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1. Full Text Structure and immune recognition of trimeric pre-fusion HIV-1 Env
by Pancera, Marie and Pancera, Marie and Zhou, Tongqing and Zhou, Tongqing and Druz, Aliaksandr and Druz, Aliaksandr and Georgiev, Ivelin S and Georgiev, Ivelin S and Soto, Cinque and Soto, Cinque and Gorman, Jason and Gorman, Jason and Huang, Jinghe and Huang, Jinghe and Acharya, Priyamvada and Acharya, Priyamvada and Chuang, Gwo-Yu and Chuang, Gwo-Yu and Ofek, Gilad and Ofek, Gilad and Stewart-Jones, Guillaume B. E and Stewart-Jones, Guillaume B.E and Stuckey, Jonathan and Stuckey, Jonathan and Bailer, Robert T and Bailer, Robert T and Joyce, M. Gordon and Joyce, M Gordon and Louder, Mark K and Louder, Mark K and Tumba, Nancy and Tumba, Nancy and Yang, Yongping and Yang, Yongping and Zhang, Baoshan and Zhang, Baoshan and Cohen, Myron S and Cohen, Myron S and Haynes, Barton F and Haynes, Barton F and Mascola, John R and Mascola, John R and Morris, Lynn and Morris, Lynn and Munro, James B and Munro, James B and Blanchard, Scott C and Blanchard, Scott C and Mothes, Walther and Mothes, Walther and Connors, Mark and Connors, Mark and Kwong, Peter D and Kwong, Peter D and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature, ISSN 0028-0836, 10/2014, Volume 514, Issue 7253, pp. 455 - 461
The human immunodeficiency virus type 1 (HIV-1) envelope (Env) spike, comprising three gp120 and three gp41 subunits, is a conformational machine that... 
ENVELOPE GLYCOPROTEIN TRIMERS | B-CELL RESPONSES | POTENT NEUTRALIZATION | NEUTRALIZING ANTIBODY | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | IMMUNODEFICIENCY-VIRUS TYPE-1 | INFLUENZA-VIRUS | CORE STRUCTURE | DEPENDENT EPITOPE | EBOLA-VIRUS | HIV Envelope Protein gp120 - genetics | HIV Envelope Protein gp41 - genetics | Protein Subunits - immunology | HIV Envelope Protein gp41 - immunology | Humans | Protein Multimerization | AIDS Vaccines - immunology | Molecular Sequence Data | Crystallography, X-Ray | HIV Envelope Protein gp41 - chemistry | Virus Internalization | Genetic Variation | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | Protein Structure, Quaternary | Polysaccharides - chemistry | HIV Envelope Protein gp120 - chemistry | Protein Subunits - genetics | Amino Acid Sequence | Membrane Fusion | Models, Molecular | Glycosylation | Polysaccharides - immunology | AIDS Vaccines - chemistry | Immune Evasion | Protein Subunits - chemistry | Structural Homology, Protein | Cohort Studies | Physiological aspects | HIV antibodies | Viral proteins | Structure | Health aspects | Infections | Immunology | Peptides | Human immunodeficiency virus--HIV | Crystals | X-ray crystallography | HIV infections | Protein function predictions | Protein vaccines | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES
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2. Full Text Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
by Lee, Jeong Hyun and Ozorowski, Gabriel and Ward, Andrew B
Science, ISSN 0036-8075, 03/2016, Volume 351, Issue 6277, pp. 1043 - 1048
The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4(+) Tcells and mediates viral entry. During this process, Env undergoes... 
