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1. Full Text Structure of the CCR5 Chemokine Receptor—HIV Entry Inhibitor Maraviroc Complex
by Qiuxiang Tan and Ya Zhu and Jian Li and Zhuxi Chen and Gye Won Han and Irina Kufareva and Tingting Li and Limin Ma and Gustavo Fenalti and Jing Li and Wenru Zhang and Xin Xie and Huaiyu Yang and Hualiang Jiang and Vadim Cherezov and Hong Liu and Raymond C. Stevens and Qiang Zhao and Beili Wu and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Science, ISSN 0036-8075, 9/2013, Volume 341, Issue 6152, pp. 1387 - 1390
The CCR5 chemokine receptor acts as a co-receptor for HIV-1 viral entry. Here we report the 2.7 angstrom-resolution crystal structure of human CCR5 bound to... 
Receptors | REPORTS | Ligands | Viruses | Viral morphology | Infections | Grants | Carbon | Chemokines | HIV 1 | Crystal structure | V3 LOOP | TERMINUS | CORECEPTOR | ANTAGONIST | PROTEIN-COUPLED RECEPTOR | SMALL-MOLECULE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ANTIBODY | BINDING | DISCOVERY | HIV-1 - drug effects | Triazoles - chemistry | Cyclohexanes - pharmacology | HIV Fusion Inhibitors - chemistry | Humans | HIV Fusion Inhibitors - pharmacology | Virus Internalization - drug effects | HIV Envelope Protein gp120 - metabolism | Triazoles - pharmacology | Receptors, CCR5 - metabolism | HIV-1 - physiology | Maraviroc | Receptors, CCR5 - chemistry | Cyclohexanes - chemistry | Protein Conformation | Binding Sites | Receptors, CXCR4 - chemistry | Research | Properties | Chemokine receptors | Chemical structure | Neurons | Human immunodeficiency virus--HIV
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2. Full Text HIV-1 antiretroviral drug therapy
by Arts, Eric J and Hazuda, Daria J
Cold Spring Harbor Perspectives in Medicine, ISSN 2157-1422, 2012, Volume 2, Issue 4, pp. a007161 - a007161
The most significant advance in the medical management of HIV-1 infection has been the treatment of patients with antiviral drugs, which can suppress HIV-1... 
IN-VIVO EMERGENCE | MEDICINE, RESEARCH & EXPERIMENTAL | DEPENDENT PRIMER UNBLOCKING | REVERSE-TRANSCRIPTASE INHIBITORS | CORECEPTOR-BINDING-SITE | SMALL-MOLECULE | IMMUNODEFICIENCY-VIRUS TYPE-1 | ZIDOVUDINE RESISTANCE MUTATIONS | HIGH-LEVEL RESISTANCE | INTEGRASE INHIBITORS | PROTEASE INHIBITORS | Anti-HIV Agents - pharmacology | HIV Integrase Inhibitors - pharmacology | Virus Replication - drug effects | Humans | Drug Resistance, Viral | Reverse Transcriptase Inhibitors - pharmacology | HIV Fusion Inhibitors - pharmacology | HIV Protease Inhibitors - therapeutic use | HIV Fusion Inhibitors - therapeutic use | HIV Protease Inhibitors - pharmacology | HIV-1 - physiology | HIV Integrase Inhibitors - therapeutic use | Anti-HIV Agents - therapeutic use | HIV Infections - drug therapy | Reverse Transcriptase Inhibitors - therapeutic use | CCR5 Receptor Antagonists | 064
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3. Full Text Inhibition of HIV Fusion with Multivalent Gold Nanoparticles
by Bowman, Mary-Catherine and Ballard, T. Eric and Ackerson, Christopher J and Feldheim, Daniel L and Margolis, David M and Melander, Christian
Journal of the American Chemical Society, ISSN 0002-7863, 06/2008, Volume 130, Issue 22, pp. 6896 - 6897
The design and synthesis of a multivalent gold nanoparticle therapeutic is presented. SDC-1721, a fragment of the potent HIV inhibitor TAK-779, was synthesized... 
