Articles

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (24) 24
humans (13) 13
hiv-1 - immunology (11) 11
animals (10) 10
env gene products, human immunodeficiency virus - immunology (9) 9
vaccines (9) 9
antibodies, neutralizing - immunology (8) 8
article (8) 8
cryo-em structure (8) 8
crystal-structure (8) 8
immunization (8) 8
immunodeficiency-virus type-1 (8) 8
virology (8) 8
affinity maturation (6) 6
antibodies (6) 6
broadly neutralizing antibodies (6) 6
hiv (6) 6
monoclonal-antibodies (6) 6
protein multimerization (6) 6
viruses (6) 6
antigens (5) 5
binding-site (5) 5
dependent epitope (5) 5
env gene products, human immunodeficiency virus - chemistry (5) 5
env trimers (5) 5
glycoprotein complex (5) 5
hiv antibodies - immunology (5) 5
hiv infections - immunology (5) 5
immunoglobulin g (5) 5
immunoglobulins (5) 5
models, molecular (5) 5
aids vaccines - immunology (4) 4
analysis (4) 4
antigenic determinants (4) 4
binding sites (4) 4
biochemistry & molecular biology (4) 4
cell biology (4) 4
epitope mapping (4) 4
epitopes - immunology (4) 4
gp120 (4) 4
hiv-1 - genetics (4) 4
human immunodeficiency virus--hiv (4) 4
immunology (4) 4
mice (4) 4
microbiology (4) 4
multidisciplinary sciences (4) 4
physiological aspects (4) 4
potent (4) 4
research (4) 4
vaccine (4) 4
vaccines and antiviral agents (4) 4
virus diseases (4) 4
aids vaccines (3) 3
antibodies, neutralizing (3) 3
biology (3) 3
conformation (3) 3
cryoelectron microscopy (3) 3
disulfide bonds (3) 3
envelope trimers (3) 3
epitopes - chemistry (3) 3
glycoprotein (3) 3
glycosylation (3) 3
hek293 cells (3) 3
hiv antigens - immunology (3) 3
hiv-1 (3) 3
hiv-1 - chemistry (3) 3
human immunodeficiency virus (3) 3
immunogen design (3) 3
immunologic diseases. allergy (3) 3
neutralizing (3) 3
protein conformation (3) 3
protein design (3) 3
proteins (3) 3
recognition (3) 3
research article (3) 3
solubility (3) 3
target (3) 3
trimers (3) 3
usage (3) 3
vaccine development (3) 3
6-helix bundle (2) 2
activation (2) 2
antibodies, neutralizing - biosynthesis (2) 2
antibodies, neutralizing - chemistry (2) 2
antibodies, neutralizing - isolation & purification (2) 2
antibody specificity (2) 2
b-cell-lineage (2) 2
b-lymphocytes - immunology (2) 2
binding (2) 2
biochemistry (2) 2
broad neutralization (2) 2
competition (2) 2
conformational epitope (2) 2
crystallography, x-ray (2) 2
cysteine residues (2) 2
design (2) 2
development and progression (2) 2
electron microscopy (2) 2
env gene products, human immunodeficiency virus - genetics (2) 2
env gene products, human immunodeficiency virus - metabolism (2) 2
more...
Library Location Library Location
Library Location Library Location
X
Sort by Item Count (A-Z)
Filter by Count
Pontifical Inst. Mediaeval Studies - Reference (2) 2
UTL at Downsview - May be requested (2) 2
Architecture Landscape (Shore + Moffat) - Stacks (1) 1
Collection Dvlpm't (Acquisitions) - Cancelled Order (1) 1
Pontifical Inst. Mediaeval Studies - Library use only (1) 1
Robarts - Stacks (1) 1
Royal Ontario Museum - Stacks (1) 1
more...
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text The Ligands for Human IgG and Their Effector Functions
by de Taeye, Steven W and Rispens, Theo and Vidarsson, Gestur
Antibodies, ISSN 2073-4468, 04/2019, Volume 8, Issue 2, p. 30
Activation of the humoral immune system is initiated when antibodies recognize an antigen and trigger effector functions through the interaction with Fc... 
Neonates | Antigens | Immunoglobulins | Laboratories | Medical treatment | Immunoglobulin G | Antibodies | Cytotoxicity | Glycosylation | Immune response (humoral) | Complement component C1 | Fc receptors | Receptors | Immunotherapy | Ligands | Autoimmune diseases | Immune system | IgG | allotypes | glycosylation | Fc effector molecules
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Full Text HIV-1 Envelope Trimer Design and Immunization Strategies To Induce Broadly Neutralizing Antibodies
by de Taeye, Steven W and Moore, John P and Sanders, Rogier W
Trends in Immunology, ISSN 1471-4906, 2016, Volume 37, Issue 3, pp. 221 - 232
The identification of multiple broadly neutralizing antibodies (bNAbs) against the HIV-1 envelope glycoprotein (Env) trimer has facilitated its structural... 