ANTIBODIES | VIRUS | RECOGNITION | MECHANISM | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | GP41 | GLYCOPROTEIN | ENV | DEPENDENT EPITOPE | NEUTRALIZATION | HIV Envelope Protein gp120 - genetics | HIV Envelope Protein gp41 - ultrastructure | Protein Structure, Tertiary | Amino Acid Sequence | HIV Envelope Protein gp41 - genetics | Humans | Protein Multimerization | Molecular Sequence Data | Crystallography, X-Ray | Glycosylation | HIV Envelope Protein gp120 - ultrastructure | HIV Envelope Protein gp41 - chemistry | Virus Internalization | Antibodies, Neutralizing - immunology | HIV-1 - physiology | Hydrophobic and Hydrophilic Interactions | HIV Envelope Protein gp120 - chemistry | Antibodies, Monoclonal - immunology | HIV (Viruses) | Chemical properties | Proteins | Glycoproteins | Structure | Observations | Health aspects | Human immunodeficiency virus--HIV | Cells
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3. Full Text Immunogenicity of Stabilized HIV-1 Envelope Trimers with Reduced Exposure of Non-neutralizing Epitopes
by de Taeye, Steven W and Ozorowski, Gabriel and Torrents de la Peña, Alba and Guttman, Miklos and Julien, Jean-Philippe and van den Kerkhof, Tom L.G.M and Burger, Judith A and Pritchard, Laura K and Pugach, Pavel and Yasmeen, Anila and Crampton, Jordan and Hu, Joyce and Bontjer, Ilja and Torres, Jonathan L and Arendt, Heather and DeStefano, Joanne and Koff, Wayne C and Schuitemaker, Hanneke and Eggink, Dirk and Berkhout, Ben and Dean, Hansi and LaBranche, Celia and Crotty, Shane and Crispin, Max and Montefiori, David C and Klasse, P.J and Lee, Kelly K and Moore, John P and Wilson, Ian A and Ward, Andrew B and Sanders, Rogier W
Cell, ISSN 0092-8674, 12/2015, Volume 163, Issue 7, pp. 1702 - 1715
The envelope glycoprotein trimer mediates HIV-1 entry into cells. The trimer is flexible, fluctuating between closed and more open conformations and sometimes... 
NEUTRALIZING ANTIBODY-RESPONSE | DESIGN | AFFINITY MATURATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLYCOPROTEIN COMPLEX | GP41 | ENV TRIMERS | GP120 | QUATERNARY | REGION | CELL BIOLOGY | Antibodies, Neutralizing | HIV-1 | Rabbits | HIV Envelope Protein gp41 - genetics | Immunoglobulin G - chemistry | AIDS Vaccines - immunology | Models, Molecular | HIV Envelope Protein gp41 - chemistry | AIDS Vaccines - chemistry | Animals | Mutagenesis | Hydrophobic and Hydrophilic Interactions | Protein Conformation | Epitopes - chemistry | env Gene Products, Human Immunodeficiency Virus - chemistry | HIV (Viruses) | AIDS vaccines | Antigenic determinants | Viral antibodies | Antibodies
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4. Full Text Open and closed structures reveal allostery and pliability in the HIV-1 envelope spike
by Ozorowski, Gabriel and Pallesen, Jesper and De Val, Natalia and Lyumkis, Dmitry and Cottrell, Christopher A and Torres, Jonathan L and Copps, Jeffrey and Stanfield, Robyn L and Cupo, Albert and Pugach, Pavel and Moore, John P and Wilson, Ian A and Ward, Andrew B
Nature, ISSN 0028-0836, 07/2017, Volume 547, Issue 7663, pp. 360 - 361
For many enveloped viruses, binding to a receptor(s) on a host cell acts as the first step in a series of events culminating in fusion with the host cell... 
