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Full-Text Articles in Molecular Biology
Elucidating Structure, Function, And Small Molecular Interactions Of Human Immunodeficiency Virus And Chikungunya Virus, Kristin Nicole Slater
Elucidating Structure, Function, And Small Molecular Interactions Of Human Immunodeficiency Virus And Chikungunya Virus, Kristin Nicole Slater
Wayne State University Theses
Abstract HIV-1:
Human immunodeficiency virus-1 (HIV-1) is a widespread, incurable retrovirus known to cause
immunodeficiency and a shortened life span. Despite successful treatment methods, HIV-1
frequently mutates, resulting in antiviral resistance. Many therapies target the HIV-1 protease
(PR), which is responsible for cleaving the viral polyprotein essential for its life cycle. HIV-1 PR
often evades treatment by way of mutations and less commonly through residue insertions. We
have identified a clinical isolate with a five residue insertion between residues 28 and 29.
Through molecular dynamics simulations we analyzed the protease protein structure and
determined that the residue insertion created a …
Biochemical, Structural, And Drug Design Studies Of Multi-Drug Resistant Hiv-1 Therapeutic Targets, Tamaria Grace Dewdney
Biochemical, Structural, And Drug Design Studies Of Multi-Drug Resistant Hiv-1 Therapeutic Targets, Tamaria Grace Dewdney
Wayne State University Dissertations
Protein point mutations acquired as a mechanism of survival against therapeutics cause structural changes that effect protein function and inhibitor binding. This work investigates the structural mechanisms that lead to multi-drug resistance to HIV-1 protease and integrase inhibitors.
Proper proteolytic processing of the HIV-1 Gag/Pol polyprotein is required for HIV infection and viral replication. This feature has made HIV-1 protease an attractive target for antiretroviral drug design for the treatment of HIV-1 infected patients, thus the development of drug resistance has arisen as a major therapeutic and drug design challenge. To understand the molecular mechanisms leading to drug resistance we …