Allergy and Immunology | B-CELL RECEPTORS | PROXIMAL EXTERNAL-REGION | CONFORMATIONAL EPITOPE | GLYCOPROTEIN TRIMERS | AFFINITY MATURATION | CRYSTAL-STRUCTURE | IMMUNODEFICIENCY-VIRUS TYPE-1 | BINDING-SITE | IMMUNOGEN DESIGN | IMMUNOLOGY | DEPENDENT EPITOPE | Antibodies, Neutralizing | Epitope Mapping | HIV Infections - immunology | HIV Infections - prevention & control | HIV-1 - immunology | Animals | env Gene Products, Human Immunodeficiency Virus - immunology | Humans | Protein Multimerization | AIDS Vaccines - immunology | Disease Models, Animal | Antigens | Development and progression | Immunization | HIV (Viruses) | Analysis | Proteins | Immunoglobulins | Viruses | Infections | Vaccines | Viral infections | Binding sites | HIV-1 vaccine development | Immunogen design | Native-like trimers | Broadly neutralizing antibodies
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
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
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
4. 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
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
5. Full Text Design and structure of two HIV-1 clade C SOSIP.664 trimers that increase the arsenal of native-like Env immunogens
by Jean-Philippe Julien and Jeong Hyun Lee and Gabriel Ozorowski and Yuanzi Hua and Alba Torrents de la Peña and Steven W. de Taeye and Travis Nieusma and Albert Cupo and Anila Yasmeen and Michael Golabek and Pavel Pugach and P. J. Klasse and John P. Moore and Rogier W. Sanders and Andrew B. Ward and Ian A. Wilson
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2015, Volume 112, Issue 38, pp. 11947 - 11952
A key challenge in the quest toward an HIV-1 vaccine is design of immunogens that can generate a broadly neutralizing antibody (bnAb) response against the... 
Antigenic diversity | HIV-1 envelope | Clade C trimers | HIV immunogens | Neutralizing antibodies | ANTIBODIES | clade C trimers | RECOGNITION | antigenic diversity | MULTIDISCIPLINARY SCIENCES | neutralizing antibodies | VULNERABILITY | GP120 | QUATERNARY | IMMUNODEFICIENCY-VIRUS TYPE-1 | CRYO-EM STRUCTURE | Temperature | env Gene Products, Human Immunodeficiency Virus - immunology | Humans | Protein Multimerization | Solubility | Models, Molecular | Negative Staining | Cryoelectron Microscopy | HIV-1 - immunology | HIV Antigens - immunology | Immunoglobulin Fab Fragments - chemistry | Drug Design | HIV Antigens - chemistry | Immunoglobulin Fab Fragments - immunology | Protein Stability | env Gene Products, Human Immunodeficiency Virus - chemistry | Complications and side effects | Care and treatment | Immunogenetics | Disease transmission | Analysis | Research | Vaccines | HIV infection | Health aspects | Biological Sciences
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text Elicitation of Robust Tier 2 Neutralizing Antibody Responses in Nonhuman Primates by HIV Envelope Trimer Immunization Using Optimized Approaches
by Pauthner, Matthias and Havenar-Daughton, Colin and Sok, Devin and Nkolola, Joseph P and Bastidas, Raiza and Boopathy, Archana V and Carnathan, Diane G and Chandrashekar, Abishek and Cirelli, Kimberly M and Cottrell, Christopher A and Eroshkin, Alexey M and Guenaga, Javier and Kaushik, Kirti and Kulp, Daniel W and Liu, Jinyan and McCoy, Laura E and Oom, Aaron L and Ozorowski, Gabriel and Post, Kai W and Sharma, Shailendra K and Steichen, Jon M and de Taeye, Steven W and Tokatlian, Talar and Torrents de la Peña, Alba and Butera, Salvatore T and LaBranche, Celia C and Montefiori, David C and Silvestri, Guido and Wilson, Ian A and Irvine, Darrell J and Sanders, Rogier W and Schief, William R and Ward, Andrew B and Wyatt, Richard T and Barouch, Dan H and Crotty, Shane and Burton, Dennis R
Immunity, ISSN 1074-7613, 06/2017, Volume 46, Issue 6, pp. 1073 - 1088.e6
The development of stabilized recombinant HIV envelope trimers that mimic the virion surface molecule has increased enthusiasm for a neutralizing antibody... 