SYSTEM | ANTIBODIES | LEGINON | IMAGES | MULTIDISCIPLINARY SCIENCES | VACCINE | CLASSIFICATION | GP120 | GLYCOPROTEIN | CRYO-EM STRUCTURE | NEUTRALIZATION | Immunoglobulin Fab Fragments - ultrastructure | env Gene Products, Human Immunodeficiency Virus - ultrastructure | HIV Envelope Protein gp41 - genetics | Antibodies - chemistry | HIV Envelope Protein gp41 - metabolism | env Gene Products, Human Immunodeficiency Virus - metabolism | HIV Envelope Protein gp41 - chemistry | Receptors, CCR5 - metabolism | env Gene Products, Human Immunodeficiency Virus - genetics | HIV-1 - chemistry | Antibodies - immunology | Binding Sites - drug effects | env Gene Products, Human Immunodeficiency Virus - chemistry | Allosteric Regulation - drug effects | HIV Envelope Protein gp41 - ultrastructure | Amino Acid Sequence | CD4 Antigens - ultrastructure | Receptors, HIV - chemistry | Antibodies - ultrastructure | Models, Molecular | Receptors, HIV - ultrastructure | Immunoglobulin Fab Fragments - pharmacology | Antibodies - pharmacology | Cryoelectron Microscopy | HIV-1 - ultrastructure | Receptors, HIV - metabolism | CD4 Antigens - chemistry | Immunoglobulin Fab Fragments - chemistry | Receptors, CCR5 - chemistry | Ligands | Immunoglobulin Fab Fragments - immunology | CD4 Antigens - metabolism | Physiological aspects | Genetic aspects | Glycoproteins | HIV (Viruses) | Structure | Binding | Carbohydrates | Antigens | CCR5 protein | Glycoprotein gp41 | Glycoprotein | Antibodies | Viruses | Glycosylation | Trimers | Cell fusion | Electron microscopy | Crystallography | CXCR4 protein | CD4 antigen | Proteins | Transmission electron microscopy | Neutralizing | Human immunodeficiency virus--HIV | Mutation | Coordination compounds | Binding sites
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5. Full Text Topological Layers in the HIV-1 gp120 Inner Domain Regulate gp41 Interaction and CD4-Triggered Conformational Transitions
by Finzi, Andrés and Xiang, Shi-Hua and Pacheco, Beatriz and Wang, Liping and Haight, Jessica and Kassa, Aemro and Danek, Brenda and Pancera, Marie and Kwong, Peter D and Sodroski, Joseph
Molecular Cell, ISSN 1097-2765, 2010, Volume 37, Issue 5, pp. 656 - 667
The entry of human immunodeficiency virus (HIV-1) into cells is initiated by binding of the gp120 exterior envelope glycoprotein to the receptor, CD4. How does... 
PROTEINS | HUMDISEASE | SIGNALING | HTLV-III | EXTERIOR ENVELOPE GLYCOPROTEIN | SOLUBLE CD4 | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSMEMBRANE GLYCOPROTEIN | HUMAN-IMMUNODEFICIENCY-VIRUS | TYPE-1 | NEUTRALIZATION | RECEPTOR-BINDING | AIDS PATIENTS | VIRAL ENTRY | CELL BIOLOGY | HIV Envelope Protein gp120 - genetics | HIV Envelope Protein gp41 - genetics | Humans | HIV Envelope Protein gp41 - metabolism | Structure-Activity Relationship | HIV Envelope Protein gp41 - chemistry | HIV Envelope Protein gp120 - metabolism | Virus Internalization | Receptors, CCR5 - metabolism | Transfection | HIV Envelope Protein gp120 - chemistry | CD4 Antigens - genetics | Protein Structure, Tertiary | HIV-1 - metabolism | Models, Molecular | Genotype | HIV-1 - genetics | HIV-1 - immunology | Phenotype | Animals | Dogs | Protein Binding | Ligands | Protein Conformation | Protein Processing, Post-Translational | HeLa Cells | Mutation | HIV Protease - metabolism | CD4 Antigens - metabolism | glycoprotein gp41 | Envelopes | Membrane fusion | Glycoprotein gp120 | CD4 antigen
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6. Full Text Structural basis for membrane anchoring of HIV-1 envelope spike
by Dev, Jyoti and Park, Donghyun and Fu, Qingshan and Chen, Jia and Ha, Heather Jiwon and Ghantous, Fadi and Herrmann, Tobias and Chang, Weiting and Liu, Zhijun and Frey, Gary and Seaman, Michael S and Chen, Bing and Chou, James J
Science, ISSN 0036-8075, 07/2016, Volume 353, Issue 6295, pp. 172 - 175
HIV-1 envelope spike (Env) is a type I membrane protein that mediates viral entry. We used nuclear magnetic resonance to determine an atomic structure of the... 
