Articles

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (172) 172
Publication (35) 35
Newspaper Article (6) 6
Book / eBook (2) 2
Magazine Article (2) 2
Paper (2) 2
Book Chapter (1) 1
Conference Proceeding (1) 1
Trade Publication Article (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (36) 36
humans (28) 28
agronomy (22) 22
hiv-1 - immunology (17) 17
article (16) 16
hiv (16) 16
hadron-hadron scattering (15) 15
antibodies (14) 14
antibodies, neutralizing - immunology (14) 14
hiv antibodies - immunology (14) 14
vaccines (14) 14
human immunodeficiency virus--hiv (12) 12
immunology (12) 12
viral antibodies (12) 12
analysis (11) 11
cell biology (11) 11
immunoglobulins (11) 11
medical research (11) 11
viruses (11) 11
animals (10) 10
female (10) 10
research (10) 10
agriculture (9) 9
agriculture, multidisciplinary (9) 9
aids vaccines - immunology (9) 9
experiment (9) 9
growth (9) 9
hiv infections - immunology (9) 9
hiv-1 (9) 9
medicine, experimental (9) 9
micropropagation (9) 9
recognition (9) 9
tissue culture (9) 9
top physics (9) 9
vaccine (9) 9
biochemistry & molecular biology (8) 8
biotechnology & applied microbiology (8) 8
immunization (8) 8
immunodeficiency-virus type-1 (8) 8
male (8) 8
maturation (8) 8
microscopy (8) 8
neutralization (8) 8
neutralizing (8) 8
aids vaccines (7) 7
binding sites (7) 7
env gene products, human immunodeficiency virus - immunology (7) 7
health aspects (7) 7
high energy physics (7) 7
monoclonal-antibodies (7) 7
orchidaceae (7) 7
physical sciences (7) 7
usage (7) 7
virology (7) 7
amino acid sequence (6) 6
anatomy (6) 6
antigens (6) 6
b-lymphocytes - immunology (6) 6
biology (6) 6
broad (6) 6
crystal-structure (6) 6
guinea pigs (6) 6
hiv envelope protein gp120 - immunology (6) 6
identification (6) 6
micropropagação (6) 6
models, molecular (6) 6
peptides (6) 6
phenomenology (6) 6
physics of elementary particles and fields (6) 6
plants (6) 6
protein conformation (6) 6
studies (6) 6
adult (5) 5
antigenic determinants (5) 5
biophysics (5) 5
breadth (5) 5
broadly neutralizing antibody (5) 5
child (5) 5
env gene products, human immunodeficiency virus - chemistry (5) 5
envelope glycoprotein (5) 5
epitopes - immunology (5) 5
fysik (5) 5
immunogen design (5) 5
infections (5) 5
lineage (5) 5
medicine, research & experimental (5) 5
natural sciences (5) 5
naturvetenskap (5) 5
physics (5) 5
potent neutralization (5) 5
protein binding (5) 5
protein multimerization (5) 5
trimers (5) 5
vaccination (5) 5
vaccine design (5) 5
acquired immune deficiency syndrome--aids (4) 4
antibodies, neutralizing - chemistry (4) 4
antibodies, neutralizing - metabolism (4) 4
antibody (4) 4
b cell ontogeny (4) 4
more...
Library Location Library Location
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text Identification of a CD4-Binding-Site Antibody to HIV that Evolved Near-Pan Neutralization Breadth
by Huang, Jinghe and Kang, Byong H and Ishida, Elise and Zhou, Tongqing and Griesman, Trevor and Sheng, Zizhang and Wu, Fan and Doria-Rose, Nicole A and Zhang, Baoshan and McKee, Krisha and O’Dell, Sijy and Chuang, Gwo-Yu and Druz, Aliaksandr and Georgiev, Ivelin S and Schramm, Chaim A and Zheng, Anqi and Joyce, M. Gordon and Asokan, Mangaiarkarasi and Ransier, Amy and Darko, Sam and Migueles, Stephen A and Bailer, Robert T and Louder, Mark K and Alam, S. Munir and Parks, Robert and Kelsoe, Garnett and Von Holle, Tarra and Haynes, Barton F and Douek, Daniel C and Hirsch, Vanessa and Seaman, Michael S and Shapiro, Lawrence and Mascola, John R and Kwong, Peter D and Connors, Mark and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Immunity, ISSN 1074-7613, 11/2016, Volume 45, Issue 5, pp. 1108 - 1121
Detailed studies of the broadly neutralizing antibodies (bNAbs) that underlie the best available examples of the humoral immune response to HIV are providing... 
