among the most heavily glycosylated proteins in nature (Myers et al, 1992), far more heavily glycosylated than envelopes of other retroviruses of similar size (e.g., HTLV-1, MuLV) (Polonoff et al, 1982). The influence of sequon variation on HIV antibody recognition and viral phenotype has been studied in the context of HIV and SIV Env proteins (Chackerian et Sigvard Olofsson and colleagues first showed that glycosylation of gp120 could change exposure of neutralizing antibody epitopes (Bolmstedt et al, 1996).…”
Section: Genome Maps Of Crf12 Crf28 Crf29 and Other Bf Recombinantsmentioning
confidence: 99%
“…HIV-1 varies dramatically within a clade and within infected individuals. HIV Env gp120 is among the most heavily glycosylated proteins in nature (Myers et al, 1992), far more heavily glycosylated than envelopes of other retroviruses of similar size (e.g., HTLV-1, MuLV) (Polonoff et al, 1982). The influence of sequon variation on HIV antibody recognition and viral phenotype has been studied in the context of HIV and SIV Env proteins (Chackerian et Sigvard Olofsson and colleagues first showed that glycosylation of gp120 could change exposure of neutralizing antibody epitopes (Bolmstedt et al, 1996).…”
Section: Genome Maps Of Crf12 Crf28 Crf29 and Other Bf Recombinantsmentioning
confidence: 99%