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1. Full Text D-106 Structural targeting of the A32-region epitopes for antibody-dependent cell-mediated cytotoxicity
by Pazgier, Marzena
JAIDS Journal of Acquired Immune Deficiency Syndromes, ISSN 1525-4135, 03/2017, Volume 74, p. 47
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2. Full Text Survivors Remorse: antibody‐mediated protection against HIV‐1
by Lewis, George K and Pazgier, Marzena and DeVico, Anthony L
Immunological Reviews, ISSN 0105-2896, 01/2017, Volume 275, Issue 1, pp. 271 - 284
Summary It is clear that antibodies can play a pivotal role in preventing the transmission of HIV‐1 and large efforts to identify an effective antibody‐based... 
neutralizing antibodies | non‐neutralizing antibodies | HIV‐1 | AIDS vaccine | HIV-1 | non-neutralizing antibodies | MUCOSAL SHIV CHALLENGE | EFFECTOR FUNCTION | HUMAN MONOCLONAL-ANTIBODY | ENVELOPE GLYCOPROTEIN | IMMUNOLOGY | HUMAN-IMMUNODEFICIENCY-VIRUS | DEPENDENT CELLULAR CYTOTOXICITY | VACCINE REGIMEN | IN-VITRO | BROADLY NEUTRALIZING ANTIBODIES | RHESUS MACAQUES | Epitopes - immunology | HIV Infections - immunology | HIV-1 - immunology | Animals | Immune Evasion | HIV Antigens - immunology | Antibodies, Neutralizing - therapeutic use | Humans | AIDS Vaccines - immunology | Primates | HIV Antibodies - therapeutic use | Clinical Trials as Topic | Viral antibodies | Antibodies | AIDS vaccines | HIV (Viruses) | Epidemics | Immunoglobulins | Disease transmission | Target recognition | Acquired immune deficiency syndrome--AIDS | Neutralizing | Human immunodeficiency virus--HIV | Vaccines | Epitopes | Neutralization
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3. PI-3 Single molecule fluorescence approaches to probe the binding of soluble-CD4 to native-like HIV-1 SOSIP trimers
by Parul Agrawal and Anthony DeVico and George Lewis and Marzena Pazgier and Krishanu Ray
Journal of Acquired Immune Deficiency Syndromes, ISSN 1525-4135, 04/2019, Volume 81, p. 77
Several lines of evidence suggest that HIV-1 envelope (Env) on virions transition through a series of conformations in solution as well as when they engage CD4... 
Binding | Stoichiometry | Fluorescence | Trimers | C-Terminus | Real time | CD4 antigen | Algorithms | Antigenicity | Human immunodeficiency virus--HIV | Virions | Occupancy | Fusion protein
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4. Full Text PI-3 Single molecule fluorescence approaches to probe the binding of soluble-CD4 to native-like HIV-1 SOSIP trimers
by Agrawal, Parul and DeVico, Anthony and Lewis, George and Pazgier, Marzena and Ray, Krishanu
JAIDS Journal of Acquired Immune Deficiency Syndromes, ISSN 1525-4135, 04/2019, Volume 81, p. 77
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5. Full Text Human α-Defensin 6 Promotes Mucosal Innate Immunity Through Self-Assembled Peptide Nanonets
by Hiutung Chu and Marzena Pazgier and Grace Jung and Sean-Paul Nuccio and Patricia A. Castillo and Maarten F. de Jong and Maria G. Winter and Sebastian E. Winter and Jan Wehkamp and Bo Shen and Nita H. Salzman and Mark A. Underwood and Renee M. Tsolis and Glenn M. Young and Wuyuan Lu and Robert I. Lehrer and Andreas J. Bäumler and Charles L. Bevins
Science, ISSN 0036-8075, 7/2012, Volume 337, Issue 6093, pp. 477 - 481
Defensins are antimicrobial peptides that contribute broadly to innate immunity, including protection of mucosal tissues. Human α-defensin (HD) 6 is highly... 