vaccine | envelope | antibody | HIV | immunotherapy | neutralizing | CD4-binding site | prophylaxis | resistance | structure | EVOLUTION | POTENCY | ENVELOPE | GLYCANS | PATTERNS | GLYCOPROTEIN | IMMUNOLOGY | MATURATION | TYPE-1 INFECTION | LINEAGE | ESCAPE | CD4-Positive T-Lymphocytes - immunology | HIV Envelope Protein gp120 - immunology | Antibody Specificity | HIV Infections - immunology | Antibodies, Neutralizing - immunology | Binding Sites, Antibody - immunology | HIV-1 - immunology | HIV Antibodies - immunology | Cell Separation | Humans | Viral antibodies | Allergy | Polysaccharides | Analysis | Communicable diseases | Antibodies | HIV (Viruses) | Allergic reaction | Medical research | Immunotherapy | Medicine, Experimental | Immunoglobulins | Cloning | Viruses | Glycoproteins | Vaccines | Patients | Proteins | Plasmids | Light | Phylogenetics | Bioinformatics | Binding sites | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Full Text Structural Repertoire of HIV-1-Neutralizing Antibodies Targeting the CD4 Supersite in 14 Donors
by Zhou, Tongqing and Lynch, Rebecca M and Chen, Lei and Acharya, Priyamvada and Wu, Xueling and Doria-Rose, Nicole A and Joyce, M. Gordon and Lingwood, Daniel and Soto, Cinque and Bailer, Robert T and Ernandes, Michael J and Kong, Rui and Longo, Nancy S and Louder, Mark K and McKee, Krisha and O’Dell, Sijy and Schmidt, Stephen D and Tran, Lillian and Yang, Yongping and Yang, An-Suei and Yang, Zhongjia and Druz, Aliaksandr and Luongo, Timothy S and Moquin, Stephanie and Srivatsan, Sanjay and Zhang, Baoshan and Zheng, Anqi and Pancera, Marie and Kirys, Tatsiana and Georgiev, Ivelin S and Gindin, Tatyana and Peng, Hung-Pin and Mullikin, James C and Gray, Matthew D and Stamatatos, Leonidas and Burton, Dennis R and Koff, Wayne C and Cohen, Myron S and Haynes, Barton F and Casazza, Joseph P and Connors, Mark and Corti, Davide and Lanzavecchia, Antonio and Sattentau, Quentin J and Weiss, Robin A and West, Anthony P and Bjorkman, Pamela J and Scheid, Johannes F and Nussenzweig, Michel C and Shapiro, Lawrence and Mascola, John R and Kwong, Peter D and NISC Comparative Sequencing and NISC Comparative Sequencing Program and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Cell, ISSN 0092-8674, 06/2015, Volume 161, Issue 6, pp. 1280 - 1292
The site on the HIV-1 gp120 glycoprotein that binds the CD4 receptor is recognized by broadly reactive antibodies, several of which neutralize over 90% of... 