rhesus macaques | NFL | Tfh cells | BG505 | HIV vaccine | SOSIP | germinal centers | GC B cells | nonhuman primates | protein design | TARGET | STANDARDIZED ASSESSMENTS | DESIGN | TFH CELLS | GLYCOPROTEIN COMPLEX | IMMUNODEFICIENCY-VIRUS TYPE-1 | ENV TRIMERS | IMMUNOLOGY | ESCAPE | Immunization | env Gene Products, Human Immunodeficiency Virus - immunology | Epitopes, B-Lymphocyte - chemistry | Germinal Center - immunology | Humans | Protein Multimerization | AIDS Vaccines - immunology | Cells, Cultured | Epitopes, B-Lymphocyte - immunology | HIV Infections - immunology | HIV-1 - immunology | Animals | Antibodies, Neutralizing - therapeutic use | Germinal Center - virology | Injections, Subcutaneous | HIV Infections - therapy | Primates | HIV Antibodies - therapeutic use | env Gene Products, Human Immunodeficiency Virus - chemistry | Antigens | AIDS vaccines | Usage | Analysis | Development and progression | HIV (Viruses) | B cells | Immunoglobulins | Trimers | Vaccines | Lymph nodes | Design | Human immunodeficiency virus--HIV | Neutralizing | Reaction kinetics | Monoclonal antibodies | Robustness | Mutation | Kinetics | Recombinant | Lymph | Resource
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text Murine Antibody Responses to Cleaved Soluble HIV-1 Envelope Trimers Are Highly Restricted in Specificity
by Hu, Joyce K and Crampton, Jordan C and Cupo, Albert and Ketas, Thomas and van Gils, Marit J and Sliepen, Kwinten and de Taeye, Steven W and Sok, Devin and Ozorowski, Gabriel and Deresa, Isaiah and Stanfield, Robyn and Ward, Anew B and Burton, Dennis R and Klasse, Per Johan and Sanders, Rogier W and Moore, John P and Crotty, Shane
Journal of virology, ISSN 0022-538X, 2015, Volume 89, Issue 20, pp. 10383 - 10398
Generating neutralizing antibodies (nAbs) is a major goal of many current HIV-1 vaccine efforts. To be of practical value, these nAbs must be both potent and... 
CENTER B-CELLS | MUCOSAL SHIV CHALLENGE | POTENT | VIROLOGY | GLYCOPROTEIN TRIMERS | BROADLY NEUTRALIZING ANTIBODIES | VACCINE | IMMUNODEFICIENCY-VIRUS TYPE-1 | FOLLICULAR HELPER-CELL | GERMINAL CENTER | MONOCLONAL-ANTIBODIES | Antibody Specificity | Epitope Mapping | HIV Infections - prevention & control | env Gene Products, Human Immunodeficiency Virus - immunology | Humans | Protein Multimerization | Epitopes - immunology | HIV Infections - immunology | env Gene Products, Human Immunodeficiency Virus - genetics | Immunoglobulin G - biosynthesis | HIV-1 - chemistry | Receptors, Antigen, B-Cell - chemistry | HEK293 Cells | Protein Engineering | HIV Antibodies - biosynthesis | env Gene Products, Human Immunodeficiency Virus - chemistry | Gene Expression | Immunization | HIV Infections - virology | Immunoglobulin G - chemistry | Solubility | Models, Molecular | Recombinant Proteins - chemistry | Antigens, Viral - chemistry | Recombinant Proteins - genetics | HIV-1 - genetics | HIV Antibodies - chemistry | Receptors, Antigen, B-Cell - immunology | Recombinant Proteins - administration & dosage | Antigens, Viral - immunology | HIV-1 - immunology | Animals | B-Lymphocytes - immunology | Recombinant Proteins - immunology | Antibodies, Neutralizing - biosynthesis | Antibodies, Neutralizing - chemistry | env Gene Products, Human Immunodeficiency Virus - administration & dosage | Protein Binding | Epitopes - chemistry | Mice
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. 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
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
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
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
10. Full Text HIV-1 anchor inhibitors and membrane fusion inhibitors target distinct but overlapping steps in virus entry
by Eggink, Dirk and Bontjer, Ilja and de Taeye, Steven W and Langedijk, Johannes P. M and Berkhout, Ben and Sanders, Rogier W
Journal of biological chemistry, ISSN 0021-9258, 2019, Volume 294, Issue 15, pp. 5736 - 5746
HIV-1 entry into cells is mediated by the envelope glycoprotein (Env) and represents an attractive target for therapeutic intervention. Two drugs that inhibit... 
inhibition mechanism | DOMAIN | human immunodeficiency virus (HIV) | 6-HELIX BUNDLE | BIOCHEMISTRY & MOLECULAR BIOLOGY | peptides | anchor inhibitor | TYPE-1 GP41 | EMERGENCE | ENFUVIRTIDE | PEPTIDE | membrane fusion | fusion peptide (FP) | fusion protein | antiviral drug | virus entry | RESISTANCE | INTERMEDIATE | drug resistance | MUTATIONS | PROMISCUOUS BINDING | Microbiology
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
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
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights