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1. 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 | Index Medicus | Resource
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2. Full Text A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans
by Sok, Devin and Pauthner, Matthias and Briney, Bryan and Lee, Jeong Hyun and Saye-Francisco, Karen L and Hsueh, Jessica and Ramos, Alejandra and Le, Khoa M and Jones, Meaghan and Jardine, Joseph G and Bastidas, Raiza and Sarkar, Anita and Liang, Chi-Hui and Shivatare, Sachin S and Wu, Chung-Yi and Schief, William R and Wong, Chi-Huey and Wilson, Ian A and Ward, Andrew B and Zhu, Jiang and Poignard, Pascal and Burton, Dennis R
Immunity, ISSN 1074-7613, 07/2016, Volume 45, Issue 1, pp. 31 - 45
The dense patch of high-mannose-type glycans surrounding the N332 glycan on the HIV envelope glycoprotein (Env) is targeted by multiple broadly neutralizing... 
POTENT | HEPATITIS-C VIRUS | BROADLY NEUTRALIZING ANTIBODIES | CRYSTAL-STRUCTURE | VACCINE DESIGN | IMMUNODEFICIENCY-VIRUS TYPE-1 | IMMUNOLOGY | HUMAN MONOCLONAL-ANTIBODIES | CRYO-EM STRUCTURE | DEPENDENT EPITOPE | GP41-GP120 INTERFACE | Epitope Mapping | Binding Sites, Antibody - immunology | Peptide Fragments - metabolism | Epitopes - metabolism | Humans | Polysaccharides - immunology | HIV Envelope Protein gp120 - metabolism | Amino Acid Motifs | Polysaccharides - metabolism | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | Receptors, CCR5 - metabolism | Genetic Engineering | HIV Antibodies - immunology | Immunity, Humoral | HEK293 Cells | Protein Binding | Immunologic Memory | CD4 Antigens - metabolism | Viral antibodies | International relief | Antigens | Polysaccharides | AIDS vaccines | Peptides | Antibodies | HIV (Viruses) | Sugars | Monosaccharides | Immunoglobulins | Immunology | Acquired immune deficiency syndrome--AIDS | Human immunodeficiency virus--HIV | Influenza | Viruses | Vaccines | Experiments | Binding sites | Manuscripts | Index Medicus | Life Sciences | Biomolecules | Biochemistry, Molecular Biology
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3. Full Text Electron-Microscopy-Based Epitope Mapping Defines Specificities of Polyclonal Antibodies Elicited during HIV-1 BG505 Envelope Trimer Immunization
by Bianchi, Matteo and Turner, Hannah L and Nogal, Bartek and Cottrell, Christopher A and Oyen, David and Pauthner, Matthias and Bastidas, Raiza and Nedellec, Rebecca and McCoy, Laura E and Wilson, Ian A and Burton, Dennis R and Ward, Andrew B and Hangartner, Lars and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Immunity, ISSN 1074-7613, 08/2018, Volume 49, Issue 2, pp. 288 - 300.e8
Characterizing polyclonal antibody responses via currently available methods is inherently complex and difficult. Mapping epitopes in an immune response is... 