FUSION | TRIMER | SPANNING DOMAIN | RECOGNITION | MECHANISM | MULTIDISCIPLINARY SCIENCES | GLYCOPROTEIN | MUTATIONS | NEUTRALIZATION | EXPRESSION | REGION | Protein Structure, Tertiary | HIV Envelope Protein gp41 - genetics | Membrane Fusion | HIV Envelope Protein gp41 - immunology | Protein Multimerization | HIV Envelope Protein gp41 - chemistry | Virus Internalization | Arginine - chemistry | HIV-1 - immunology | HIV-1 - physiology | HIV Antibodies - immunology | Arginine - genetics | Nuclear Magnetic Resonance, Biomolecular | Lipid Bilayers - chemistry | Mutation | Protein Stability | Research | HIV (Viruses) | Analysis | Membrane proteins | Proteins | Membranes | Vaccines | Human immunodeficiency virus--HIV | Spikes | Envelopes | Antibodies | Lipids | Trimers
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7. Full Text Mechanism of HIV-1 Neutralization by Antibodies Targeting a Membrane-Proximal Region of gp41
by Jia Chen and Gary Frey and Hanqin Peng and Sophia Rits-Volloch and Jetta Garrity and Michael S. Seaman and Bing Chen
Journal of Virology, ISSN 0022-538X, 01/2014, Volume 88, Issue 2, pp. 1249 - 1258
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
VIRAL MEMBRANE | RESPONSES | POTENT | DESIGN | EPITOPE | FUSION | VIROLOGY | EXTERNAL REGION | ENVELOPE | IMMUNODEFICIENCY-VIRUS TYPE-1 | INFECTION | Cell Line | Complementarity Determining Regions - genetics | HIV Envelope Protein gp41 - genetics | HIV Envelope Protein gp41 - immunology | HIV Infections - virology | Humans | Neutralization Tests | Antibodies, Neutralizing - genetics | HIV Envelope Protein gp41 - chemistry | HIV-1 - genetics | HIV Antibodies - chemistry | Amino Acid Motifs | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV Antibodies - immunology | Complementarity Determining Regions - chemistry | HIV-1 - chemistry | Antibodies, Neutralizing - chemistry | Complementarity Determining Regions - immunology | Cell Membrane - virology | HIV Antibodies - genetics | Vaccines and Antiviral Agents
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8. Full Text HIV-1 gp41 residues modulate CD4- induced conformational changes in the envelope glycoprotein and evolution of a relaxed conformation of gp120
by Keller, Paul W and Morrison, Orrianne and Vassell, Russell and Weiss, Carol D
Journal of Virology, ISSN 0022-538X, 08/2018, Volume 92, Issue 16
Entry of human immunodeficiency virus type 1 (HIV-1) into host cells is mediated by conformational changes in the envelope glycoprotein (Env) that are... 
