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1. The decision to discriminate
: a study of executive selection
by Quinn, Robert P and Tabor, Joyce M and Gordon, Laura K
1968, 162
Executives | Jews | United States | Employment | Discrimination in employment
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2. Full Text Intestinal UDP-glucuronosyltransferase as a potential target for the treatment and prevention of lymphatic filariasis
by Flynn, Alexander F and Joyce, M Gordon and Taylor, Rebekah T and Bennuru, Sasisekhar and Lindrose, Alyssa R and Sterling, Spencer L and Morris, C Paul and Nutman, Thomas B and Mitre, Edward
PLoS neglected tropical diseases, ISSN 1935-2735, 09/2019, Volume 13, Issue 9, p. e0007687
Lymphatic filariasis (LF), a morbid disease caused by the tissue-invasive nematodes Wuchereria bancrofti, Brugia malayi, and Brugia timori, affects millions of... 
Health sciences | Visualization | Immunoprecipitation | Endemic species | Populations | Immunoglobulin E | Infections | mRNA | Vaccines | Drug development | Tropical diseases | Proteins | Reduction | Intestine | Worms | Glucuronosyltransferase | Vector-borne diseases | Antigens | UDP-glucuronosyltransferase | Therapeutic applications | siRNA | Metabolism | Gene expression | Disease control | Survival | Medicine | Infectious diseases | Albendazole | Filariasis | Nematodes
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3. 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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4. Full Text Germline VRC01 antibody recognition of a modified clade C HIV-1 envelope trimer and a glycosylated HIV-1 gp120 core
by Borst, Andrew J and Borst, Andrew J and Weidle, Connor E and Gray, Matthew D and Frenz, Brandon and Snijder, Joost and Joyce, M Gordon and Joyce, M. Gordon and Georgiev, Ivelin S and Stewart-Jones, Guillaume B. E and Stewart-Jones, Guillaume Be and Kwong, Peter D and Kwong, Peter D and McGuire, Andrew T and Dimaio, Frank and Stamatatos, Leonidas and Stamatatos, Leonidas and Pancera, Marie and Pancera, Marie and Veesler, David and Veesler, David
eLife, ISSN 2050-084X, 11/2018, Volume 7
VRC01 broadly neutralizing antibodies (bnAbs) target the CD4-binding site (CD4 ) of the human immunodeficiency virus-1 (HIV-1) envelope glycoprotein (Env).... 
crystallography | fusion protein | HIV envelope | cryoEM | HIV | glycan shield | structural biology | VRC01 | molecular biophysics | virus | Amino Acid Sequence | HIV-1 - metabolism | Antibodies - metabolism | Protein Structure, Secondary | Antibodies - chemistry | Humans | Protein Multimerization | Antibodies - ultrastructure | Models, Molecular | Glycosylation | HIV Envelope Protein gp120 - metabolism | Polysaccharides - metabolism | Immunoglobulin Fab Fragments - chemistry | HEK293 Cells | Protein Binding | Germ Cells - metabolism | Immunoglobulin G - metabolism | Viral antibodies | Antibodies | Physiological aspects | Viral envelopes | Glycoproteins | HIV (Viruses) | Medical research | Immunoglobulins | Immunoprecipitation | Trimers | Oligosaccharides | Electron microscopy | Crystallography | CD4 antigen | X-ray crystallography | Proteins | Human immunodeficiency virus--HIV | Software | Mutation | Glycoprotein gp120 | Binding sites
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5. WOCE operations manual. Volume 3, The observational programme. Section 3.1, WOCE hydrographic programme. Part 3.1.2, Requirements for WHP data reporting
by Joyce, T and Corry, C. Stalcup, M and Gordon, L and Huyer, A and Jenkins, W and Jennings, J and Key, R and Knapp, G and MacMurray, C and Millard, R and Stanley, R and Toole, J and Van Woy, R and Weiss, R and World Ocean Circulation Experiment
1991, WHPO publication, Volume 90-1., v.
This publication describes procedures for reporting hydrographic and tracer data to the International WOCE Hydrographic Programme Office and describes how... 
sea water | marine water | cruise reports | international cooperation | oceanographic data | hydrographic data | water analysis
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6. Full Text Humoral Response to the HIV-1 Envelope V2 Region in a Thai Early Acute Infection Cohort
by Trinh, HV and Gohain, N and Pham, PT and Hamlin, C and Song, HS and Sanders-Buell, E and Bose, M and Eller, LA and Tovanabutra, S and Michael, NL and Robb, ML and Joyce, MG and Rao, M
CELLS, ISSN 2073-4409, 04/2019, Volume 8, Issue 4, p. 365
Reduced risk of HIV-1 infection correlated with antibody responses to the envelope variable 1 and 2 regions in the RV144 vaccine trial. To understand the... 
HIV-1 | single genome amplification (SGA) | RECOGNITION | NEUTRALIZING ANTIBODY | IMMUNE PRESSURE | CRYSTAL-STRUCTURE | LOOP | surface plasmon resonance (SPR) | transmitted | RV217 prospective study | CELL BIOLOGY | TRIAL | V1V2 | founder (T | acute infection | immune response | CRF01_AE | structural biology | VACCINE EFFICACY | F) virus | CRYO-EM STRUCTURE | BINDING | V2 region | transmitted/founder (T/F) virus
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7. Full Text Correction: Trinh, H.V., et al. Humoral Response to the HIV-1 Envelope V2 Region in a Thai Early Acute Infection Cohort. Cells 2019, 8 , 365
by Trinh, Hung V and Gohain, Neelakshi and Pham, Peter T and Hamlin, Christopher and Song, Hongshuo and Sanders-Buell, Eric and Bose, Meera and Eller, Leigh A and Jain, Swati and Uritskiy, Gherman and Rao, Venigalla B and Tovanabutra, Sodsai and Michael, Nelson L and Robb, Merlin L and Joyce, M Gordon and Rao, Mangala
Cells, ISSN 2073-4409, 06/2019, Volume 8, Issue 6, p. 554
In the original version of our article [...]. 
