Targeting RNA-protein interactions within the human immunodeficiency virus type 1 lifecycle

• Main Authors: Bell, N.M, L'Hernault, A, Murat, P, Richards, J.E, Lever, A.M.L, Balasubramanian, S
• Other Authors: MEDICINE
• Format: Article
• Published: American Chemical Society 2020
• Subjects: Diseases; Genes; Life cycle; Molecules; Proteins; Viruses; H NMR spectroscopy; Human immunodeficiency virus type-1; Inhibitory activity; RNA-protein interactions; Structural elements; Structural proteins; Therapeutic targets; Viral replication; RNA; Gag protein; structural protein; virus protein; virus RNA; anti human immunodeficiency virus agent; molecular library; NSC-260594; quinoline derivative; ribonucleoprotein; Schiff base; spliced leader RNA; NSC 260594; 5' untranslated region; article; controlled study; human; human cell; Human immunodeficiency virus 1; in vitro study; life cycle stage; molecule; nonhuman; priority journal; protein expression; protein RNA binding; proton nuclear magnetic resonance; virus genome; virus infectivity; virus particle; virus replication; antagonists and inhibitors; binding site; cell survival; chemical structure; chemistry; conformation; DNA denaturation; drug effects; drug screening; HEK293 cell line; HeLa cell line; HIV Infections; metabolism; molecularly targeted therapy; osmolarity; physiology; cell strain HEK293; drug antagonism; drug effect; HeLa cell; Human immunodeficiency virus infection; Anti-HIV Agents; Binding Sites; Cell Survival; Drug Evaluation, Preclinical; gag Gene Products, Human Immunodeficiency Virus; HEK293 Cells; HeLa Cells; HIV-1; Humans; Models, Molecular; Molecular Targeted Therapy; Nucleic Acid Conformation; Nucleic Acid Denaturation; Osmolar Concentration; Quinolinium Compounds; Ribonucleoproteins; RNA, Spliced Leader; RNA, Viral; Schiff Bases; Small Molecule Libraries; Virus Replication
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/183903
• Institution: National University of Singapore

10.1021/bi401270d