vaccine | antibody epitope mapping | HIV | BG505 | negative-stain EM | SOSIP | electron microscopy | antibodies | Env | cryo-EM | polyclonal antibodies | IMMUNOGENICITY | ELICITATION | BROADLY NEUTRALIZING ANTIBODIES | GLYCOPROTEIN COMPLEX | IMMUNOLOGY | HUMAN MONOCLONAL-ANTIBODIES | IDENTIFICATION | DEPENDENT EPITOPE | V2 APEX | QUATERNARY | PRECURSORS | Cell Line | HIV Infections - prevention & control | Rabbits | Antibody Formation - immunology | Immunization | env Gene Products, Human Immunodeficiency Virus - immunology | Humans | AIDS Vaccines - immunology | Epitopes - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | Animals | HIV Antibodies - immunology | Microscopy, Electron - methods | Recombinant Proteins - immunology | HEK293 Cells | Epitope Mapping - methods | Female | Immunoglobulin Fab Fragments - immunology | International relief | Medical research | AIDS vaccines | Medicine, Experimental | Research institutes | HIV (Viruses) | Electron microscopy | Antigenic determinants | Pathogens | Antigens | Immunoglobulins | Immune response | Glycoprotein | Antibodies | Mapping | Trimers | Vaccines | Experiments | Immune response (humoral) | Antibody response | Proteins | Immune systems | Microscopy | Acquired immune deficiency syndrome--AIDS | Neutralizing | Human immunodeficiency virus--HIV | Epitope mapping | Index Medicus
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4. Full Text Vaccine-Induced Protection from Homologous Tier 2 SHIV Challenge in Nonhuman Primates Depends on Serum-Neutralizing Antibody Titers
by Pauthner, Matthias G and Nkolola, Joseph P and Havenar-Daughton, Colin and Murrell, Ben and Reiss, Samantha M and Bastidas, Raiza and Prévost, Jérémie and Nedellec, Rebecca and von Bredow, Benjamin and Abbink, Peter and Cottrell, Christopher A and Kulp, Daniel W and Tokatlian, Talar and Nogal, Bartek and Bianchi, Matteo and Li, Hui and Lee, Jeong Hyun and Butera, Salvatore T and Evans, David T and Hangartner, Lars and Finzi, Andrés and Wilson, Ian A and Wyatt, Richard T and Irvine, Darrell J and Schief, William R and Ward, Andrew B and Sanders, Rogier W and Crotty, Shane and Shaw, George M and Barouch, Dan H and Burton, Dennis R
Immunity, ISSN 1074-7613, 01/2019, Volume 50, Issue 1, pp. 241 - 252.e6
Passive administration of HIV neutralizing antibodies (nAbs) can protect macaques from hard-to-neutralize (tier 2) chimeric simian-human immunodeficiency virus... 
correlates of protection | BG505 | HIV vaccine | non-human primates | tier 2 protection | neutralizing antibodies | ADCC | vaccination | IMMUNIZATION | RESPONSES | REPLICATION | HIV-1 ENVELOPE TRIMERS | INFECTION | CELL-MEDIATED CYTOTOXICITY | IMMUNOLOGY | HUMAN-IMMUNODEFICIENCY-VIRUS | TYPE-1 | T-CELLS | RHESUS MACAQUES | Immunization | Toxicity | Vaccination | Antibodies | Envelope protein | Cytotoxicity | Viruses | Homology | Lymphocytes T | Trimers | Infections | Vaccines | Proteins | Studies | Animals | Acquired immune deficiency syndrome--AIDS | Lymphocytes | Human immunodeficiency virus--HIV | Neutralizing | Primates | Recombinant | Index Medicus
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5. Full Text Differential processing of HIV envelope glycans on the virus and soluble recombinant trimer
by Cao, Liwei and Pauthner, Matthias and Andrabi, Raiees and Rantalainen, Kimmo and Berndsen, Zachary and Diedrich, Jolene K and Menis, Sergey and Sok, Devin and Bastidas, Raiza and Park, Sung-Kyu Robin and Delahunty, Claire M and He, Lin and Guenaga, Javier and Wyatt, Richard T and Schief, William R and Ward, Andrew B and Yates, John R and Burton, Dennis R and Paulson, James C
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 3693 - 14
As the sole target of broadly neutralizing antibodies (bnAbs) to HIV, the envelope glycoprotein (Env) trimer is the focus of vaccination strategies designed to... 
