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1. 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
PROTEINS | HUMDISEASE | SIGNALING | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | 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 | Index Medicus | glycoprotein gp41 | Envelopes | Membrane fusion | Glycoprotein gp120 | CD4 antigen
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2. 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 (London), ISSN 0028-0836, 07/2017, Volume 547, Issue 7663, pp. 360 - 361
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 | Viral envelopes | Allosteric proteins | Binding | Carbohydrates | Antigens | CCR5 protein | Glycoprotein gp41 | 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 | Index Medicus
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3. Full Text Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface
by Huang, Jinghe and Kang, Byong H and Pancera, Marie and Lee, Jeong Hyun and Tong, Tommy and Feng, Yu and Imamichi, Hiromi and Georgiev, Ivelin S and Chuang, Gwo-Yu and z, Aliaksan and Doria-Rose, Nicole A and Laub, Leo and Sliepen, Kwinten and van Gils, Marit J and de la Peña, Alba Torrents and Derking, Ronald and Klasse, Per-Johan and Migueles, Stephen A and Bailer, Robert T and Alam, Munir and Pugach, Pavel and Haynes, Barton F and Wyatt, Richard T and Sanders, Rogier W and Binley, James M and Ward, Anew B and Mascola, John R and Kwong, Peter D and Connors, Mark
Nature (London), ISSN 0028-0836, 2014, Volume 515, Issue 7525, pp. 138 - 142
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Immunoglobulin Fab Fragments - ultrastructure | Antibody Specificity | Epitope Mapping | HIV Envelope Protein gp41 - immunology | Humans | AIDS Vaccines - immunology | Molecular Sequence Data | Leukocytes, Mononuclear | HIV Envelope Protein gp41 - chemistry | Virus Internalization - drug effects | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | Receptors, CCR5 - metabolism | HIV Antibodies - immunology | Conserved Sequence | Inhibitory Concentration 50 | HIV Envelope Protein gp120 - chemistry | HIV Antibodies - pharmacology | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Cell Line | Immunoglobulin Fab Fragments - genetics | HIV-1 - drug effects | Antibodies, Monoclonal - pharmacology | Models, Molecular | Antibodies, Neutralizing - pharmacology | Antibody Affinity | Antibodies, Neutralizing - genetics | HIV Antibodies - chemistry | AIDS Vaccines - chemistry | Antibodies, Monoclonal - genetics | HIV-1 - immunology | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | Cell Membrane - virology | Epitopes - chemistry | HIV Antibodies - genetics | Immunoglobulin Fab Fragments - immunology | CD4 Antigens - metabolism | Viral antibodies | Care and treatment | Antibodies | Physiological aspects | Genetic aspects | Research | HIV infection | Antigenic determinants | Amino acids | Mutation | Vaccines | Human immunodeficiency virus--HIV | Binding sites | Index Medicus
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4. 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 (London), ISSN 0028-0836, 10/2014, Volume 514, Issue 7253, pp. 455 - 461
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | 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 | Index Medicus | X-ray crystallography | HIV infections | Protein function predictions | Protein vaccines | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES
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5. 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
Resistance | Gp41 | Gp120 | Conformational changes | Fusion | Envelope glycoprotein | HIV-1 entry | Fusion inhibitor | Life Sciences & Biomedicine | Science & Technology | Virology | 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 | Index Medicus
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6. 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 (American Association for the Advancement of Science), ISSN 0036-8075, 03/2016, Volume 351, Issue 6277, pp. 1043 - 1048
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | 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 | Index Medicus
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7. Full Text Probing the Structure of the HIV-1 Envelope Trimer Using Aspartate Scanning Mutagenesis
by Das, Raksha and Datta, Rohini and Varadarajan, Raghavan
Journal of virology, ISSN 0022-538X, 11/2020, Volume 94, Issue 21
Life Sciences & Biomedicine | Science & Technology | Virology | HIV Envelope Protein gp120 - genetics | HIV Envelope Protein gp41 - genetics | Humans | Protein Multimerization | HIV Envelope Protein gp41 - metabolism | HIV Envelope Protein gp41 - chemistry | HIV Envelope Protein gp120 - metabolism | HIV Envelope Protein gp160 - chemistry | Proteolysis | Cloning, Molecular | HEK293 Cells | HIV Envelope Protein gp160 - genetics | HIV Envelope Protein gp120 - chemistry | Protein Stability | HIV Envelope Protein gp160 - metabolism | CD4 Antigens - genetics | Recombinant Proteins - metabolism | HIV-1 - metabolism | Gene Expression | Genetic Vectors - chemistry | Genetic Vectors - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | HIV-1 - genetics | Intrinsically Disordered Proteins - genetics | Mutagenesis | Intrinsically Disordered Proteins - chemistry | Aspartic Acid - metabolism | Aspartic Acid - chemistry | Amino Acid Substitution | CD4 Antigens - metabolism | Intrinsically Disordered Proteins - metabolism | Index Medicus
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