IMMUNODEFICIENCY-VIRUS TYPE-1 | ANTIBODY | ENTRY | SMALL-MOLECULE | CHEMISTRY, MULTIDISCIPLINARY | NONPEPTIDE CCR5 ANTAGONIST | Amides - pharmacology | Gold - chemistry | HIV-1 - physiology | HIV Fusion Inhibitors - chemistry | Metal Nanoparticles - chemistry | Metal Nanoparticles - therapeutic use | Amides - chemistry | HIV Infections - drug therapy | Gold - pharmacology | HIV Fusion Inhibitors - pharmacology | Quaternary Ammonium Compounds - chemistry | Quaternary Ammonium Compounds - pharmacology | Nanoparticles | Gold | Ligand binding (Biochemistry) | Analysis | Atomic properties | Research | Chemical properties | HIV (Viruses)
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4. Full Text Enfuvirtide (T20)-based lipopeptide is a potent HIV-1 cell fusion inhibitor: Implications for viral entry and inhibition
by Ding, Xiaohui and Zhang, Xiujuan and Chong, Huihui and Zhu, Yuanmei and Wei, Huamian and Wu, Xiyuan and He, Jinsheng and Wang, Xinquan and He, Yuxian
Journal of Virology, ISSN 0022-538X, 09/2017, Volume 91, Issue 18
The peptide drug enfuvirtide (T20) is the only viral fusion inhibitor used in combination therapy for HIV-1 infection, but it has relatively low antiviral... 
HIV-1 | T20 | Lipopeptide | Gp41 | Fusion inhibitor | ENVELOPE GLYCOPROTEIN | T HOOK STRUCTURE | MEMBRANE-FUSION | HEPTAD-REPEAT | ATOMIC-STRUCTURE | fusion inhibitor | VIROLOGY | lipopeptide | gp41 | GP41 CORE STRUCTURE | IMMUNODEFICIENCY-VIRUS TYPE-1 | RESISTANT HIV-1 | DRUG TARGET | COILED-COIL | HIV Envelope Protein gp41 - pharmacology | Lipopeptides - pharmacology | HIV Fusion Inhibitors - chemistry | HIV Fusion Inhibitors - isolation & purification | Lipopeptides - isolation & purification | Protein Binding | Crystallography, X-Ray | Peptide Fragments - pharmacology | Lipopeptides - chemistry | HIV Fusion Inhibitors - pharmacology | Virus Internalization - drug effects | HIV - drug effects
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5. Full Text Pyrroloaryls and pyrroloheteroaryls: Inhibitors of the HIV fusion/attachment, reverse transcriptase and integrase
by Patel, Rahul V and Park, Se Won
Bioorganic & Medicinal Chemistry, ISSN 0968-0896, 09/2015, Volume 23, Issue 17, pp. 5247 - 5263
Heterocyclic compounds execute a very important role in drug design and discovery. This article provides the basic milestones of the research for pyrroloaryl... 
Pyrrolopyrimidines | Pyrroloquinolines | Reverse transcriptase | Arylthiopyrrole | Pyrrole | Triciribine | HIV reverse transcriptase inhibitors | Pyrrolopyridines | HIV attachment inhibitors | HIV integrase inhibitor | NONNUCLEOSIDE INHIBITORS | CHEMISTRY, MEDICINAL | ENTRY INHIBITORS | ACTIVE COMPONENT | TRICYCLIC NUCLEOSIDE | ANALOGS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHEMISTRY, ORGANIC | PRODRUG BMS-663068 | IMMUNODEFICIENCY-VIRUS TYPE-1 | BIOLOGICAL EVALUATION | ANTIVIRAL ACTIVITY | ATTACHMENT INHIBITOR | Anti-HIV Agents - pharmacology | HIV Integrase Inhibitors - pharmacology | HIV - enzymology | Virus Replication - drug effects | HIV - physiology | RNA-Directed DNA Polymerase - metabolism | HIV Fusion Inhibitors - chemistry | HIV Infections - virology | Humans | Reverse Transcriptase Inhibitors - pharmacology | HIV Fusion Inhibitors - pharmacology | HIV Integrase - metabolism | Drug Discovery | HIV - drug effects | Reverse Transcriptase Inhibitors - chemistry | Anti-HIV Agents - chemistry | Pyrroles - pharmacology | HIV Integrase Inhibitors - chemistry | Pyrroles - chemistry | HIV Infections - drug therapy | DNA polymerases | HIV (Viruses) | Antiviral agents | Drug discovery | Anti-HIV agents
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6. Inhibition of HIV-1 by fusion inhibitors
by Eggink, Dirk and Berkhout, Ben and Sanders, Rogier W
Current Pharmaceutical Design, ISSN 1381-6128, 11/2010, Volume 16, Issue 33, pp. 3716 - 3728
The envelope glycoprotein complex (Env) is responsible for entry of the human immunodeficiency virus type 1 (HIV-1) into cells by mediating attachment to... 
