Non-cleavage site gag mutations in amprenavir-resistant human immunodeficiency virus type 1 (HIV-1) predispose HIV-1 to rapid acquisition of amprenavir resistance but delay development of resistance to other protease inhibitors

Non-cleavage site gag mutations in amprenavir-resistant human immunodeficiency virus type 1 (HIV-1) predispose HIV-1 to rapid acquisition of amprenavir resistance but delay development of resistance to other protease inhibitors

Item
http://www.wikidata.org/entity/Q37127869
Deep sequencing of protease inhibitor resistant HIV patient isolates reveals patterns of correlated mutations in Gag and proteaseHIV-1 subtype influences susceptibility and response to monotherapy with the protease inhibitor lopinavir/ritonavir.Single genome sequencing of HIV-1 gag and protease resistance mutations at virologic failure during the OK04 trial of simplified versus standard maintenance therapyLoss of protease dimerization inhibition activity of darunavir is associated with the acquisition of resistance to darunavir by HIV-1.Loss of the protease dimerization inhibition activity of tipranavir (TPV) and its association with the acquisition of resistance to TPV by HIV-1.C-5-Modified Tetrahydropyrano-Tetrahydofuran-Derived Protease Inhibitors (PIs) Exert Potent Inhibition of the Replication of HIV-1 Variants Highly Resistant to Various PIs, including DarunavirPositive selection pressure introduces secondary mutations at Gag cleavage sites in human immunodeficiency virus type 1 harboring major protease resistance mutationsHuman Immunodeficiency Virus Gag and protease: partners in resistance.Gag-Protease Sequence Evolution Following Protease Inhibitor Monotherapy Treatment Failure in HIV-1 Viruses Circulating in East Africa.Phenotypic characterization of virological failure following lopinavir/ritonavir monotherapy using full-length Gag-protease genesA novel central nervous system-penetrating protease inhibitor overcomes human immunodeficiency virus 1 resistance with unprecedented aM to pM potency.GRL-079, a novel P2-Tp-THF-C5-alkylamine- and P2' -Abt-containing HIV-1 protease inhibitor, is extremely potent against multi-drug-resistant HIV-1 variants including HIVDRVRp51 and has a high genetic barrier against the emergence of resistant varianMechanism of Darunavir (DRV)'s High Genetic Barrier to HIV-1 Resistance: A Key V32I Substitution in Protease Rarely Occurs, but Once It Occurs, It Predisposes HIV-1 To Develop DRV Resistance.Characterization of HIV-1 from patients with virological failure to a boosted protease inhibitor regimen.
P2860

Non-cleavage site gag mutations in amprenavir-resistant human immunodeficiency virus type 1 (HIV-1) predispose HIV-1 to rapid acquisition of amprenavir resistance but delay development of resistance to other protease inhibitors

Item
http://www.wikidata.org/entity/Q37127869
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 28 January 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Non-cleavage site gag mutation ...... e to other protease inhibitors
@en
Non-cleavage site gag mutation ...... immunodeficiency virus type 1
@nl
type
label
Non-cleavage site gag mutation ...... e to other protease inhibitors
@en
Non-cleavage site gag mutation ...... immunodeficiency virus type 1
@nl
prefLabel
Non-cleavage site gag mutation ...... e to other protease inhibitors
@en
Non-cleavage site gag mutation ...... immunodeficiency virus type 1
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
Non-cleavage site gag mutation ...... e to other protease inhibitors
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932