COMPLEX | POTENT NEUTRALIZATION | NEUTRALIZING HIV-1 ANTIBODY | RECOGNITION | CD4-BINDING SITE | DETERMINANTS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BROAD | MONOCLONAL-ANTIBODIES | MATURATION | CELL BIOLOGY | Amino Acid Sequence | Antibodies, Viral - metabolism | Humans | Antibodies, Neutralizing - metabolism | Models, Molecular | Molecular Sequence Data | HIV Envelope Protein gp120 - metabolism | HIV Envelope Protein gp120 - immunology | Sequence Alignment | B-Lymphocytes - immunology | HIV-1 - physiology | Antibodies, Neutralizing - chemistry | Antibodies, Viral - chemistry | HIV Envelope Protein gp120 - chemistry | Complementarity Determining Regions | CD4 Antigens - metabolism | Epitopes, B-Lymphocyte | Viral antibodies | Antibodies | HIV (Viruses) | Structure | Analysis | Crystals
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
3. Full Text Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env
by Do Kwon, Young and Pancera, Marie and Acharya, Priyamvada and Georgiev, Ivelin S and Crooks, Emma T and Gorman, Jason and Joyce, M Gordon and Guttman, Miklos and Ma, Xiaochu and Narpala, Sandeep and Soto, Cinque and Terry, Daniel S and Yang, Yongping and Zhou, Tongqing and Ahlsen, Goran and Bailer, Robert T and Chambers, Michael and Chuang, Gwo-Yu and Doria-Rose, Nicole A and Druz, Aliaksandr and Hallen, Mark A and Harned, Adam and Kirys, Tatsiana and Louder, Mark K and O'Dell, Sijy and Ofek, Gilad and Osawa, Keiko and Prabhakaran, Madhu and Sastry, Mallika and Stewart-Jones, Guillaume B E and Stuckey, Jonathan and Thomas, Paul V and Tittley, Tishina and Williams, Constance and Zhang, Baoshan and Zhao, Hong and Zhou, Zhou and Donald, Bruce R and Lee, Lawrence K and Zolla-Pazner, Susan and Baxa, Ulrich and Schön, Arne and Freire, Ernesto and Shapiro, Lawrence and Lee, Kelly K and Arthos, James and Munro, James B and Blanchard, Scott C and Mothes, Walther and Binley, James M and McDermott, Adrian B and Mascola, John R and Kwong, Peter D and National Inst. of Health (NIH), Bethesda, MD (United States)
Nature Structural and Molecular Biology, ISSN 1545-9993, 07/2015, Volume 22, Issue 7, pp. 522 - 531
As the sole viral antigen on the HIV-1-virion surface, trimeric Env is a focus of vaccine efforts. Here we present the structure of the ligand-free HIV-1-Env... 
PROTEIN | BROAD NEUTRALIZATION | NEUTRALIZING ANTIBODY | BIOCHEMISTRY & MOLECULAR BIOLOGY | HUMAN MONOCLONAL-ANTIBODY | ENVELOPE GLYCOPROTEIN COMPLEX | FUSION GLYCOPROTEIN | GP120 | CELL BIOLOGY | BIOPHYSICS | IMMUNODEFICIENCY-VIRUS TYPE-1 | BINDING-SITE | EPITOPES | CD4 Antigens - immunology | env Gene Products, Human Immunodeficiency Virus - immunology | HIV Infections - virology | Humans | Protein Multimerization | Models, Molecular | Crystallography, X-Ray | Virus Internalization | Epitopes - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV-1 - physiology | HIV Antibodies - immunology | HIV-1 - chemistry | HEK293 Cells | Protein Conformation | env Gene Products, Human Immunodeficiency Virus - chemistry | Antigens | Vaccines | Molecular biology | Human immunodeficiency virus--HIV | Crystal structure | X-ray crystallography | Computational biology and bioinformatics | Immunology | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES | Viral membrane fusion
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
4. Full Text Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody
by Kong, Rui and Xu, Kai and Zhou, Tongqing and Acharya, Priyamvada and Lemmin, Thomas and Liu, Kevin and Ozorowski, Gabriel and Soto, Cinque and Taft, Justin D and Bailer, Robert T and Cale, Evan M and Chen, Lei and Choi, Chang W and Chuang, Gwo-Yu and Doria-Rose, Nicole A and Druz, Aliaksandr and Georgiev, Ivelin S and Gorman, Jason and Huang, Jinghe and Joyce, M. Gordon and Louder, Mark K and Ma, Xiaochu and McKee, Krisha and O'Dell, Sijy and Pancera, Marie and Yang, Yongping and Blanchard, Scott C and Mothes, Walther and Burton, Dennis R and Koff, Wayne C and Connors, Mark and Ward, Andrew B and Kwong, Peter D and Mascola, John R and National Inst. of Health (NIH), Bethesda, MD (United States)
Science, ISSN 0036-8075, 05/2016, Volume 352, Issue 6287, pp. 828 - 833
The HIV-1 fusion peptide, comprising 15 to 20 hydrophobic residues at the N terminus of the Env-gp41 subunit, is a critical component of the virus-cell entry... 
Immunodominant Epitopes - immunology | Amino Acid Sequence | HIV Envelope Protein gp41 - immunology | Humans | Peptides - immunology | AIDS Vaccines - immunology | Molecular Sequence Data | Antibodies, Neutralizing - ultrastructure | Crystallography, X-Ray | Viral Fusion Proteins - immunology | Virus Internalization | Antibodies, Neutralizing - isolation & purification | HIV Envelope Protein gp120 - immunology | HIV-1 - immunology | Antibodies, Viral - ultrastructure | B-Lymphocytes - immunology | Antibodies, Neutralizing - chemistry | Antibodies, Viral - chemistry | B-Lymphocytes - virology | Hydrophobic and Hydrophilic Interactions | Protein Conformation | Viral antibodies | Peptides | Antibodies | Host-virus relationships | HIV (Viruses) | Observations | Health aspects | Immunoglobulins | Human immunodeficiency virus--HIV | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
5. Full Text Structures of HIV-1 Env V1V2 with broadly neutralizing antibodies reveal commonalities that enable vaccine design
by Gorman, Jason and Soto, Cinque and Yang, Max M and Davenport, Thaddeus M and Guttman, Miklos and Bailer, Robert T and Chambers, Michael and Chuang, Gwo-Yu and Dekosky, Brandon J and Doria-Rose, Nicole A and Druz, Aliaksandr and Ernandes, Michael J and Georgiev, Ivelin S and Jarosinski, Marissa C and Joyce, M. Gordon and Lemmin, Thomas M and Leung, Sherman and Louder, Mark K and McDaniel, Jonathan R and Narpala, Sandeep and Pancera, Marie and Stuckey, Jonathan and Wu, Xueling and Yang, Yongping and Zhang, Baoshan and Zhou, Tongqing and Mullikin, James C and Baxa, Ulrich and Georgiou, George and McDermott, Adrian B and Bonsignori, Mattia and Haynes, Barton F and Moore, Penny L and Morris, Lynn and Lee, Kelly K and Shapiro, Lawrence and Mascola, John R and Kwong, Peter D and NISC Comparative Sequencing and NISC Comparative Sequencing Program and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature Structural and Molecular Biology, ISSN 1545-9993, 01/2016, Volume 23, Issue 1, pp. 81 - 90
Broadly neutralizing antibodies (bNAbs) against HIV-1 Env V1V2 arise in multiple donors. However, atomic-level interactions had previously been determined only... 
