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index medicus (21) 21
humans (14) 14
hiv-1 - immunology (13) 13
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env gene products, human immunodeficiency virus - immunology (9) 9
antibodies (8) 8
antibodies, neutralizing - immunology (8) 8
broadly neutralizing antibodies (8) 8
immunology (8) 8
vaccine (8) 8
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article (7) 7
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epitopes - immunology (6) 6
hiv (6) 6
hiv-1 (6) 6
immunization (6) 6
immunodeficiency-virus type-1 (6) 6
potent (6) 6
protein multimerization (6) 6
virology (6) 6
antigenic determinants (5) 5
biochemistry & molecular biology (5) 5
cryo-em structure (5) 5
dependent epitope (5) 5
env trimers (5) 5
glycoprotein complex (5) 5
hiv infections - immunology (5) 5
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human immunodeficiency virus--hiv (5) 5
immunogen design (5) 5
mice (5) 5
multidisciplinary sciences (5) 5
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virus diseases (5) 5
affinity maturation (4) 4
antibodies, neutralizing - chemistry (4) 4
binding-site (4) 4
crystallography, x-ray (4) 4
env gene products, human immunodeficiency virus - chemistry (4) 4
epitope mapping (4) 4
epitopes - chemistry (4) 4
hiv envelope protein gp120 - immunology (4) 4
human immunodeficiency virus (4) 4
immunogenicity (4) 4
models, molecular (4) 4
molecular sequence data (4) 4
nanoparticles (4) 4
proteins (4) 4
target (4) 4
trimers (4) 4
vaccine development (4) 4
viruses (4) 4
aids vaccines (3) 3
crystal structure (3) 3
crystal-structure (3) 3
env (3) 3
envelope glycoprotein (3) 3
germline precursors (3) 3
glycoprotein (3) 3
gp120 (3) 3
grants (3) 3
hiv antibodies - chemistry (3) 3
hiv envelope protein gp41 - immunology (3) 3
hiv infections - prevention & control (3) 3
hiv infections - virology (3) 3
immunoglobulins (3) 3
microscopy (3) 3
monoclonal-antibodies (3) 3
neutralizing (3) 3
neutralizing antibodies (3) 3
protein design (3) 3
protein engineering (3) 3
recognition (3) 3
sosip (3) 3
viral antibodies (3) 3
acquired immune deficiency syndrome--aids (2) 2
aids vaccines - chemistry (2) 2
amino acid sequence (2) 2
antibodies, monoclonal - immunology (2) 2
antibodies, neutralizing - biosynthesis (2) 2
antibody response (2) 2
antibody specificity (2) 2
b-cells (2) 2
binding (2) 2
binding sites (2) 2
biology (2) 2
care and treatment (2) 2
cell activation (2) 2
cell line (2) 2
competition (2) 2
conserved sequence (2) 2
dendritic cells (2) 2
disulfide bonds (2) 2
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1. Full Text Toll-like receptor expression and function in human dendritic cell subsets: implications for dendritic cell-based anti-cancer immunotherapy
by Schreibelt, G and Tel, J and Sliepen, K.H and Benitez-Ribas, D and Figdor, C.G and Adema, G.J and Vries, I.J.M. de
Cancer Immunology Immunotherapy, ISSN 0340-7004, 2010, Volume 59, Issue 10, pp. 1573 - 1582
Dendritic cells (DCs) are central players of the immune response. To date, DC-based immunotherapy is explored worldwide in clinical vaccination trials with... 
Plasmacytoid dendritic cells | Immunology | Medicine & Public Health | Myeloid dendritic cells | Toll-like receptors | Oncology | Cancer Research | Dendritic cell vaccination | COLONY-STIMULATING FACTOR | IMMUNOLOGY | CPG DNA | BREAST-CANCER | METASTATIC MELANOMA | HUMAN PERIPHERAL-BLOOD | MESSENGER-RNA | ONCOLOGY | IMMUNE-RESPONSES | IN-VIVO | T-LYMPHOCYTES | ANTIGEN | Neoplasms - therapy | Neoplasms - immunology | Dendritic Cells - immunology | Humans | Immunotherapy | Toll-Like Receptors - metabolism | Dendritic Cells - transplantation | Lymphocyte Subsets - immunology | Antigens | Care and treatment | Dendritic cells | Vaccination | Cancer
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2. Full Text Strategies for inducing effective neutralizing antibody responses against HIV-1
by del Moral-Sánchez, Iván and Sliepen, Kwinten
Expert Review of Vaccines, ISSN 1476-0584, 12/2019, pp. 1 - 17
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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, ISSN 0028-0836, 2014, Volume 515, Issue 7525, pp. 138 - 142
The isolation of human monoclonal antibodies is providing important insights into the specificities that underlie broad neutralization of HIV-1 (reviewed in... 
B-CELLS | SPECIFICITIES | MULTIDISCIPLINARY SCIENCES | SERA | IMMUNODEFICIENCY-VIRUS TYPE-1 | ENV TRIMERS | VULNERABILITY | GP120 | HUMAN MONOCLONAL-ANTIBODIES | CLEAVAGE | DEPENDENT EPITOPE | 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 Structural Delineation of a Quaternary, Cleavage-Dependent Epitope at the gp41-gp120 Interface on Intact HIV-1 Env Trimers
by Blattner, Claudia and Lee, Peter S and Lee, Jeong Hyun and Sliepen, Kwinten and Derking, Ronald and Falkowska, Emilia and de la Peña, Alba Torrents and Cupo, Albert and Julien, Jean-Philippe and van Gils, Marit and Peng, Wenjie and Paulson, James C and Poignard, Pascal and Burton, Dennis R and Moore, John P and Sanders, Rogier W and Wilson, Ian A and Ward, Andrew B
Immunity, ISSN 1074-7613, 05/2014, Volume 40, Issue 5, pp. 669 - 680
All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we... 
REFINEMENT | SITE | POTENT NEUTRALIZATION | RECOGNITION | BROADLY NEUTRALIZING ANTIBODIES | GP41 | IMMUNOLOGY | IDENTIFICATION | COMBINATION | BINDING | Cell Line | HIV Infections - prevention & control | Binding Sites, Antibody - immunology | env Gene Products, Human Immunodeficiency Virus - immunology | HIV Envelope Protein gp41 - immunology | Humans | Crystallization | HIV Envelope Protein gp41 - metabolism | Molecular Sequence Data | Antibodies, Neutralizing - ultrastructure | Crystallography, X-Ray | Polysaccharides - immunology | Epitopes - immunology | HIV Antibodies - ultrastructure | HIV Envelope Protein gp120 - immunology | Antibodies, Monoclonal - ultrastructure | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV Antibodies - immunology | HEK293 Cells | Protein Structure, Quaternary | Antibodies, Monoclonal - immunology | Monoclonal antibodies | Polysaccharides | HIV (Viruses) | Antigenic determinants | Proteins | Medical research | Scholarships & fellowships | Acquired immune deficiency syndrome--AIDS | Councils | Microscopy | Colleges & universities | Chemical bonds | Vaccines | Grants | Viral infections
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5. Full Text Nanoparticle Vaccines for Inducing HIV-1 Neutralizing Antibodies
by Brinkkemper, M and Sliepen, K
VACCINES, ISSN 2076-393X, 09/2019, Volume 7, Issue 3, p. 76
The enormous sequence diversity between human immunodeficiency virus type 1 (HIV-1) strains poses a major roadblock for generating a broadly protective... 
TARGET | MEDICINE, RESEARCH & EXPERIMENTAL | virus-like particles | VIRUS | GERMLINE PRECURSORS | liposomes | self-assembling protein nanoparticles | IMMUNOGEN DESIGN | IMMUNOLOGY | ENVELOPE TRIMERS | RESPONSES | PROXIMAL EXTERNAL REGION | EPITOPE | ENV TRIMERS | BINDING | HIV-1 Env
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6. Full Text Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo
by Medina-Ramírez, Max and Garces, Fernando and Escolano, Amelia and Skog, Patrick and de Taeye, Steven W and del Moral-Sanchez, Ivan and McGuire, Anew T and Yasmeen, Anila and Behrens, Anna-Janina and Ozorowski, Gabriel and van den Kerkhof, Tom L. G. M and Freund, Natalia T and Dosenovic, Pia and Hua, Yuanzi and Gitlin, Alexander D and Cupo, Albert and van der Woude, Patricia and Golabek, Michael and Sliepen, Kwinten and Blane, Tanya and Kootstra, Neeltje and van Breemen, Mariëlle J and Pritchard, Laura K and Stanfield, Robyn L and Crispin, Max and Ward, Anew B and Stamatatos, Leonidas and Klasse, Per Johan and Moore, John P and Nemazee, David and Nussenzweig, Michel C and Wilson, Ian A and Sanders, Rogier W
Journal of experimental medicine, ISSN 0022-1007, 2017, Volume 214, Issue 9, pp. 2573 - 2590
Induction of broadly neutralizing antibodies (bNAbs) by HIV-1 envelope glycoprotein immunogens would be a major advance toward an effective vaccine. A critical... 
VACCINE DEVELOPMENT | MEDICINE, RESEARCH & EXPERIMENTAL | POTENT | GERMLINE PRECURSORS | RECOGNITION | AFFINITY MATURATION | IMMUNODEFICIENCY-VIRUS TYPE-1 | B-CELL-LINEAGE | BINDING-SITE | IMMUNOGEN DESIGN | IMMUNOLOGY | MONOCLONAL-ANTIBODIES | Protein Structure, Tertiary | Antibodies, Neutralizing - immunology | HIV-1 - immunology | Animals | Humans | HEK293 Cells | Protein Multimerization - immunology | Crystallography, X-Ray | HIV Envelope Protein gp160 - immunology | Mice | Gene Knock-In Techniques | Immunization | Immunoglobulins | Secretion | Glycoprotein | Reengineering | Antibodies | T cell receptors | Activation | Vaccines | CD4 antigen | Cell activation | Lymphocytes B | Neutralizing | Human immunodeficiency virus--HIV | Binding sites | Crystal structure | Conformation | 312
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7. Full Text Complete epitopes for vaccine design derived from a crystal structure of the broadly neutralizing antibodies PGT128 and 8ANC195 in complex with an HIV-1 Env trimer
by Kong, Leopold and Torrents de la Peña, Alba and Deller, Marc C and Garces, Fernando and Sliepen, Kwinten and Hua, Yuanzi and Stanfield, Robyn L and Sanders, Rogier W and Wilson, Ian A and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Acta crystallographica. Section D, Biological crystallography, ISSN 0907-4449, 2015, Volume 71, Issue Part 10, pp. 2099 - 2108
The HIV-1 envelope gp160 glycoprotein (Env) is a trimer of gp120 and gp41 heterodimers that mediates cell entry and is the primary target of the humoral immune... 
SOSIP gp140 | HIV‐1 | vaccine design | glycans | broadly neutralizing antibodies | HIV-1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | ENVELOPE GLYCOPROTEIN | VULNERABILITY | CRYSTALLOGRAPHY | GP120 | POTENT | BIOPHYSICS | SEQUENCE | GLYCAN RECOGNITION | REVEALS | env Gene Products, Human Immunodeficiency Virus - immunology | HIV Infections - virology | Humans | Protein Multimerization | Models, Molecular | Crystallography, X-Ray | Polysaccharides - immunology | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV-1 - chemistry | Antibodies, Neutralizing - chemistry | Polysaccharides - chemistry | Protein Conformation | Epitopes - chemistry | HIV Envelope Protein gp120 - chemistry | env Gene Products, Human Immunodeficiency Virus - chemistry | Polysaccharides | AIDS vaccines | Analysis | Force and energy | Crystals | HIV (Viruses) | Structure | Antigenic determinants | Neutralizing | Antibodies | Evolution | Trimers | Vaccines | Shields | Glycan | Crystal structure
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8. Full Text Comprehensive antigenic map of a cleaved soluble HIV-1 envelope trimer
by Derking, Ronald and Ozorowski, Gabriel and Sliepen, Kwinten and Yasmeen, Anila and Cupo, Albert and Torres, Jonathan L and Julien, Jean-Philippe and Lee, Jeong Hyun and van Montfort, Thijs and de Taeye, Steven W and Connors, Mark and Burton, Dennis R and Wilson, Ian A and Klasse, Per-Johan and Ward, Anew B and Moore, John P and Sanders, Rogier W
PLoS pathogens, ISSN 1553-7366, 2015, Volume 11, Issue 3, pp. 1 - 22
The trimeric envelope (Env) spike is the focus of vaccine design efforts aimed at generating broadly neutralizing antibodies (bNAbs) to protect against HIV-1... 
MICROBIOLOGY | DEPENDENT EPITOPE | GP41-GP120 INTERFACE | POTENT | VIROLOGY | BROADLY NEUTRALIZING ANTIBODIES | GLYCOPROTEIN COMPLEX | IMMUNODEFICIENCY-VIRUS TYPE-1 | ENV TRIMERS | BINDING-SITE | CD4 BINDING | MONOCLONAL-ANTIBODIES | PARASITOLOGY | Epitope Mapping | Gene Products, env - immunology | HIV Antibodies - chemistry | Epitopes - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV Antibodies - immunology | HIV Antigens - immunology | Gene Products, env - chemistry | HIV-1 - chemistry | Antibodies, Neutralizing - chemistry | HIV Antigens - chemistry | Epitopes - chemistry | Competition | Acquired immune deficiency syndrome | Microscopy | AIDS | Vaccines | Grants | Experiments
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9. Full Text Antibodies to a conformational epitope on gp41 neutralize HIV-1 by destabilizing the Env spike
by Lee, Jeong Hyun and Leaman, Daniel P and Kim, Arthur S and Torrents de la Peña, Alba and Sliepen, Kwinten and Yasmeen, Anila and Derking, Ronald and Ramos, Alejana and de Taeye, Steven W and Ozorowski, Gabriel and Klein, Florian and Burton, Dennis R and Nussenzweig, Michel C and Poignard, Pascal and Moore, John P and Klasse, Per Johan and Sanders, Rogier W and Zwick, Michael B and Wilson, Ian A and Ward, Anew B and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature communications, ISSN 2041-1723, 2015, Volume 6, Issue 1, p. 8167
The recent identification of three broadly neutralizing antibodies (bnAbs) against gp120-gp41 interface epitopes has expanded the targetable surface on the... 
PROXIMAL EXTERNAL-REGION | POTENT NEUTRALIZATION | BROAD NEUTRALIZATION | RECOGNITION | TRIMERS | MULTIDISCIPLINARY SCIENCES | ENVELOPE | VACCINE | BINDING-SITE | CRYO-EM STRUCTURE | DEPENDENT EPITOPE | Epitope Mapping | HIV Envelope Protein gp41 - immunology | Humans | Models, Molecular | Crystallography, X-Ray | Epitopes | Cryoelectron Microscopy | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV Antibodies - immunology | Immunoglobulin G - immunology | Computer Simulation | HEK293 Cells | Protein Conformation | Immunoglobulin Fab Fragments - immunology | Antibodies, Neutralizing | HIV-1 | Immunoglobulin G | HIV Antibodies | Biochemistry, Molecular Biology | HIV Envelope Protein gp120 | HIV Envelope Protein gp41 | Life Sciences | Biomolecules | Immunoglobulin Fab Fragments
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10. Full Text Presenting native-like HIV-1 envelope trimers on ferritin nanoparticles improves their immunogenicity
by Sliepen, Kwinten and Ozorowski, Gabriel and Burger, Judith A and van Montfort, Thijs and Stunnenberg, Melissa and Labranche, Celia and Montefiori, David C and Moore, John P and Ward, Anew B and Sanders, Rogier W
Retrovirology, ISSN 1742-4690, 2015, Volume 12, Issue 1, p. 82
Background: Presenting vaccine antigens in particulate form can improve their immunogenicity by enhancing B cell activation. Findings: We describe... 
HIV-1 | Nanoparticles | BG505 | Ferritin | SOSIP | Vaccine | Envelope glycoprotein | VIROLOGY | GLYCOPROTEIN COMPLEX | GP41 | DEPENDENT EPITOPE | VACCINES | Rabbits | Immunization | env Gene Products, Human Immunodeficiency Virus - immunology | Ferritins - immunology | Humans | Protein Multimerization | AIDS Vaccines - immunology | AIDS Vaccines - chemistry | HIV-1 - immunology | Animals | Antibodies, Neutralizing - biosynthesis | HIV-1 - chemistry | HIV Antibodies - biosynthesis | Female | Mice | env Gene Products, Human Immunodeficiency Virus - chemistry | Viral antibodies | Antigens | AIDS vaccines | Immune response | Antibodies | Air pollution | HIV (Viruses)
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11. Full Text Improving the Immunogenicity of Native-like HIV-1 Envelope Trimers by Hyperstabilization
by Torrents de la Peña, Alba and Julien, Jean-Philippe and de Taeye, Steven W and Garces, Fernando and Guttman, Miklos and Ozorowski, Gabriel and Pritchard, Laura K and Behrens, Anna-Janina and Go, Eden P and Burger, Judith A and Schermer, Edith E and Sliepen, Kwinten and Ketas, Thomas J and Pugach, Pavel and Yasmeen, Anila and Cottrell, Christopher A and Torres, Jonathan L and Vavourakis, Charlotte D and van Gils, Marit J and LaBranche, Celia and Montefiori, David C and Desaire, Heather and Crispin, Max and Klasse, Per Johan and Lee, Kelly K and Moore, John P and Ward, Andrew B and Wilson, Ian A and Sanders, Rogier W and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Cell Reports, ISSN 2211-1247, 08/2017, Volume 20, Issue 8, pp. 1805 - 1817
The production of native-like recombinant versions of the HIV-1 envelope glycoprotein (Env) trimer requires overcoming the natural flexibility and instability... 
TARGET | DISULFIDE BONDS | BROADLY NEUTRALIZING ANTIBODIES | GLYCOPROTEIN COMPLEX | GLYCOSYLATION | CRYO-EM STRUCTURE | CELL BIOLOGY
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