Military medicine | Infectious diseases | Clonal deletion | Human immunodeficiency virus--HIV | Hypersensitivity | Armed forces | Immune response (humoral) | n/a
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8. Sequence intrinsic somatic mutation mechanisms contribute to affinity maturation of VRC01-class HIV-1 broadly neutralizing antibodies
by Joyce K Hwang and Chong Wang and Zhou Du and Robin M Meyers and Thomas B Kepler and Donna Neuberg and Peter D Kwong and John R Mascola and M Gordon Joyce and Mattia Bonsignori and Barton F Haynes and Leng-Siew Yeap and Frederick W Alt
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 08/2017, Volume 114, Issue 32, p. 8614
Variable regions of Ig chains provide the antigen recognition portion of B-cell receptors and derivative antibodies. Ig heavy-chain variable region exons are... 
Exons | Variable region | Antibodies | Chains | Nucleotides | Receptors | J gene | Human immunodeficiency virus--HIV | Complementarity-determining region 1 | Complementarity-determining region 3 | Immunoglobulins | Complementarity | Maturation | Nucleotide sequence | Saturation | Hot spots | Pyridine nucleotide reductase | Cells | Substrates | Somatic hypermutation | Passengers | Lymphocytes B | Neutralizing | Affinity | Mutation | Neutralization
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9. Full Text Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection
by Yassine, Hadi M and Boyington, Jeffrey C and McTamney, Patrick M and Wei, Chih-Jen and Kanekiyo, Masaru and Kong, Wing-Pui and Gallagher, John R and Wang, Lingshu and Zhang, Yi and Joyce, M Gordon and Lingwood, Daniel and Moin, Syed M and Andersen, Hanne and Okuno, Yoshinobu and Rao, Srinivas S and Harris, Audray K and Kwong, Peter D and Mascola, John R and Nabel, Gary J and Graham, Barney S
Nature Medicine, ISSN 1078-8956, 09/2015, Volume 21, Issue 9, pp. 1065 - 1070
The antibody response to influenza is primarily focused on the head region of the hemagglutinin (HA) glycoprotein, which in turn undergoes antigenic drift,... 
MEDICINE, RESEARCH & EXPERIMENTAL | IMMUNITY | CELLS | DESIGN | COMPLEX | DOMAIN | VIRUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | DEPENDENT CELLULAR CYTOTOXICITY | IMMUNOGEN | MICE | MONOCLONAL-ANTIBODIES | Nanoparticles | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Animals | Influenza Vaccines - immunology | Influenza A Virus, H5N1 Subtype - immunology | Vaccination | Female | Mice | Mice, Inbred BALB C | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Ferrets | Antibodies, Viral - blood | Influenza vaccines | Avian influenza | Prevention | Physiological aspects | Lectins | Research | B cells | Health aspects | Immunoglobulins | Influenza | Rodents
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10. 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
Structure, ISSN 0969-2126, 08/2016, Volume 24, Issue 8
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11. Full Text Maturation and Diversity of the VRC01-Antibody Lineage over 15 Years of Chronic HIV-1 Infection
by Wu, Xueling and Zhang, Baoshan and Zhang, Zhenhai and Schramm, Chaim A and Joyce, M. Gordon and Do Kwon, Young and Zhou, Tongqing and Sheng, Zizhang and O’Dell, Sijy and McKee, Krisha and Georgiev, Ivelin S and Chuang, Gwo-Yu and Longo, Nancy S and Lynch, Rebecca M and Saunders, Kevin O and Soto, Cinque and Srivatsan, Sanjay and Yang, Yongping and Bailer, Robert T and Louder, Mark K 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 Legaspi, Richelle and Maduro, Quino and Masiello, Cathy and Maskeri, Baishali and McDowell, Jenny and Montemayor, Casandra and Park, Morgan and Riebow, Nancy and Schandler, Karen and Schmidt, Brian and Sison, Christina and Stantripop, Mal and Thomas, Pam and Thomas, James and Vemulapalli, Meg and Young, Alice and Mullikin, James C and Connors, Mark and Kwong, Peter D and Mascola, John R and Shapiro, Lawrence and Program, NCS and NISC Comparative Sequencing Program and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Cell, ISSN 0092-8674, 04/2015, Volume 161, Issue 3, pp. 470 - 485
HIV-1-neutralizing antibodies develop in most HIV-1-infected individuals, although highly effective antibodies are generally observed only after years of... 
B-CELL RECEPTORS | POTENT NEUTRALIZATION | STRUCTURAL BASIS | CD4-BINDING SITE | BROADLY NEUTRALIZING ANTIBODIES | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-SITE | ENVELOPE TRIMER | RATIONAL DESIGN | GENE USAGE | CELL BIOLOGY | Amino Acid Sequence | Antibody Diversity | Humans | Models, Molecular | Molecular Sequence Data | Antibodies, Neutralizing - genetics | Leukocytes, Mononuclear | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | Sequence Alignment | B-Lymphocytes - immunology | Antibodies, Neutralizing - chemistry | Chronic Disease | Evolution, Molecular | Viral antibodies | Antibodies | Phylogeny | HIV (Viruses) | Health aspects | HIV infection | Medical research | Genomics | Crystals | Medicine, Experimental | Research institutes | Structure | 60 APPLIED LIFE SCIENCES
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12. 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
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