2002
DOI: 10.1099/0022-1317-83-9-2225
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Human immunodeficiency virus type 1 Vif binds the viral protease by interaction with its N-terminal region

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Cited by 13 publications
(11 citation statements)
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“…69 Other studies involved the Vif and protease proteins of HIV-1 that have been shown to interact with each other. 70 A peptide derived from the N-terminus of protease seems to block that interaction and consequently inhibit HIV-1 replication in restrictive cells. 71 It yet has to be seen if these peptides and similar will have antagonistic effects when expressed inside the cell.…”
Section: Prospectsmentioning
confidence: 99%
“…69 Other studies involved the Vif and protease proteins of HIV-1 that have been shown to interact with each other. 70 A peptide derived from the N-terminus of protease seems to block that interaction and consequently inhibit HIV-1 replication in restrictive cells. 71 It yet has to be seen if these peptides and similar will have antagonistic effects when expressed inside the cell.…”
Section: Prospectsmentioning
confidence: 99%
“…Accumulated evidence suggests that Vif selectively inhibits protease-mediated proteolytic processing at specific cleavage sites (e.g., matrix Խ capsid [518] and SP1 Խ NC [307]). Although it remains debated, the Vif-protease interaction is speculated to inhibit the protease digestion of cellular cofactors (516,519).…”
Section: Protease-vif Interactionmentioning
confidence: 99%
“…Regarding the interaction domains, the N-terminal domain of protease (positions 1 to 9 [516,517]) may interact with the central domain of Vif (positions 78 to 98 [516,519]). Of interest, Vifderived peptides (positions 21 to 65 [520], 30 to 65 [519], 81 to 88 [521], 78 to 98 [519], and 88 to 98 [521]) may efficiently inhibit HIV-1 protease activity.…”
Section: Protease-vif Interactionmentioning
confidence: 99%
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