PROTEIN | SITE-SPECIFIC ANALYSIS | CRYOELECTRON MICROSCOPY | BROADLY NEUTRALIZING ANTIBODIES | VACCINE DESIGN | MULTIDISCIPLINARY SCIENCES | GLYCOPROTEIN COMPLEX | ENV TRIMERS | GLYCOSYLATION | TYPE-1 | DEPENDENT EPITOPE | Epitopes - immunology | HIV-1 - metabolism | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV-1 - pathogenicity | HIV Antibodies - immunology | Humans | Protein Multimerization | Polysaccharides - immunology | Polysaccharides - metabolism | Polysaccharides | Antigenicity | Human immunodeficiency virus--HIV | Vaccination | Glycoprotein | Antibodies | Viruses | Glycosylation | Trimers | Vaccines | N-glycans | Recombinant | Index Medicus
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6. Full Text Slow Delivery Immunization Enhances HIV Neutralizing Antibody and Germinal Center Responses via Modulation of Immunodominance
by Cirelli, Kimberly M and Carnathan, Diane G and Nogal, Bartek and Martin, Jacob T and Rodriguez, Oscar L and Upadhyay, Amit A and Enemuo, Chiamaka A and Gebru, Etse H and Choe, Yury and Viviano, Federico and Nakao, Catherine and Pauthner, Matthias G and Reiss, Samantha and Cottrell, Christopher A and Smith, Melissa L and Bastidas, Raiza and Gibson, William and Wolabaugh, Amber N and Melo, Mariane B and Cossette, Benjamin and Kumar, Venkatesh and Patel, Nirav B and Tokatlian, Talar and Menis, Sergey and Kulp, Daniel W and Burton, Dennis R and Murrell, Ben and Schief, William R and Bosinger, Steven E and Ward, Andrew B and Watson, Corey T and Silvestri, Guido and Irvine, Darrell J and Crotty, Shane
Cell, ISSN 0092-8674, 05/2019, Volume 177, Issue 5, pp. 1153 - 1171.e28
Conventional immunization strategies will likely be insufficient for the development of a broadly neutralizing antibody (bnAb) vaccine for HIV or other... 
somatic hypermutation | HIV vaccine | non-human primates | affinity maturation | FNA | memory B cells | rhesus macaque genome | GC- TFH | immune complexes | GC- T | NONHUMAN-PRIMATES | RNA-SEQ | PERFORMANCE | BIOCHEMISTRY & MOLECULAR BIOLOGY | VACCINE | MICRONEEDLES | MICROSCOPY | MULTIPLE SEQUENCE ALIGNMENT | CRYO-EM STRUCTURE | FOLLICULAR HELPER-CELLS | ANTIGEN | CELL BIOLOGY | Immunization | AIDS vaccines | Analysis | Genomics | Primates | B cells | Research institutes | HIV (Viruses) | Antigenic determinants
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7. Full Text Mapping the Prion Protein Using Recombinant Antibodies
by R. Anthony Williamson and David Peretz and Clemencia Pinilla and Hadyn Ball and Raiza B. Bastidas and Roman Rozenshteyn and Richard A. Houghten and Stanley B. Prusiner and Dennis R. Burton
Journal of Virology, ISSN 0022-538X, 11/1998, Volume 72, Issue 11, pp. 9413 - 9418
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
SCRAPIE ISOFORM | VIROLOGY | COMBINATORIAL LIBRARIES | INFECTIVITY | FRAGMENT | CONFORMATIONAL TRANSITIONS | N-TERMINUS | MONOCLONAL-ANTIBODIES | EXPRESSION | LIPOSOMES | PRP | Amino Acid Sequence | Immunization | Prions - genetics | PrPSc Proteins - immunology | Molecular Sequence Data | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Antibodies, Monoclonal | Prions - chemistry | Epitopes - genetics | PrPC Proteins - chemistry | PrPSc Proteins - chemistry | PrPSc Proteins - genetics | Prions - immunology | Animals | Recombinant Proteins - immunology | Epitope Mapping - methods | Protein Conformation | Epitopes - chemistry | Mice | PrPC Proteins - genetics | PrPC Proteins - immunology | Index Medicus | Viral Pathogenesis and Immunity
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8. Full Text Exudados de la raiz y su relevancia actual en las interacciones alelopaticas
by Oliveros-Bastidas, Alberto De J and Macías, Francisco A and Fernández, Ceferino Carrera and Marín, David and Molinillo, José M. G
Quimica Nova, ISSN 0100-4042, 2009, Volume 32, Issue 1, pp. 198 - 213
Exudate | Root | Allelopathy
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9. Full Text A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform
by Peretz, David and Williamson, R.Anthony and Matsunaga, Yoichi and Serban, Hana and Pinilla, Clemencia and Bastidas, Raiza B and Rozenshteyn, Roman and James, Thomas L and Houghten, Richard A and Cohen, Fred E and Prusiner, Stanley B and Burton, Dennis R
Journal of Molecular Biology, ISSN 0022-2836, 10/1997, Volume 273, Issue 3, pp. 614 - 622
The scrapie prion protein (PrPSc) is formed from the cellular isoform (PrPC) by a post-translational process that involves a profound conformational change.... 
