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1. Full Text Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
by McLellan, Jason S and Pancera, Marie and Carrico, Chris and Gorman, Jason and Julien, Jean-Philippe and Khayat, Reza and Louder, Robert and Pejchal, Robert and Sastry, Mallika and Dai, Kaifan and O'Dell, Sijy and Patel, Nikita and Shahzad-Ul-Hussan, Syed and Yang, Yongping and Zhang, Baoshan and Zhou, Tongqing and Zhu, Jiang and Boyington, Jeffrey C and Chuang, Gwo-Yu and Diwanji, Devan and Georgiev, Ivelin and Do Kwon, Young and Lee, Doyung and Louder, Mark K and Moquin, Stephanie and Schmidt, Stephen D and Yang, Zhi-Yong and Bonsignori, Mattia and Crump, John A and Kapiga, Saidi H and Sam, Noel E and Haynes, Barton F and Burton, Dennis R and Koff, Wayne C and Walker, Laura M and Phogat, Sanjay and Wyatt, Richard and Orwenyo, Jared and Wang, Lai-Xi and Arthos, James and Bewley, Carole A and Mascola, John R and Nabel, Gary J and Schief, William R and Ward, Andrew B and Wilson, Ian A and Kwong, Peter D and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature, ISSN 0028-0836, 12/2011, Volume 480, Issue 7377, pp. 336 - 343
Variable regions 1 and 2 (V1/V2) of human immunodeficiency virus-1 (HIV-1) gp120 envelope glycoprotein are critical for viral evasion of antibody... 
SYSTEM | POTENT NEUTRALIZATION | DEXTRAN SULFATE | EPITOPE | MULTIDISCIPLINARY SCIENCES | IMMUNODEFICIENCY-VIRUS TYPE-1 | ENVELOPE GLYCOPROTEIN | RECEPTOR | BINDING | T-CELLS | SOFTWARE | AIDS Vaccines - immunology | Glycopeptides - chemistry | Molecular Sequence Data | Antibody Affinity - immunology | Crystallography, X-Ray | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | Glycopeptides - immunology | Antibody Specificity - immunology | HIV Antibodies - immunology | HIV-1 - chemistry | Protein Structure, Quaternary | Conserved Sequence | Polysaccharides - chemistry | HIV Envelope Protein gp120 - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | Binding Sites, Antibody - immunology | Models, Molecular | Glycosylation | Polysaccharides - immunology | HIV Antibodies - chemistry | AIDS Vaccines - chemistry | Amino Acid Motifs | HIV-1 - immunology | Immune Evasion | Hydrogen Bonding | Antigen-Antibody Complex - chemistry | Antibodies, Neutralizing - chemistry | Epitopes - chemistry | Antigen-Antibody Complex - immunology | Viral envelopes | Genetic aspects | Research | HIV (Viruses) | Structure | Binding sites (Biochemistry) | Proteins | Crystals | Vaccines | ANTIBODIES | AIDS VIRUS | BASIC BIOLOGICAL SCIENCES | AFFINITY | BIOLOGY | GLYCOPROTEINS | VULNERABILITY | ANTIGENS | IMMUNOLOGY | 60 APPLIED LIFE SCIENCES
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2. Full Text Molecular architecture of native HIV-1 gp120 trimers
by Subramaniam, Sriram and Liu, Jun and Bartesaghi, Alberto and Borgnia, Mario J and Sapiro, Guillermo
Nature, ISSN 0028-0836, 09/2008, Volume 455, Issue 7209, pp. 109 - 113
The envelope glycoproteins (Env) of human and simian immunodeficiency viruses (HIV and SIV, respectively) mediate virus binding to the cell surface receptor... 