SITE | REPERTOIRE | POTENT NEUTRALIZATION | RECOGNITION | HIV-1-NEUTRALIZING ANTIBODIES | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENVELOPE PROTEIN | IMMUNOGEN DESIGN | MATURATION | CELL BIOLOGY | TRIMER | BIOPHYSICS | Cell Line | env Gene Products, Human Immunodeficiency Virus - immunology | Humans | AIDS Vaccines - immunology | Models, Molecular | Crystallography, X-Ray | HIV Antibodies - chemistry | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV Antibodies - immunology | HIV-1 - chemistry | Antibodies, Neutralizing - chemistry | Protein Binding | Protein Conformation | env Gene Products, Human Immunodeficiency Virus - chemistry | Prevention | Development and progression | Care and treatment | Research | HIV infection | Immunoglobulins | Immunology | Vaccines | Human immunodeficiency virus--HIV
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text Quantification of the Impact of the HIV-1-Glycan Shield on Antibody Elicitation
by Zhou, Tongqing and Doria-Rose, Nicole A and Cheng, Cheng and Stewart-Jones, Guillaume B.E and Chuang, Gwo-Yu and Chambers, Michael and Druz, Aliaksandr and Geng, Hui and McKee, Krisha and Kwon, Young Do and O’Dell, Sijy and Sastry, Mallika and Schmidt, Stephen D and Xu, Kai and Chen, Lei and Chen, Rita E and Louder, Mark K and Pancera, Marie and Wanninger, Timothy G and Zhang, Baoshan and Zheng, Anqi and Farney, S. Katie and Foulds, Kathryn E and Georgiev, Ivelin S and Joyce, M. Gordon and Lemmin, Thomas and Narpala, Sandeep and Rawi, Reda and Soto, Cinque and Todd, John-Paul and Shen, Chen-Hsiang and Tsybovsky, Yaroslav and Yang, Yongping and Zhao, Peng and Haynes, Barton F and Stamatatos, Leonidas and Tiemeyer, Michael and Wells, Lance and Scorpio, Diana G and Shapiro, Lawrence and McDermott, Adrian B and Mascola, John R and Kwong, Peter D and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Cell Reports, ISSN 2211-1247, 04/2017, Volume 19, Issue 4, pp. 719 - 732
While the HIV-1-glycan shield is known to shelter Env from the humoral immune response, its quantitative impact on antibody elicitation has been unclear. Here,... 
HIV-1 | glycomics | immunogen design | crystal structure | targeted deglycosylation | glycan shield | vaccine design | CD4-binding site | immunogenicity | envelope glycoprotein | POTENT | NEUTRALIZING ANTIBODIES | RECOGNITION | HIV-1 ENVELOPE TRIMERS | STRUCTURAL BASIS | RECEPTOR | BROAD | GLYCOPROTEIN | GP120 | IDENTIFICATION | CELL BIOLOGY | HIV Antibodies - blood | Antibody Specificity | env Gene Products, Human Immunodeficiency Virus - immunology | Humans | Crystallography, X-Ray | env Gene Products, Human Immunodeficiency Virus - metabolism | Macaca mulatta | Epitopes - immunology | Polysaccharides - deficiency | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | Protein Structure, Quaternary | Binding Sites | env Gene Products, Human Immunodeficiency Virus - chemistry | HIV-1 - metabolism | Immunization | Guinea Pigs | Glycosylation | Polysaccharides - immunology | Molecular Dynamics Simulation | Polysaccharides - metabolism | Animals | CD4 Antigens - chemistry | Antibodies, Neutralizing - blood | CD4 Antigens - metabolism | BASIC BIOLOGICAL SCIENCES
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text Virus-like Particles Identify an HIV V1V2 Apex-Binding Neutralizing Antibody that Lacks a Protruding Loop
by Cale, Evan M and Gorman, Jason and Radakovich, Nathan A and Crooks, Ema T and Osawa, Keiko and Tong, Tommy and Li, Jiaqi and Nagarajan, Raju and Ozorowski, Gabriel and Ambrozak, David R and Asokan, Mangai and Bailer, Robert T and Bennici, Anthony K and Chen, Xuejun and Doria-Rose, Nicole A and Druz, Aliaksandr and Feng, Yu and Joyce, M. Gordon and Louder, Mark K and O’Dell, Sijy and Oliver, Courtney and Pancera, Marie and Connors, Mark and Hope, Thomas J and Kepler, Thomas B and Wyatt, Richard T and Ward, Andrew B and Georgiev, Ivelin S and Kwong, Peter D and Mascola, John R and Binley, James M
Immunity, ISSN 1074-7613, 05/2017, Volume 46, Issue 5, pp. 777 - 791.e10
Most HIV-1-specific neutralizing antibodies isolated to date exhibit unusual characteristics that complicate their elicitation. Neutralizing antibodies that... 