conformational rearrangement | prion disease | scrapie | recombinant antibody | liposome | Liposome | Prion disease | Conformational rearrangement | Scrapie | Recombinant antibody | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMBINATORIAL LIBRARIES | INFECTIVITY | HUMAN-IMMUNODEFICIENCY-VIRUS | ALPHA-HELICES | PRP | GENE | K CQ BIOCHEMISTRY & MOLECULAR BIOLOGY | SECONDARY STRUCTURE | MICE | HUMAN MONOCLONAL-ANTIBODIES | EXPRESSION | Recombinant Fusion Proteins - immunology | PrP 27-30 Protein - immunology | Epitopes, B-Lymphocyte - chemistry | Guanidines - pharmacology | Epitopes, B-Lymphocyte - immunology | Structure-Activity Relationship | Isomerism | PrPC Proteins - chemistry | Mesocricetus | Protein Denaturation | Thiocyanates - pharmacology | Scrapie - immunology | PrP 27-30 Protein - drug effects | CHO Cells | Cricetinae | Enzyme-Linked Immunosorbent Assay | Models, Molecular | Recombinant Fusion Proteins - chemistry | Precipitin Tests | Animals | PrP 27-30 Protein - chemical synthesis | Protein Conformation | Mice | Immunoglobulin Fab Fragments - immunology | PrP 27-30 Protein - chemistry | PrPC Proteins - immunology | Index Medicus
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10. Full Text Abstracts of the HIV Research for Prevention Meeting, HIVR4P, 17-20 October, 2016, Chicago, USA
by Sullivan, Patrick and Yuan, Maoli and Coleman, John and Destefano, Joanne and Zhang, Xinsheng and Yates, Nicole and Barouch, Dan and Ackerman, Margaret and Decamp, Allan and Alter, Galit and Tomaras, Georgia and Tomaras, Georgia and Montefiori, David and Montefiori, David and Rasmussen, Beth and Morrow, Gavin and Koff, Wayne and Kashuba, Angela and Kashuba, Angela and Mascola, John and Picker, Louis and Kent, Stephen and Selhorst, Philippe and Masson, Lindi and Ngandu, Nobubelo and Rademeyer, Cecilia and Karim, Quarraisha Abdool and Kijak, Gustavo and Barouch, Dan and Rasheed, Ata Ur and Havenar-Daughton, Colin and Pham, Matthew and Kovalenkov, Yevgeniy and Gumber, Sanjeev and Johnson, Matthew and Wrammert, Jens and Villinger, Francois and Haynes, Barton and Haynes, Barton and Fox, Christopher and Reed, Steve and Vasilakos, John and Tomai, Mark and Crotty, Shane and Ahmed, Rafi and Pulendran, Bali and Fukazawa, Yoshinori and Lifson, Jeffrey and Lifson, Jeffrey and Moore, Penny and Chatora, Kumbirai and Skorochod, Elisabeth and Madidi, Ngonidzashe and Gomez, Anabel and Ncube, Getrude and Sundaram, Maaya and Kretschmer, Steve and Pauthner, Matthias and Briney, Bryan and Lee, Jeong Hyun and Saye-Francisco, Karen and Hsueh, Jessica and Ramos, Alejandra and Le, Khoa and Jones, Meaghan and Jardine, Joseph and Bastidas, Raiza and Sarkar, Anita and Liang, Chi-Hui and Wilson, Ian and Ward, Andrew and Zhu, Jiang and Poignard, Pascal and Burton, Dennis and Krebs, Shelly and Law, Wiliam and Gift, Syna and Chenine, Agnes and Rolland, Morgane and Moody, M. Anthony and Jarosinski, Marissa and Georgiev, Ivelin and Chuang, Gwo-Yu and Chuang, Gwo-Yu and Asokan, Mangaiarkarasi and Bailer, Robert T and Cale, Evan M and Louder, Mark and Kwong, Peter D and Polonis, Victoria and Tovanabutra, Sodsai and Robb, Merlin and Mascola, John R and Wibmer, Constantinos Kurt and Wibmer, Constantinos Kurt and Madzorera, Vimbai S and Doria-Rose, Nicole A and Morris, Lynn and Moore, Penny L and Anthony, Colin and ...