LACKING | REPLICATION | EPITOPE | VACCINE DESIGN | MULTIDISCIPLINARY SCIENCES | ENVELOPE GLYCOPROTEIN | RECEPTOR | HUMAN-IMMUNODEFICIENCY-VIRUS | NEUTRALIZATION | BINDING | ELECTRON TOMOGRAPHY | Models, Molecular | HIV Envelope Protein gp120 - metabolism | Protein Subunits - metabolism | Cryoelectron Microscopy | HIV Envelope Protein gp120 - immunology | CD4 Antigens - chemistry | HIV-1 - chemistry | Immunoglobulin Fab Fragments - chemistry | Protein Structure, Quaternary | Protein Binding | Protein Subunits - chemistry | HIV Envelope Protein gp120 - chemistry | Immunoglobulin Fab Fragments - immunology | CD4 Antigens - metabolism | Usage | CD4 lymphocytes | Tomography | Glycoproteins | Genetic aspects | Research | HIV (Viruses) | Changes | Software packages | Maps | Molecular structure | Human immunodeficiency virus--HIV | Electron microscopes | Data collection | Viruses
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3. Full Text SAXS data analysis and modeling of tetravalent neutralizing antibody CD4–IgG2 −/+ HIV-1 gp120 revealed that first two gp120 bind to the same Fab arm
by Rathore, Yogendra S and Solanki, Ashish K and Dhoke, Reema R and Ashish and BROOKHAVEN NATIONAL LABORATORY (BNL)
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 2011, Volume 415, Issue 4, pp. 680 - 685
► SAXS data analysis and modeling provided global shape of CD4–IgG2 and its complexes with HIV-1 gp120. ► Models of ternary complex revealed that first two... 
CD4–IgG2 | Structure reconstruction | Engineered antibody | Small angle X-ray scattering | HIV-1 gp120 | CD4-IgG2 | BIOLOGICAL MACROMOLECULES | SMALL-ANGLE SCATTERING | SOLUBLE CD4 | VIRIONS | BIOCHEMISTRY & MOLECULAR BIOLOGY | PRO 542 | HUMAN-IMMUNODEFICIENCY-VIRUS | BIOPHYSICS | DISSOCIATION | TYPE-1 | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | Models, Chemical | X-Ray Diffraction | Antibodies, Neutralizing - chemistry | Humans | Immunoglobulin Fab Fragments - chemistry | Scattering, Small Angle | Immunoglobulin Fab Fragments - immunology | CD4 Immunoadhesins - immunology | CD4 Immunoadhesins - chemistry | Models | HIV (Viruses) | Analysis | Immunoglobulin G
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4. Full Text Structure of a V3-Containing HIV-1 gp120 Core
by Chih-chin Huang and Min Tang and Mei-Yun Zhang and Shahzad Majeed and Elizabeth Montabana and Robyn L. Stanfield and Dimiter S. Dimitrov and Bette Korber and Joseph Sodroski and Ian A. Wilson and Richard Wyatt and Peter D. Kwong
Science, ISSN 0036-8075, 11/2005, Volume 310, Issue 5750, pp. 1025 - 1028
The third variable region (V3) of the HIV-1 gp120 envelope glycoprotein is immunodominant and contains features essential for coreceptor binding. We determined... 
Receptors | HIV | Antibodies | Atoms | Research facilities | Viruses | Reports | Trimers | Cell membranes | Binding sites | HIV 1 | V3 LOOP | SOLUBLE CD4 | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ENVELOPE GLYCOPROTEIN | RECEPTOR | ANTIBODY | HUMAN-IMMUNODEFICIENCY-VIRUS | TYPE-1 | BINDING | NEUTRALIZATION | Humans | Molecular Sequence Data | Crystallography, X-Ray | HIV Envelope Protein gp120 - metabolism | HIV Envelope Protein gp120 - immunology | Receptors, CCR5 - metabolism | HIV Antibodies - immunology | HIV-1 - chemistry | Peptide Fragments - immunology | HIV Envelope Protein gp120 - chemistry | Binding Sites | Protein Structure, Tertiary | Amino Acid Sequence | HIV-1 - metabolism | Peptide Fragments - metabolism | Crystallization | Models, Molecular | Receptors, CXCR4 - metabolism | HIV-1 - immunology | Peptide Fragments - chemistry | Hydrogen Bonding | CD4 Antigens - chemistry | Protein Binding | Receptors, CCR5 - chemistry | Protein Conformation | Receptors, CXCR4 - chemistry | Immunodominant Epitopes | CD4 Antigens - metabolism | HIV (Viruses) | Analysis | Research | Glycoproteins | Immunology | Molecular structure | Human immunodeficiency virus--HIV
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5. Full Text Chemical Synthesis of Highly Congested gp120 V1V2 N‑Glycopeptide Antigens for Potential HIV-1-Directed Vaccines
by Aussedat, Baptiste and Vohra, Yusuf and Park, Peter K and Fernández-Tejada, Alberto and Alam, S. Munir and Dennison, S. Moses and Jaeger, Frederick H and Anasti, Kara and Stewart, Shelley and Blinn, Julie H and Liao, Hua-Xin and Sodroski, Joseph G and Haynes, Barton F and Danishefsky, Samuel J
Journal of the American Chemical Society, ISSN 0002-7863, 09/2013, Volume 135, Issue 35, pp. 13113 - 13120
Critical to the search for an effective HIV-1 vaccine is the development of immunogens capable of inducing broadly neutralizing antibodies (BnAbs). A key first... 
HIV-1 | BETA-MANNOPYRANOSIDES | NEUTRALIZING ANTIBODY PG9 | IMMUNODEFICIENCY-VIRUS TYPE-1 | HIGH-MANNOSE | CONVERGENT | GLYCOPROTEINS | LINKED GLYCOPEPTIDE | GLYCAN RECOGNITION | SULFOXIDE METHOD | CHEMISTRY, MULTIDISCIPLINARY | AIDS Vaccines - immunology | Glycopeptides - chemistry | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Antigens - chemistry | AIDS Vaccines - chemistry | HIV Envelope Protein gp120 - immunology | Glycopeptides - immunology | HIV-1 - immunology | Antigens - immunology | HIV Envelope Protein gp120 - chemistry | Carbohydrate Conformation | Care and treatment | Helix-loop-helix motif | Analysis | Protein biosynthesis | Diagnosis | Research | HIV (Viruses) | Protein-protein interactions
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6. Full Text GP120: Target for neutralizing HIV-1 antibodies
by Pantophlet, Ralph and Burton, Dennis R
Annual Review of Immunology, ISSN 0732-0582, 2006, Volume 24, Issue 1, pp. 739 - 769
The glycoprotein (gp) 120 subunit is an important part of the envelope spikes that decorate the surface of HIV-1 and a major target for neutralizing... 
Antigen engineering | AIDS | Vaccine design | Neutralizing antibodies | INTERMOLECULAR DISULFIDE BOND | V3 LOOP | CORECEPTOR-BINDING-SITE | CD4 RECEPTOR-BINDING | neutralizing antibodies | IMMUNOLOGY | antigen engineering | HUMAN-IMMUNODEFICIENCY-VIRUS | PROTECTIVE EFFICACY | N-LINKED GLYCOSYLATION | vaccine design | TYPE-1 ENVELOPE GLYCOPROTEIN | HUMAN MONOCLONAL-ANTIBODIES | HIV Envelope Protein gp120 - genetics | HIV Infections - prevention & control | HIV Infections - virology | Humans | Membrane Glycoproteins - chemistry | AIDS Vaccines - immunology | Models, Molecular | Neutralization Tests | Epitopes - genetics | HIV-1 - genetics | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | HIV-1 - immunology | Models, Immunological | Animals | HIV Antibodies - immunology | Viral Envelope Proteins - chemistry | Protein Engineering | Receptors, HIV - immunology | Viral Envelope Proteins - immunology | Epitopes - chemistry | HIV Envelope Protein gp120 - chemistry | Membrane Glycoproteins - immunology | Simian Immunodeficiency Virus - immunology
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7. Full Text Identification of N-phenyl- N′-(2,2,6,6-tetramethyl-piperidin-4-yl)-oxalamides as a new class of HIV-1 entry inhibitors that prevent gp120 binding to CD4
by Zhao, Qian and Ma, Liying and Jiang, Shibo and Lu, Hong and Liu, Shuwen and He, Yuxian and Strick, Nathan and Neamati, Nouri and Debnath, Asim Kumar
Virology, ISSN 0042-6822, 2005, Volume 339, Issue 2, pp. 213 - 225
We have identified two -phenyl- ′-(2,2,6,6-tetramethyl-piperidin-4-yl)-oxalamide analogs as a novel class of human immunodeficiency virus type 1 (HIV-1) entry... 
Inhibition | CD4–gp120 interaction | Cell–cell fusion | HIV-1 entry | Virus–cell fusion | Cell-cell fusion | Virus-cell fusion | CD4-gp120 interaction | Anti-HIV Agents - pharmacology | Binding, Competitive | Virus Replication - drug effects | CD4 Antigens - drug effects | Humans | Oxamic Acid - analogs & derivatives | HIV Envelope Protein gp120 - metabolism | Oxamic Acid - pharmacology | Anti-HIV Agents - chemistry | Receptors, HIV - antagonists & inhibitors | HIV-1 - physiology | CD4 Antigens - chemistry | HIV-1 - chemistry | Protein Binding - drug effects | Oxamic Acid - chemistry | Anti-HIV Agents - isolation & purification | CD4 Antigens - metabolism | Protein Structure, Tertiary - drug effects | Prevention | Reverse transcriptase | Proteases | Analysis | Chemical properties | Lead compounds | HIV (Viruses) | Health aspects | Organic compounds
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8. Full Text Sequence‐Controlled Multi‐Block Glycopolymers to Inhibit DC‐SIGN‐gp120 Binding
by Zhang, Qiang and Collins, Jennifer and Anastasaki, Athina and Wallis, Russell and Mitchell, Daniel A and Becer, C. Remzi and Haddleton, David M
Angewandte Chemie International Edition, ISSN 1433-7851, 04/2013, Volume 52, Issue 16, pp. 4435 - 4439
Chain of command: Multi‐block glycopolymers made of mannose (M, see figure), glucose, and di(ethylene glycol) ethyl ether (D) monomers were synthesized using a... 
block copolymers | polymerization | glycosylation | polymers | supramolecular chemistry | LIGAND-BINDING | RECOGNITION | CLICK CHEMISTRY | SET-LRP | CHEMISTRY, MULTIDISCIPLINARY | LECTIN | LIVING RADICAL POLYMERIZATION | DC-SIGN | GLYCOPROTEIN | HIV ENTRY | Polymers - chemical synthesis | Polymers - pharmacology | HIV Envelope Protein gp120 - antagonists & inhibitors | Polymerization | Dendritic Cells - drug effects | Polymers - chemistry | Molecular Structure | HIV Envelope Protein gp120 - chemistry | Dendritic Cells - virology | Binding Sites - drug effects | Medical colleges | Equipment and supplies | Fire extinction | Block copolymers | Proteins | Binding | HIV | Glycopolymers | Mannose | Glucose | Ethers | Monomers
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9. Full Text Structural definition of a conserved neutralization epitope on HIV-1 gp120
by Van Ryk, Donald and Wyatt, Richard and Dey, Barna and Zhang, Mei-Yun and Nabel, Gary J and Xu, Ling and Xiang, Shi-Hua and Dimitrov, Dimiter S and Sodroski, Joseph and Arthos, James and Yang, Xinzhen and Zhou, Tongqing and Kwong, Peter D and Hessell, Ann J and Burton, Dennis R and Zwick, Michael B
Nature, ISSN 0028-0836, 02/2007, Volume 445, Issue 7129, pp. 732 - 737
The remarkable diversity, glycosylation and conformational flexibility of the human immunodeficiency virus type 1 (HIV-1) envelope (Env), including substantial... 
DOMAIN | PROTEIN | RECOGNITION | MULTIDISCIPLINARY SCIENCES | GP41 | IMMUNODEFICIENCY-VIRUS TYPE-1 | HUMAN MONOCLONAL-ANTIBODY | ENVELOPE GLYCOPROTEIN | BINDING SITES | RECEPTOR | ANTIGEN | Molecular Weight | HIV-1 - drug effects | Models, Molecular | Neutralization Tests | HIV Envelope Protein gp120 - metabolism | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | HIV-1 - immunology | HIV-1 - physiology | HIV Antibodies - immunology | CD4 Antigens - chemistry | HIV-1 - chemistry | Conserved Sequence | Protein Conformation | Epitopes - chemistry | HIV Envelope Protein gp120 - chemistry | HIV Antibodies - pharmacology | Binding Sites | CD4 Antigens - metabolism | Proteins | Human immunodeficiency virus | HIV | Molecular structure | Binding sites
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10. Full Text Sensitive electrochemical detection of gp120 based on the combination of NBD-556 and gp120
by Ma, Ya and Liu, Cheng and Wang, Min and Wang, Li-Shi
Talanta, ISSN 0039-9140, 05/2019, Volume 196, pp. 486 - 492
As is known, the employment of molecular imprinting polymer (MIP) as specific sensing materials in sensors, namely MIP-based sensors. In this contribution, we... 
NBD-556 | Gp120 | CNF-Bi composites | Electrochemical sensor | Molecularly imprinted polymer | CHEMISTRY, ANALYTICAL | MOLECULARLY IMPRINTED POLYMERS | GLASSY-CARBON ELECTRODE | CHITOSAN | ENVELOPE GLYCOPROTEIN | GRAPHENE NANOPLATELETS | RECEPTOR | SENSOR | HIV GP120 | PROTEIN CONFORMATION | BINDING
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11. Full Text Interaction of the gp120 V1V2 loop with a neighboring gp120 unit shields the HIV envelope trimer against cross-neutralizing antibodies
by Rusert, Peter and Krarup, Anders and Magnus, Carsten and Brandenberg, Oliver F and Weber, Jacqueline and Ehlert, Anna-Katharina and Regoes, Roland R and Günthard, Huldrych F and Trkola, Alexandra
Journal of Experimental Medicine, ISSN 0022-1007, 07/2011, Volume 208, Issue 7, pp. 1419 - 1433
The HIV-1 envelope trimer adopts a quaternary conformation that effectively shields neutralization-sensitive domains and thus represents a major obstacle for... 
MEDICINE, RESEARCH & EXPERIMENTAL | TYPE-1 ISOLATE | CHRONIC INFECTION | INTEGRIN ALPHABETA | SOLUBLE CD4 | HUMORAL IMMUNITY | IMMUNOLOGY | HUMAN-IMMUNODEFICIENCY-VIRUS | RECEPTOR-BINDING | SUBTYPE-B | DISEASE PROGRESSION | GLYCOSYLATION SITES | HIV Envelope Protein gp120 - genetics | HIV Antibodies | Humans | Molecular Sequence Data | HIV Envelope Protein gp120 - metabolism | HIV Envelope Protein gp120 - immunology | HIV-1 - chemistry | Base Sequence | Peptide Fragments - immunology | Protein Structure, Quaternary | Protein Interaction Domains and Motifs | HIV Envelope Protein gp120 - chemistry | Peptide Fragments - genetics | Antibodies, Neutralizing | Amino Acid Sequence | Cell Line | Peptide Fragments - metabolism | Models, Molecular | HIV-1 - genetics | Cross Reactions | HIV-1 - immunology | Models, Immunological | Peptide Fragments - chemistry | Epitopes - chemistry | DNA, Viral - genetics
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