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Hongmei Mo

Researcher at New York University

Publications -  10
Citations -  1563

Hongmei Mo is an academic researcher from New York University. The author has contributed to research in topics: Protease & Protease inhibitor (pharmacology). The author has an hindex of 9, co-authored 10 publications receiving 1557 citations. Previous affiliations of Hongmei Mo include Aaron Diamond AIDS Research Center.

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Ordered accumulation of mutations in HIV protease confers resistance to ritonavir.

TL;DR: Analysis of the HIV protease gene from the plasma of HIV–infected patients revealed substitutions at nine different codons selected in response to monotherapy with the protease inhibitors ritonavir, suggesting that dual protease inhibitor therapy might increase the duration of viral suppression.
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Selection and analysis of human immunodeficiency virus type 1 variants with increased resistance to ABT-538, a novel protease inhibitor.

TL;DR: In vitro selection of viral variants with decreased sensitivity to a symmetry-based protease inhibitor, ABT-538, currently being tested in clinical trials is reported, emphasizing the importance of closely monitoring patients receiving ABt-538 for the emergence of viral resistance.
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Characterization of human immunodeficiency virus type 1 variants with increased resistance to a C2-symmetric protease inhibitor.

TL;DR: In this article, a single amino acid substitution (Arg to Gln or Lys) at position 8 of the protease results in a substantial decrease in the inhibitory activity of the drug on the enzyme and a comparable increase in viral resistance.
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Expression Patterns of the HIV Type 1 Coreceptors CCR5 and CXCR4 on CD4+ T Cells and Monocytes from Cord and Adult Blood

TL;DR: The overall extent of CCR5 expression was reduced in cord blood, compared with adult blood, and IL-2 activation of CD4+ T cells from both cord and adult bloods caused a substantial increase in C CR5 expression, but moderately decreased CXCR4 expression.
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Human immunodeficiency virus type 1 mutants that escape neutralization by human monoclonal antibody IgG1b12. off.

TL;DR: The results suggest that escape from IgG1b12 neutralization is due to a local rather than a global modification of the gp120 structure, which has implications for the therapeutic and prophylactic applications of antibodies for HIV-1 infection.