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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2013, Volume 110, Issue 44, pp. 17921 - 17926
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2013, Volume 110, Issue 33, pp. 13481 - 13486
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2013, Volume 110, Issue 16, pp. 6470 - 6475
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2010, Volume 107, Issue 33, pp. 14799 - 14804
Diabetics frequently suffer from chronic, nonhealing wounds. Although bacterial colonization and/or infection are generally acknowledged to negatively impact... 
Microbiota | Wound healing | Diabetes complications | Genes | Bacteria | Skin | Diabetes | Gene expression | Sequencing | Staphylococcus | Innate immunity | Microbiome | ULCERS | wound healing | BACTERIA | PROJECT | DB/DB MICE | MACROPHAGES | MULTIDISCIPLINARY SCIENCES | microbiome | FOOT | IN-VITRO | innate immunity | GENE | INFLAMMATION | DIVERSITY | diabetes | gene expression | Skin - microbiology | Receptors, Leptin - genetics | Skin - metabolism | Diabetes Mellitus, Type 2 - genetics | Molecular Sequence Data | Gene Expression Profiling | Wound Healing | Biodiversity | Bacteria - growth & development | Bacterial Infections - genetics | Metagenome - genetics | Time Factors | Bacteria - classification | Staphylococcus - physiology | Female | Staphylococcus - genetics | Bacterial Infections - microbiology | Bacteria - genetics | Sequence Analysis, DNA | Mice, Knockout | Bacterial Infections - physiopathology | Host-Pathogen Interactions | Animals | Diabetes Mellitus, Type 2 - physiopathology | Receptors, Leptin - physiology | RNA, Ribosomal, 16S - genetics | Mice | Skin - physiopathology | Cluster Analysis | Population Dynamics | Microbiota (Symbiotic organisms) | Health aspects | Wounds and injuries | Immune response | rRNA 16S | Diabetes mellitus | Abundance | Data processing | Colonization | Biological Sciences
Journal Article
Journal Article
Nature, ISSN 0028-0836, 2014, Volume 514, Issue 7520, pp. 59 - 64
Journal Article
Nature, ISSN 0028-0836, 2013, Volume 498, Issue 7454, pp. 367 - 370
Journal Article
Immunity, ISSN 1074-7613, 03/2018, Volume 48, Issue 3, pp. 500 - 513.e6
Virtually the entire surface of the HIV-1-envelope trimer is recognized by neutralizing antibodies, except for a highly glycosylated region at the center of... 
glycan cluster | broadly neutralizing antibody | glycan recognition | viral escape | glycopeptide epitope | HIV vaccine | prefusion-closed Env trimer | crystal structure | HIV silent face | TRIMER | RECOGNITION | CD4-BINDING SITE | CRYSTAL-STRUCTURE | ELECTRON-MICROSCOPY | GP120 | IMMUNOLOGY | ENV | CRYO-EM STRUCTURE | DEPENDENT EPITOPE | REVEALS | Epitope Mapping | Epitopes - metabolism | Somatic Hypermutation, Immunoglobulin - immunology | Humans | Molecular Conformation | Antibodies, Neutralizing - metabolism | Glycopeptides - chemistry | Structure-Activity Relationship | HIV Envelope Protein gp120 - metabolism | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | Glycopeptides - immunology | HIV Antibodies - immunology | Polysaccharides - chemistry | HIV Envelope Protein gp120 - chemistry | Binding Sites | HIV Antibodies - metabolism | Amino Acid Sequence | Models, Molecular | Antigens, Viral - chemistry | Antibodies, Neutralizing - genetics | Glycosylation | Polysaccharides - immunology | Protein Binding - immunology | HIV Antibodies - chemistry | Antigens, Viral - immunology | HIV-1 - immunology | Antibodies, Neutralizing - chemistry | Epitopes - chemistry | HIV Antibodies - genetics | Competition | Plasma | Antigens | Immunoglobulins | Face recognition | Antibodies | Amino acids | Epitopes | Glycan | Somatic hypermutation | Polysaccharides | Acquired immune deficiency syndrome--AIDS | Neutralizing | Human immunodeficiency virus--HIV | Face | Glycoprotein gp120 | Binding sites | Crystal structure | Neutralization
Journal Article
Genome Research, ISSN 1088-9051, 05/2012, Volume 22, Issue 5, pp. 850 - 859
Journal Article
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... 
B-CELL RESPONSES | CONFORMATIONAL EPITOPE | POTENT NEUTRALIZATION | CD4 BINDING-SITE | VACCINE DESIGN | MULTIDISCIPLINARY SCIENCES | ENVELOPE GLYCOPROTEIN | HIV-1-INFECTED INDIVIDUALS | 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
Journal Article