Resistance | Gp41 | Gp120 | Conformational changes | Fusion | Envelope glycoprotein | HIV-1 entry | Fusion inhibitor | ENTRY | CRYSTAL-STRUCTURE | RECEPTOR | resistance | envelope glycoprotein | PEPTIDE FUSION INHIBITOR | fusion | fusion inhibitor | TRIMER | VIROLOGY | HEPTAD REPEAT | gp41 | IMMUNODEFICIENCY-VIRUS TYPE-1 | TRANSMEMBRANE PROTEIN GP41 | gp120 | conformational changes | HUMAN MONOCLONAL-ANTIBODIES | CRYO-EM STRUCTURE | Cell Line | HIV Envelope Protein gp41 - genetics | Humans | CD4-Positive T-Lymphocytes - metabolism | HIV Envelope Protein gp41 - metabolism | HIV Envelope Protein gp41 - chemistry | HIV-1 - genetics | HIV Envelope Protein gp120 - metabolism | Virus Internalization | HIV-1 - physiology | Protein Binding | Protein Conformation | HIV Envelope Protein gp120 - chemistry
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9. Full Text HIV gp41 C-terminal heptad repeat contains multifunctional domains: Relation to mechanisms of action of anti-HIV peptides
by Liu, Shuwen and Jing, Weiguo and Cheung, Byron and Lu, Hong and Sun, Jane and Yan, Xuxia and Niu, Jinkui and Farmar, James and Wu, Shuguang and Jiang, Shibo
Journal of Biological Chemistry, ISSN 0021-9258, 03/2007, Volume 282, Issue 13, pp. 9612 - 9620
T20 (Fuzeon), a novel anti-human immunodeficiency virus (HIV) drug, is a peptide derived from HIV-1 gp41 C-terminal heptad repeat (CHR). Its mechanism of... 
MEMBRANE-FUSION | 6-HELIX BUNDLE FORMATION | ENTRY INHIBITORS | BIOCHEMISTRY & MOLECULAR BIOLOGY | IMMUNODEFICIENCY-VIRUS TYPE-1 | ENVELOPE GLYCOPROTEIN | CONFORMATION | COILED-COIL | INHIBITORY-ACTION | BINDING | ENV-MEDIATED FUSION | Anti-HIV Agents - pharmacology | Protein Structure, Tertiary | Amino Acid Sequence | HIV Envelope Protein gp41 - genetics | Peptide Fragments - metabolism | HIV-1 - drug effects | Humans | HIV Envelope Protein gp41 - metabolism | Membrane Fusion - genetics | Molecular Sequence Data | Recombinant Fusion Proteins - chemical synthesis | Peptide Fragments - physiology | Repetitive Sequences, Amino Acid | HIV Envelope Protein gp41 - physiology | Anti-HIV Agents - metabolism | Membrane Fusion - drug effects
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10. Full Text Antibody neutralization and escape by HIV-1
by Wu, Xiaoyun and Salazar, Maria G and Saag, Michael S and Nowak, Martin A and Decker, Julie M and Wang, Shuyi and Kilby, J. Michael and Hui, Huxiong and Shaw, George M and Komarova, Natalia L and Salazar-Gonzalez, Jesus F and Wei, Xiping and Kwong, Peter D and Hahn, Beatrice H and Kappes, John C
Nature, ISSN 0028-0836, 03/2003, Volume 422, Issue 6929, pp. 307 - 312
Neutralizing antibodies (Nab) are a principal component of an effective human immune response to many pathogens, yet their role in HIV-1 infection is unclear.... 
INDIVIDUALS | RESPONSES | VARIANTS | MULTIDISCIPLINARY SCIENCES | GP120 ENVELOPE GLYCOPROTEIN | GLYCOSYLATION | HUMAN-IMMUNODEFICIENCY-VIRUS | TYPE-1 | EMERGENCE | RESIDUES | PRIMARY INFECTION | HIV Envelope Protein gp120 - genetics | Antibody Specificity | HIV Envelope Protein gp41 - genetics | HIV Envelope Protein gp41 - immunology | Humans | Molecular Sequence Data | Neutralization Tests | HIV Envelope Protein gp41 - chemistry | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | HIV-1 - physiology | HIV Antibodies - immunology | Time Factors | HIV-1 - chemistry | HIV Envelope Protein gp120 - chemistry | Antibodies, Monoclonal - immunology | Amino Acid Sequence | CD4 Antigens - immunology | Immune Sera - immunology | HIV Infections - virology | Glycosylation | Epitopes - genetics | HIV-1 - genetics | HIV-1 - immunology | HIV Antigens - genetics | HIV Antigens - immunology | Mutagenesis | Models, Biological | HIV Antigens - chemistry | Epitopes - chemistry | Immunology | Human immunodeficiency virus | HIV | Immune system
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