Resistance | Antiviral peptide | T20 | Enfuvirtide | Hiv | Virip | Fusion inhibitors | Virus entry | fusion inhibitors | TERMINAL HEPTAD REPEATS | enfuvirtide | TYPE-1 ENTRY INHIBITORS | REVERSE-TRANSCRIPTASE | ENVELOPE GLYCOPROTEIN | PEPTIDE INHIBITOR | HUMAN-IMMUNODEFICIENCY-VIRUS | antiviral peptide | resistance | 6-HELIX BUNDLE FORMATION | HIV | VIRAL MEMBRANE-FUSION | virus entry | VIRIP | PHARMACOLOGY & PHARMACY | IN-VITRO SYNERGY | CELL-CELL FUSION | Drug Carriers - therapeutic use | HIV Fusion Inhibitors - chemistry | Humans | Drug Resistance, Viral | Peptide Fragments - pharmacology | env Gene Products, Human Immunodeficiency Virus - metabolism | Molecular Targeted Therapy | Virus Internalization - drug effects | Drug Carriers - chemistry | HIV Fusion Inhibitors - administration & dosage | Drug Design | Protein Interaction Domains and Motifs | env Gene Products, Human Immunodeficiency Virus - chemistry | HIV-1 - metabolism | HIV-1 - drug effects | Peptide Fragments - administration & dosage | HIV Fusion Inhibitors - pharmacology | Drug Carriers - pharmacology | HIV Fusion Inhibitors - therapeutic use | alpha 1-Antitrypsin - administration & dosage | Peptide Fragments - chemistry | alpha 1-Antitrypsin - therapeutic use | Animals | alpha 1-Antitrypsin - pharmacology | HIV Infections - drug therapy | Peptide Fragments - therapeutic use
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7. Full Text Development of potent and long-acting HIV-1 fusion inhibitors
by Chong, Huihui and Wu, Xiyuan and Su, Yang and He, Yuxian
AIDS, ISSN 0269-9370, 05/2016, Volume 30, Issue 8, pp. 1187 - 1196
BACKGROUND:T20 (enfuvirtide) is the first approved HIV entry inhibitor and currently the only viral fusion inhibitor, but its low efficacy and genetic barrier... 
HIV-1 | fusion inhibitor | M-T hook structure | lipopeptide | HIV-1 - drug effects | Lipopeptides - pharmacology | Drug Stability | HIV Fusion Inhibitors - chemistry | Humans | HIV Fusion Inhibitors - isolation & purification | Injections, Intraperitoneal | Lipopeptides - isolation & purification | Rats | HIV Envelope Protein gp41 - antagonists & inhibitors | HIV Fusion Inhibitors - pharmacology | Microbial Sensitivity Tests | Animals | Plasma - chemistry | HEK293 Cells | Lipopeptides - chemical synthesis | HIV Fusion Inhibitors - chemical synthesis | Lipopeptides - chemistry
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8. Full Text Entry inhibitors in the treatment of HIV-1 infection
by Tilton, John C and Doms, Robert W
Antiviral Research, ISSN 0166-3542, 2010, Volume 85, Issue 1, pp. 91 - 100
Infection of target cells by HIV is a complex, multi-stage process involving attachment to host cells and CD4 binding, coreceptor binding, and membrane fusion.... 
