Introduction: Additional mutations have been reported (L74M, E92Q, E138K, G140S/A and G163R).
Introduction: Other mutations reported for elvitegravir are H51Y, T66I, Q95K, E138K, Q146P, S147G and E157Q.
Resistance mutations in human immunodeficiency virus type 1 integrase selected with elvitegravir confer reduced susceptibility to a wide range of integrase inhibitors.
Abstract: In addition, mutations that do not confer reduced susceptibility when present alone (H114Y, L74M, R20K, A128T, E138K, and S230R) are also discussed in relation to their position in the catalytic core domain and their proximity to known structural features of integrase.
Binding modes of two novel non-nucleoside reverse transcriptase inhibitors, YM-215389 and YM-228855, to HIV type-1 reverse transcriptase.
Abstract: A single amino acid substitution confers only moderate resistance to YM-215389; indeed, four amino acid substitutions (V106L, V108I, E138K and L214F) were necessary for high-level resistance.
[Resistance to integrase inhibitors].
PMID: 19572425
2008
Enfermedades infecciosas y microbiologia clinica
Abstract: The most common resistance pattern seems to be E138K + E147G + Q148R.
Abstract: The most frequently observed mutations in failure with elvitegravir are E92Q, E138K, Q148R/K/H and N155H, and less frequently S147G and T66A/I/K.
Natural polymorphism of the HIV-1 integrase gene and mutations associated with integrase inhibitor resistance.
Abstract: Of the 42 aa substitutions currently associated with INI resistance, 21 occurred as natural polymorphisms: V72I, L74I, T97A, T112I, A128T, E138K, Q148H, V151I, S153Y/A, M154I, N155H, K156N, E157Q, G163R, V165I, V201I, I203M, T206S, S230N and R263K.
In vitro selection of mutations in human immunodeficiency virus type 1 reverse transcriptase that confer resistance to capravirine, a novel nonnucleoside reverse transcriptase inhibitor.
Abstract: Compound 3 does not select for the TSAO-specific E138K mutation in the RT.
Abstract: However, the compound markedly lost its antiviral potential against a variety of virus strains that contain NNRTI-characteristic mutations in RT including E138K.
Structural insights into mechanisms of non-nucleoside drug resistance for HIV-1 reverse transcriptases mutated at codons 101 or 138.
Abstract: Both RT(Glu138Lys) and RT(Lys101Glu) have remarkably similar protein conformations to wild-type RT, except for significant movement of the mutated side-chains away from the NNRTI pocket induced by charge inversion.
Abstract: We have determined crystal structures of RT(Glu138Lys) and RT(Lys101Glu) in complexes with nevirapine to 2.5 A, allowing the determination of water structure within the NNRTI-binding pocket, essential for an understanding of nevirapine binding.
Mechanism of action and resistant profile of anti-HIV-1 coumarin derivatives.
Abstract: An E138K mutation in the non-nucleoside RT inhibitors (NNRTIs) binding pocket of HIV-1 RT confers resistance to DCK and its chromone derivative, DCP8.
Abstract: However, the DCK-escape virus carrying the E138K mutation remains resistant to DCP8.
Abstract: Our results indicate that a single amino acid mutation, E138K in HIV-1 RT, is sufficient to confer DCK resistance.
Genetic analyses of DNA-binding mutants in the catalytic core domain of human immunodeficiency virus type 1 integrase.
HIV mutation literature information.
PMID: 
2008
Biochemistry
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