AIDS Research and Human Retroviruses, ISSN 0889-2229, 10/2016, Volume 32, Issue S1, pp. 1 - 409
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11. Full Text Circumventing Tolerance to Generate Autologous Monoclonal Antibodies to the Prion Protein
by R. Anthony Williamson and David Peretz and Nechama Smorodinsky and Raiza Bastidas and Hana Serban and Ingrid Mehlhorn and Stephen J. DeArmond and Stanley B. Prusiner and Dennis R. Burton
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/1996, Volume 93, Issue 14, pp. 7279 - 7282
Prion diseases are disorders of protein conformation and do not provoke an immune response. Raising antibodies to the prion protein (PrP) has been difficult... 
Bacteriophages | Reactivity | Enzyme linked immunosorbent assay | Prions | Hybridomas | Cell lines | Antibodies | Prion diseases | Libraries | Epitopes | gene ablation | prion disease | mouse antibody libraries | phage display | scrapie | VIRUS | CONVERSION | FORM | MULTIDISCIPLINARY SCIENCES | COMBINATORIAL LIBRARIES | CULTURED-CELLS | HAMSTER | PRP | MICE | SCRAPIE PRION | Antibody Specificity | Cricetinae | Immunoglobulin Heavy Chains - biosynthesis | Enzyme-Linked Immunosorbent Assay | Prion Diseases - immunology | Antibodies, Monoclonal - biosynthesis | Immune Tolerance | Molecular Sequence Data | Prions - analysis | Recombinant Proteins - biosynthesis | DNA Primers | Immunoglobulin Fab Fragments - biosynthesis | Prions - immunology | Animals | Base Sequence | Mesocricetus | Polymerase Chain Reaction | Mice | Monoclonal antibodies | Reports | Genetic aspects | Research | Proteins | Medical research | Rodents | Genes | Index Medicus
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12. Full Text Human Antibody Responses to Mature and Immature Forms of Viral Envelope in Respiratory Syncytial Virus Infection: Significance for Subunit Vaccines
by Hiroshi Sakurai and R. Anthony Williamson and James E. Crowe and Judy A. Beeler and Pascal Poignard and Raiza B. Bastidas and Robert M. Chanock and Dennis R. Burton
Journal of Virology, ISSN 0022-538X, 04/1999, Volume 73, Issue 4, pp. 2956 - 2962
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
VIROLOGY | RSV | PROTECTION | COMBINATORIAL LIBRARIES | SYNTHETIC PEPTIDES | MICE | FUSION GLYCOPROTEIN | HUMAN MONOCLONAL-ANTIBODIES | FAB FRAGMENTS | F-GLYCOPROTEIN | CHILDREN | Virion - immunology | Amino Acid Sequence | Antigens, Viral - immunology | Cell Line | Humans | Isoantigens - immunology | Respiratory Syncytial Viruses - immunology | Molecular Sequence Data | Antibodies, Viral - immunology | Viral Envelope Proteins - immunology | Respiratory Syncytial Virus Infections - immunology | Viral Vaccines - immunology | Index Medicus | Pathogenesis and Immunity
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13. Full Text Exudados de la raiz y su relevancia actual en las interacciones alelopaticas
by Oliveros-Bastidas, Alberto de J and Macías, Francisco A and Fernández, Ceferino Carrera and Marín, David and Molinillo, José M. G
Química Nova, ISSN 1678-7064, 2009, Volume 32, Issue 1, pp. 198 - 213
CHEMISTRY, MULTIDISCIPLINARY
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