Entry inhibitors | HIV | Maraviroc | Enfuvirtide | Highly active antiretroviral therapy (HAART) | ENVELOPE GLYCOPROTEIN TRIMERS | TREATMENT EXPERIENCED PATIENTS | SMALL-MOLECULE | CHEMOKINE RECEPTOR CXCR4 | HUMAN-IMMUNODEFICIENCY-VIRUS | ENFUVIRTIDE RESISTANCE MUTATIONS | CCR5 MONOCLONAL-ANTIBODY | VIROLOGY | ACTIVE ANTIRETROVIRAL THERAPY | SYNCYTIUM-INDUCING PHENOTYPE | PHARMACOLOGY & PHARMACY | DISEASE PROGRESSION | HIV Fusion Inhibitors - history | History, 21st Century | HIV-1 - drug effects | Cyclohexanes - pharmacology | History, 20th Century | Humans | Drug Resistance, Viral | Peptide Fragments - history | Peptide Fragments - pharmacology | HIV Envelope Protein gp41 - history | HIV Fusion Inhibitors - pharmacology | HIV Fusion Inhibitors - therapeutic use | Triazoles - history | Triazoles - pharmacology | Cyclohexanes - therapeutic use | HIV Envelope Protein gp41 - pharmacology | HIV Envelope Protein gp41 - therapeutic use | Cyclohexanes - history | HIV Infections - drug therapy | Peptide Fragments - therapeutic use | Triazoles - therapeutic use
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9. Full Text Synthesis, biophysical characterization, and anti-HIV-1 fusion activity of DNA helix-based inhibitors with a p-benzyloxyphenyl substituent at the 5′-nucleobase site
by Tang, Yongjia and Han, Zeye and Guo, Jiamei and Tian, Yangli and Liu, Keliang and Xu, Liang
Bioorganic & Medicinal Chemistry Letters, ISSN 0960-894X, 06/2018, Volume 28, Issue 10, pp. 1842 - 1845
DNA helix-based HIV-1 fusion inhibitors have been discovered as potent drug candidates. Introduction of hydrophobic groups to a nucleobase provides an... 
HIV-1 | Quadruplex | SPR | Duplex | Fusion inhibitor | CHEMISTRY, MEDICINAL | ANTI-HIV ACTIVITY | D(TGGGAG) | QUADRUPLEX-FORMING OLIGONUCLEOTIDES | IMMUNODEFICIENCY-VIRUS TYPE-1 | CHEMISTRY, ORGANIC | APTAMERS | Surface Plasmon Resonance | Nucleosides - chemistry | HIV-1 - drug effects | Humans | HIV Envelope Protein gp41 - metabolism | DNA - metabolism | HIV Envelope Protein gp41 - antagonists & inhibitors | HIV Fusion Inhibitors - pharmacology | HIV Fusion Inhibitors - metabolism | DNA - chemistry | HIV Fusion Inhibitors - chemical synthesis | Kinetics | Circular Dichroism | Transition Temperature | Genetic research | Nucleosides | HIV (Viruses) | Analysis | DNA
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10. Full Text Mechanism of HIV-1 resistance to short-peptide fusion inhibitors targeting the Gp41 pocket
by Su, Yang and Chong, Huihiui and Qiu, Zonglin and Xiong, Shengwen and He, Yuxian
Journal of Virology, ISSN 0022-538X, 2015, Volume 89, Issue 11, pp. 5801 - 5811
The deep hydrophobic pocket on the N trimer of HIV-1 gp41 has been considered an ideal drug target. On the basis of the M-T hook structure, we recently... 
AMINO-ACID-SEQUENCE | VIROLOGY | HEPTAD REPEAT | VIRAL MEMBRANE-FUSION | VIROLOGICAL FAILURE | 6-HELIX BUNDLE | IMMUNODEFICIENCY-VIRUS TYPE-1 | ENVELOPE GLYCOPROTEIN | CLINICAL RESISTANCE | COILED-COIL | T HOOK STRUCTURE | HIV Envelope Protein gp41 - pharmacology | Enfuvirtide | HIV-1 - drug effects | Drug Resistance, Viral | Protein Binding | Peptide Fragments - pharmacology | HIV Envelope Protein gp41 - antagonists & inhibitors | Mutation | Mutation, Missense | HIV Fusion Inhibitors - pharmacology | Amino Acid Substitution | Peptides - pharmacology
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11. Full Text Structure–Activity Relationship Studies of Indole-Based Compounds as Small Molecule HIV‑1 Fusion Inhibitors Targeting Glycoprotein 41
by Zhou, Guangyan and Sofiyev, Vladimir and Kaur, Hardeep and Snyder, Beth A and Mankowski, Marie K and Hogan, Priscilla A and Ptak, Roger G and Gochin, Miriam
Journal of Medicinal Chemistry, ISSN 0022-2623, 06/2014, Volume 57, Issue 12, pp. 5270 - 5281
We previously described indole-containing compounds with the potential to inhibit HIV-1 fusion by targeting the hydrophobic pocket of transmembrane... 
MEMBRANE-FUSION | COILED-COIL DOMAIN | MEDIATED FUSION | CHEMISTRY, MEDICINAL | CONFORMER GENERATION | HTLV-III | 6-HELIX BUNDLE | IMMUNODEFICIENCY-VIRUS TYPE-1 | ENVELOPE GLYCOPROTEIN | BIOLOGICAL EVALUATION | ANTIRETROVIRAL THERAPY | Cell Line | Virus Replication - drug effects | HIV-1 - drug effects | Benzoates - chemistry | HIV Fusion Inhibitors - chemistry | Humans | Drug Resistance, Viral | HIV Envelope Protein gp41 - metabolism | Indoles - chemical synthesis | Peptide Fragments - pharmacology | Benzoates - chemical synthesis | Structure-Activity Relationship | HIV Fusion Inhibitors - pharmacology | Cell Fusion | HIV Envelope Protein gp41 - pharmacology | HIV-1 - physiology | Benzoates - pharmacology | Indoles - pharmacology | HIV Fusion Inhibitors - chemical synthesis | Molecular Docking Simulation | Indoles - chemistry
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12. Full Text Dose-response curve slope sets class-specific limits on inhibitory potential of anti-HIV drugs
by Sedaghat, Ahmad R and Zhou, Yan and Callender, Marc and Zhang, Haili and Shen, Lin and Peterson, Susan and Pitt, Eleanor and Acosta, Edward P and McMahon, Moira A and Siliciano, Robert F and Anderson, Karen S
Nature Medicine, ISSN 1078-8956, 07/2008, Volume 14, Issue 7, pp. 762 - 766
Highly active antiretroviral therapy (HAART) can control HIV-1 replication, but suboptimal treatment allows for the evolution of resistance and rebound... 
MEDICINE, RESEARCH & EXPERIMENTAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | REVERSE-TRANSCRIPTASE | SUSCEPTIBILITY | PHARMACODYNAMICS | CELL BIOLOGY | DARUNAVIR-RITONAVIR | THERAPY | REPLICATION | VIRAL DYNAMICS | ZIDOVUDINE | IMMUNODEFICIENCY-VIRUS TYPE-1 | INFECTION | Anti-HIV Agents - classification | Anti-HIV Agents - pharmacology | HIV Infections - virology | Humans | Reverse Transcriptase Inhibitors - pharmacology | Integrase Inhibitors - pharmacology | Treatment Outcome | HIV Fusion Inhibitors - pharmacology | HIV Protease Inhibitors - therapeutic use | HIV Fusion Inhibitors - therapeutic use | Antiretroviral Therapy, Highly Active | Dose-Response Relationship, Drug | HIV Protease Inhibitors - pharmacology | Inhibitory Concentration 50 | Anti-HIV Agents - therapeutic use | HIV Infections - drug therapy | Integrase Inhibitors - therapeutic use | Reverse Transcriptase Inhibitors - therapeutic use | Complications and side effects | Antiviral agents | Highly active antiretroviral therapy | Dosage and administration | Research | Drug therapy | HIV infection | Health aspects | Anti-HIV agents | Medical research | Antiretroviral drugs | Drug dosages | Human immunodeficiency virus--HIV | Medical treatment | Index Medicus
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