V1V2 | antibody | bnAb | HIV | trimer | neutralization | glycan shield | VLP | B cell ontogeny | CDRH3 | vaccine-design template | NAb | CONFORMATIONAL EPITOPE | RECOGNITION | BROAD | FUSION PEPTIDE | IMMUNOLOGY | MONOCLONAL-ANTIBODIES | IDENTIFICATION | REVEAL | ELECTRON-MICROSCOPE | QUATERNARY | ENVELOPE TRIMERS | env Gene Products, Human Immunodeficiency Virus - immunology | Humans | Protein Multimerization | Antibodies, Neutralizing - metabolism | Vaccines, Virus-Like Particle - metabolism | Phylogeny | HIV Envelope Protein gp120 - metabolism | Vaccines, Virus-Like Particle - chemistry | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | Complementarity Determining Regions - chemistry | Peptide Fragments - immunology | Protein Interaction Domains and Motifs | HIV Envelope Protein gp120 - chemistry | Binding Sites | B-Lymphocytes - metabolism | HIV Antibodies - metabolism | Amino Acid Sequence | Peptide Fragments - metabolism | HIV Infections - virology | Models, Molecular | HIV Antibodies - chemistry | HIV-1 - immunology | Peptide Fragments - chemistry | B-Lymphocytes - immunology | Antibodies, Neutralizing - chemistry | Complementarity Determining Regions - immunology | Protein Binding | Protein Conformation | Vaccines, Virus-Like Particle - immunology | Viral antibodies | Medical research | Crystals | Medicine, Experimental | Antibodies | Research institutes | Structure | HIV (Viruses) | Immunoglobulins | Recombination | Particulates | Viruses | Vaccines | Virus-like particles | Lymphocytes B | Plasmids | Human immunodeficiency virus--HIV | Probes | Binding sites | Crystal structure
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. Full Text Strategies to guide the antibody affinity maturation process
by Doria-Rose, Nicole A and Joyce, M Gordon
Current Opinion in Virology, ISSN 1879-6257, 04/2015, Volume 11, pp. 137 - 147
Antibodies with protective activity are critical for vaccine efficacy. Affinity maturation increases antibody activity through multiple rounds of somatic... 
B-CELL RECEPTORS | ENVELOPE GLYCOPROTEIN TRIMERS | RECEPTOR-BINDING SITE | POTENT NEUTRALIZATION | VIROLOGY | HIV-1 ENVELOPE | STRUCTURAL BASIS | BROADLY NEUTRALIZING ANTIBODIES | IMMUNODEFICIENCY-VIRUS TYPE-1 | GERMINAL CENTER | HUMAN MONOCLONAL-ANTIBODIES | Viral Vaccines - isolation & purification | HIV-1 - immunology | Vaccination - methods | Humans | Antibodies, Viral - immunology | Antibody Affinity | Drug Discovery - methods | Viral Vaccines - immunology | Orthomyxoviridae - immunology | HIV-1 | influenza | Influenza Hemagglutinin | germinal center | HIV envelope glycoprotein | broadly neutralizing antibodies | structure-based design | vaccine | initial recombinant | somatic hypermutation | nanoparticles | immunization strategies | viral evolution | B cell ontogeny
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
9. Full Text Somatic Hypermutation-Induced Changes in the Structure and Dynamics of HIV-1 Broadly Neutralizing Antibodies
by Davenport, Thaddeus M and Gorman, Jason and Joyce, M. Gordon and Zhou, Tongqing and Soto, Cinque and Guttman, Miklos and Moquin, Stephanie and Yang, Yongping and Zhang, Baoshan and Doria-Rose, Nicole A and Hu, Shiu-Lok and Mascola, John R and Kwong, Peter D and Lee, Kelly K and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Structure, ISSN 0969-2126, 08/2016, Volume 24, Issue 8, pp. 1346 - 1357
Antibody somatic hypermutation (SHM) and affinity maturation enhance antigen recognition by modifying antibody paratope structure to improve its... 
PROTEIN DYNAMICS | DESIGN | EVOLUTION | BIOPHYSICS | RECOGNITION | AFFINITY MATURATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | FRAMEWORK | BINDING-SITE | DIVERSITY | FAMILY | CELL BIOLOGY | Viral antibodies | Antibodies | HIV (Viruses) | Mass spectrometry | Antigenic determinants | Crystals | Structure
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights