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1. Full Text MOLECULAR INTERACTIONS MEDIATING T CELL ANTIGEN RECOGNITION
by Merwe, P. Anton van der and Davis, Simon J
Annual Review of Immunology, ISSN 0732-0582, 04/2003, Volume 21, Issue 1, pp. 659 - 684
Over the past decade, key protein interactions contributing to T cell antigen recognition have been characterized in molecular detail. These have included... 
coreceptor | accessory molecules | T cell receptor | costimulation | Coreceptor | Costimulation | Accessory molecules | NATURAL-KILLER | CRYSTAL-STRUCTURE | IMMUNOLOGY | MHC CLASS-I | PROTEIN-PROTEIN RECOGNITION | CD8 CORECEPTOR FUNCTION | ECTODOMAIN FRAGMENT | VERY-LOW AFFINITY | PEPTIDE-MHC | IMMUNOLOGICAL SYNAPSE | RECEPTOR-BINDING | Receptors, Antigen, T-Cell - chemistry | Membrane Glycoproteins - metabolism | Humans | Membrane Glycoproteins - chemistry | Antigens, CD - metabolism | CD28 Antigens - metabolism | B7-2 Antigen | Abatacept | B7-1 Antigen - chemistry | Antigens, Differentiation - metabolism | Antigens, CD - chemistry | CD2 Antigens - metabolism | Receptors, Antigen, T-Cell - metabolism | Lymphocyte Activation | Models, Molecular | Antigens - metabolism | B7-1 Antigen - metabolism | Static Electricity | Antigens - chemistry | CD2 Antigens - chemistry | CTLA-4 Antigen | CD8 Antigens - metabolism | Animals | CD8 Antigens - chemistry | Antigens, Differentiation - chemistry | Immunoconjugates | CD4 Antigens - chemistry | T-Lymphocytes - immunology | CD28 Antigens - chemistry | Kinetics | CD4 Antigens - metabolism
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2. Full Text Identifying specificity groups in the T cell receptor repertoire
by Glanville, Jacob and Huang, Huang and Nau, Allison and Hatton, Olivia and Wagar, Lisa E and Rubelt, Florian and Ji, Xuhuai and Han, Arnold and Krams, Sheri M and Pettus, Christina and Haas, Nikhil and Arlehamn, Cecilia S. Lindestam and Sette, Alessandro and Boyd, Scott D and Scriba, Thomas J and Martinez, Olivia M and Davis, Mark M
Nature, ISSN 0028-0836, 07/2017, Volume 547, Issue 7661, pp. 94 - 98
T cell receptor (TCR) sequences are very diverse, with many more possible sequence combinations than T cells in any one individual(1-4). Here we define the... 
PROTEIN | EPITOPE | RECOGNITION | MULTIDISCIPLINARY SCIENCES | CD4(+) | DIVERSITY | NAIVE | Amino Acid Sequence | Receptors, Antigen, T-Cell - chemistry | Humans | Mycobacterium tuberculosis - immunology | HLA Antigens - immunology | Models, Molecular | Substrate Specificity | Crystallography, X-Ray | HLA Antigens - chemistry | Epitopes, T-Lymphocyte - chemistry | Algorithms | Adolescent | Ligands | Mycobacterium tuberculosis - chemistry | Receptors, Antigen, T-Cell - immunology | Epitopes, T-Lymphocyte - immunology | Physiological aspects | Cell receptors | Genetic aspects | T cells | Antigens | Cytomegalovirus | Peptides | Amino acids | Infections | Lymphocytes T | T cell receptors | Epitopes | CD4 antigen | Proteins | T-cell receptor | Tuberculosis | Major histocompatibility complex | Mutagenesis | Lymphocytes | Complementarity-determining region | Histocompatibility antigen HLA | Histocompatibility | Complementarity-determining region 3 | Index Medicus
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3. 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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4. Full Text Isolation of neoantigen-specific T cells from tumor and peripheral lymphocytes
by Cohen, Cyrille J and Gartner, Jared J and Horovitz-Fried, Miryam and Shamalov, Katerina and Trebska-McGowan, Kasia and Bliskovsky, Valery V and Parkhurst, Maria R and Ankri, Chen and Prickett, Todd D and Crystal, Jessica S and Li, Yong F and El-Gamil, Mona and Rosenberg, Steven A and Robbins, Paul F
Journal of Clinical Investigation, ISSN 0021-9738, 10/2015, Volume 125, Issue 10, pp. 3981 - 3991
Adoptively transferred tumor-infiltrating T lymphocytes (TILs) that mediate complete regression of metastatic melanoma have been shown to recognize mutated... 
CD4+T CELLS | MEDICINE, RESEARCH & EXPERIMENTAL | METASTATIC MELANOMA | TCR | THERAPY | RECOGNITION | ANTI-CTLA-4 | MUTATIONAL LANDSCAPE | CD4(+) | ANTIGENS | BLOCKADE | Humans | Middle Aged | Neoplasm Proteins - immunology | Molecular Sequence Data | Male | Antigen-Antibody Reactions | Epitopes - immunology | Exome | Melanoma - genetics | Peptide Fragments - immunology | Adult | Female | Receptor, ErbB-2 - immunology | Neoplasm Proteins - genetics | Nuclear Proteins - genetics | Transcription Factors - immunology | Amino Acid Sequence | Antigens, Neoplasm - genetics | DNA-Binding Proteins - immunology | HLA-A2 Antigen - immunology | Antigens, Neoplasm - immunology | Interferon-gamma Release Tests | Cells, Cultured | HLA-A1 Antigen - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Epitopes - genetics | Nuclear Proteins - immunology | Melanoma - secondary | HLA-A2 Antigen - chemistry | Algorithms | Genes, erbB-2 | Melanoma - immunology | Adolescent | RNA, Neoplasm - genetics | T-Cell Antigen Receptor Specificity | T-Lymphocytes - immunology | HLA-A1 Antigen - immunology | DNA, Neoplasm - genetics | Mutation | Antigens, Neoplasm - classification | Lymphocytes, Tumor-Infiltrating - immunology | Physiological aspects | T cells | Lymphocytes | Identification and classification | Health aspects | Tumors | Antigens | Peptides | Cloning | Melanoma | T cell receptors | Metastasis | Cancer therapies | Patients | Studies | Immunotherapy | Cancer
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5. Full Text Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus
by Liao, Hua-Xin and Lynch, Rebecca and Zhou, Tongqing and Gao, Feng and Munir Alam, S and Boyd, Scott D and Fire, Andrew Z and Roskin, Krishna M and Schramm, Chaim A and Zhang, Zhenhai and Zhu, Jiang and Shapiro, Lawrence and Mullikin, James C and Gnanakaran, S and Hraber, Peter and Wiehe, Kevin and Kelsoe, Garnett and Yang, Guang and Xia, Shi-Mao and Montefiori, David C and Parks, Robert and Lloyd, Krissey E and Scearce, Richard M and Soderberg, Kelly A and Cohen, Myron and Kamanga, Gift and Louder, Mark K and Tran, Lillian M and Chen, Yue and Cai, Fangping and Chen, Sheri and Moquin, Stephanie and Du, Xiulian and Gordon Joyce, M and Srivatsan, Sanjay and Zhang, Baoshan and Zheng, Anqi and Shaw, George M and Hahn, Beatrice H and Kepler, Thomas B and Korber, Bette T. M and Kwong, Peter D and Mascola, John R and Haynes, Barton F and Becker, Jesse and Benjamin, Betty and Blakesley, Robert and Bouffard, Gerry and Brooks, Shelise and Coleman, Holly and Dekhtyar, Mila and Gregory, Michael and Guan, Xiaobin and Gupta, Jyoti and Han, Joel and Hargrove, April and Ho, Shi-Ling and Johnson, Taccara and Legaspi, Richelle and Lovett, Sean and Maduro, Quino and Masiello, Cathy and Maskeri, Baishali and McDowell, Jenny and Montemayor, Casandra and Mulliki, James and Park, Morgan and Riebow, Nancy and Schandler, Karen and Schmidt, Brian and Sison, Christina and Stantripop, Mal and Thomas, James and Thomas, Pam and Vemulapalli, Meg and Young, Alice and NISC Comparative Sequencing Progra and NISC Comparative Sequencing Program
Nature, ISSN 0028-0836, 04/2013, Volume 496, Issue 7446, pp. 469 - 476
Current human immunodeficiency virus-1 (HIV-1) vaccines elicit strain-specific neutralizing antibodies. However, cross-reactive neutralizing antibodies arise... 
CRYSTALLIZATION | B-CELL RESPONSES | CONFORMATIONAL EPITOPE | POTENT NEUTRALIZATION | EVOLUTION | CD4 BINDING-SITE | MULTIDISCIPLINARY SCIENCES | ENVELOPE GLYCOPROTEIN | HUMAN MONOCLONAL-ANTIBODIES | SUBTYPE-B | IN-SITU PROTEOLYSIS | HIV Envelope Protein gp120 - genetics | Clone Cells - cytology | Humans | AIDS Vaccines - immunology | Molecular Sequence Data | Crystallography, X-Ray | Neutralization Tests | Phylogeny | HIV Envelope Protein gp120 - metabolism | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HIV-1 - chemistry | HIV Envelope Protein gp120 - chemistry | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Protein Structure, Tertiary | Amino Acid Sequence | CD4 Antigens - immunology | Africa | Cells, Cultured | Models, Molecular | Antibodies, Neutralizing - genetics | Cross Reactions - immunology | HIV Antibodies - chemistry | HIV-1 - classification | Antibodies, Monoclonal - genetics | Cell Lineage | HIV-1 - immunology | CD4 Antigens - chemistry | Antibodies, Neutralizing - chemistry | Epitopes - chemistry | HIV Antibodies - genetics | Mutation | Evolution, Molecular | Monoclonal antibodies | AIDS vaccines | Genetic aspects | Research | HIV (Viruses) | Properties | Proteins | Plasma | Infections | Patients | Binding sites | Crystal structure
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6. Full Text Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer
by Dmitry Lyumkis and Jean-Philippe Julien and Natalia de Val and Albert Cupo and Clinton S. Potter and Per-Johan Klasse and Dennis R. Burton and Rogier W. Sanders and John P. Moore and Bridget Carragher and Ian A. Wilson and Andrew B. Ward
Science, ISSN 0036-8075, 12/2013, Volume 342, Issue 6165, pp. 1484 - 1490
The HIV-1 envelope glycoprotein (Env) trimer contains the receptor binding sites and membrane fusion machinery that introduce the viral genome into the host... 
Medical research | Polysaccharides | Neutralizing antibodies | RESEARCH ARTICLES | Vaccination | Antibodies | Trimers | Epitopes | Binding sites | Protein subunits | HIV 1 | B-CELL RECEPTORS | NEUTRALIZING ANTIBODY PG9 | GP120 CORE | PARTICLE ELECTRON CRYOMICROSCOPY | MULTIDISCIPLINARY SCIENCES | GLYCOPROTEIN COMPLEX | MOLECULAR ARCHITECTURE | RESOLUTION | IMMUNODEFICIENCY-VIRUS TYPE-1 | CD4-BOUND CONFORMATION | VARIABLE LOOPS | Immunodominant Epitopes - immunology | Protein Structure, Tertiary | CD4 Antigens - immunology | env Gene Products, Human Immunodeficiency Virus - immunology | Immunodominant Epitopes - chemistry | Protein Multimerization | AIDS Vaccines - immunology | Models, Molecular | Glycosylation | AIDS Vaccines - chemistry | Cryoelectron Microscopy | CD4 Antigens - chemistry | Antibodies, Neutralizing - chemistry | Antibodies, Viral - chemistry | Protein Structure, Quaternary | Polysaccharides - chemistry | Binding Sites | env Gene Products, Human Immunodeficiency Virus - chemistry | Proteins | Physiological aspects | Host-parasite relationships | Glycoproteins | Research | HIV (Viruses) | Structure | Microscopy | Human immunodeficiency virus--HIV | Crystal structure
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7. Full Text Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01
by Tongqing Zhou and Ivelin Georgiev and Xueling Wu and Zhi-Yong Yang and Kaifan Dai and Andrés Finzi and Young Do Kwon and Johannes F. Scheid and Wei Shi and Ling Xu and Yongping Yang and Jiang Zhu and Michel Nussenzweig and Joseph Sodroski and Lawrence Shapiro and Gary J. Nabel and John R. Mascola and Peter D. Kwong
Science, ISSN 0036-8075, 8/2010, Volume 329, Issue 5993, pp. 811 - 817
During HIV-1 infection, antibodies are generated against the region of the viral gp120 envelope glycoprotein that binds CD4, the primary receptor for HIV-1.... 
Polysaccharides | Immunoglobulins | Receptors | Hydrogen bonds | Neutralizing antibodies | RESEARCH ARTICLES | Genomics | Antibodies | Viruses | Infections | HIV 1 | INDIVIDUALS | SITE | ATTACHMENT | EPITOPE | MULTIDISCIPLINARY SCIENCES | HYPOTHESIS | GP120 ENVELOPE GLYCOPROTEIN | SURFACE | RECEPTOR | MATURATION | VACCINES | HIV Envelope Protein gp120 - genetics | Humans | Molecular Sequence Data | Crystallography, X-Ray | Neutralization Tests | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | Molecular Mimicry | HIV Antibodies - immunology | Immunoglobulin Fab Fragments - metabolism | Base Sequence | HIV Envelope Protein gp120 - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | CD4 Antigens - immunology | Antigenic Variation | Models, Molecular | Antibody Affinity | HIV Antibodies - chemistry | HIV-1 - immunology | CD4 Antigens - chemistry | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | AIDS Vaccines | Protein Conformation | Immunoglobulin Fab Fragments - immunology | Binding Sites, Antibody | CD4 Antigens - metabolism | Molecular biology | Human immunodeficiency virus--HIV | Crystal structure | Immune system
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