Molecules | Epithelial cells | Transgenic animals | Biosensing techniques | Humans | REPORTS | Cell lines | Bacteria | Mice | Monomers | Vehicles | HD5 | MICE | PANETH CELLS | MULTIDISCIPLINARY SCIENCES | Intestine, Small - ultrastructure | Protein Multimerization | Immunity, Mucosal | env Gene Products, Human Immunodeficiency Virus - metabolism | Nanostructures | Salmonella Infections, Animal - immunology | Adhesins, Bacterial - metabolism | Salmonella typhimurium - ultrastructure | Macromolecular Substances - chemistry | Peptides - metabolism | Paneth Cells - immunology | Intestinal Mucosa - immunology | Protein Structure, Quaternary | Macromolecular Substances - immunology | alpha-Defensins - metabolism | Yersinia enterocolitica - immunology | Intestine, Small - immunology | Paneth Cells - metabolism | Cell Line | Microscopy, Electron, Scanning | alpha-Defensins - chemistry | Intestinal Mucosa - ultrastructure | Peptides - chemistry | Salmonella typhimurium - immunology | Salmonella typhimurium - pathogenicity | Yersinia enterocolitica - pathogenicity | Intestine, Small - microbiology | Models, Molecular | Mice, Transgenic | Intestinal Mucosa - microbiology | Immunity, Innate | Animals | alpha-Defensins - immunology | Salmonella Infections, Animal - microbiology | Protein Binding | Bacterial Proteins - metabolism | Macromolecular Substances - metabolism
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6. Full Text Structural Basis for High-Affinity Peptide Inhibition of P53 Interactions with MDM2 and MDMX
by Marzena Pazgier and Min Liu and Guozhang Zou and Weirong Yuan and Changqing Li and Chong Li and Jing Li and Juahdi Monbo and Davide Zella and Sergey G. Tarasov and Wuyuan Lu and Robert C. Gallo
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2009, Volume 106, Issue 12, pp. 4665 - 4670
The oncoproteins MDM2 and MDMX negatively regulate the activity and stability of the tumor suppressor protein p53—a cellular process initiated by MDM2 and/or... 
Bacteriophages | Proteins | Private mortgage insurance | Ligation | Medical treatment | Libraries | Transactivation | Tumors | Crystal structure | Cancer | SUPPRESSOR TRANSACTIVATION DOMAIN | CELLS | ACTIVATION | TERMINAL DOMAIN | MULTIDISCIPLINARY SCIENCES | IN-VIVO | PROTEIN-PROTEIN INTERACTIONS | CHEMICAL LIGATION | DEGRADATION | RESTORATION | BINDING | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Peptides - chemistry | Protein Structure, Secondary | Humans | Tumor Suppressor Protein p53 - metabolism | Models, Molecular | Molecular Sequence Data | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - chemistry | Structure-Activity Relationship | Oligopeptides - metabolism | Peptide Library | Nuclear Proteins - chemistry | Proto-Oncogene Proteins c-mdm2 - chemistry | Peptides - pharmacology | Peptides - metabolism | Protein Binding - drug effects | Tumor Suppressor Protein p53 - chemistry | Oligopeptides - pharmacology | Oligopeptides - chemistry | Proto-Oncogene Proteins c-mdm2 - metabolism | Cellular proteins | Cell interaction | Research | Structure | Protein binding | Biological Sciences
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7. Full Text PJ-1 The HIV-1 antisense protein ASP is a structural protein of the viral envelope
by Affram, Yvonne and Zapata, Juan Carlos and Zhou, Wei and Pazgier, Marzena and Iglesias-Ussel, Maria and Ray, Krishanu and Latinovic, Olga and Romerio, Fabio
JAIDS Journal of Acquired Immune Deficiency Syndromes, ISSN 1525-4135, 04/2019, Volume 81, p. 79
Introduction: The antisense strand of the HIV-1 genome encodes a 189-aa, highly hydrophobic protein (ASP) with no known homologs. Humoral and cellular immune... 
Fluorescence spectroscopy | Flow cytometry | Biotechnology | Chromatin | Fluorescence | Confocal microscopy | Antisense | Homology | Viruses | Genomes | Activation | Nucleotides | Vaccines | Hydrophobicity | Density | Cell surface | Nuclei | Image acquisition | Proteins | Virions | Foxp3 protein | Localization | Microscopes | Guava | Image resolution | Data acquisition | Cell division | Amino acid sequence | Cell membranes | Gene expression | Immune response (humoral) | Domains | Microscopy | Cell lines | Monoclonal antibodies | Replication | Nuclei (cytology) | Codons | Budding | Glycoprotein gp120 | Cytoplasm | ASP protein | Fitness
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8. Full Text D-peptide inhibitors of the p53–MDM2 interaction for targeted molecular therapy of malignant neoplasms
by Min Liu and Chong Li and Marzena Pazgier and Changqing Li and Yubin Mao and Yifan Lv and Bing Gu and Gang Wei and Weirong Yuan and Changyou Zhan and Wei-Yue Lu and Wuyuan Lu and Robert C. Gallo
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2010, Volume 107, Issue 32, pp. 14321 - 14326
The oncoproteins MDM2 and MDMX negatively regulate the activity and stability of the tumor suppressor protein p53, conferring tumor development and survival.... 
Bacteriophages | Ligation | HCT116 cells | Medical treatment | Glioblastoma | Cell lines | Liposomes | Cells | Tumors | Cancer | Native chemical ligation | Mirror-image phage display | MDM2 PROMOTES | PROTEIN | CANCER CELLS | GLIOBLASTOMA-MULTIFORME | MULTIDISCIPLINARY SCIENCES | mirror-image phage display | P53 PATHWAY | IMAGE PHAGE DISPLAY | glioblastoma | AUTOREGULATORY FEEDBACK LOOP | IN-VIVO | HIV-1 ENTRY | CHEMICAL LIGATION | native chemical ligation | Amino Acid Sequence | Oligopeptides | Humans | Tumor Suppressor Protein p53 - metabolism | Transplantation, Heterologous | Peptides - pharmacology | Animals | Mice, Nude | Glioblastoma - pathology | Protein Binding - drug effects | Cell Line, Tumor | Cell Proliferation - drug effects | Mice | Glioblastoma - drug therapy | Drug Delivery Systems - methods | Proto-Oncogene Proteins c-mdm2 - metabolism | Peptides - therapeutic use | Drug Screening Assays, Antitumor | Tumor suppressor genes | Genetic aspects | Peptides | Health aspects | Biological Sciences
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9. Full Text Diverse specificity and effector function among human antibodies to HIV-1 envelope glycoprotein epitopes exposed by CD4 binding
by Yongjun Guan and Marzena Pazgier and Mohammad M. Sajadi and Roberta Kamin-Lewis and Salma Al-Darmarki and Robin Flinko and Elena Lovo and Xueji Wu and James E. Robinson and Michael S. Seaman and Timothy R. Fouts and Robert C. Gallo and Anthony L. DeVico and George K. Lewis and SLAC National Accelerator Lab., Menlo Park, CA (United States)
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 01/2013, Volume 110, Issue 1, pp. E69 - E78
The HIV-1 envelope glycoprotein (Env) undergoes conformational transitions consequent to CD4 binding and coreceptor engagement during viral entry. The physical... 
DEPENDENT CELLULAR CYTOTOXICITY | CONFORMATIONAL EPITOPE | MEDIATED CYTOTOXICITY | MULTIDISCIPLINARY SCIENCES | CD4-INDUCED EPITOPES | PASSIVE TRANSFER | IMMUNODEFICIENCY-VIRUS TYPE-1 | HUMAN MONOCLONAL-ANTIBODY | SYNERGISTIC NEUTRALIZATION | PROTECTIVE EFFICACY | ANTIGENIC PROPERTIES | HIV Envelope Protein gp120 - genetics | Antibody Specificity | CD4 Antigens - immunology | Epitopes - metabolism | Enzyme-Linked Immunosorbent Assay | Humans | Antibody-Dependent Cell Cytotoxicity - immunology | Models, Molecular | Crystallography, X-Ray | Neutralization Tests | Binding Sites - genetics | Epitopes - genetics | HIV Antibodies - chemistry | HIV Envelope Protein gp120 - immunology | HIV-1 - immunology | HIV Antibodies - immunology | CD4 Antigens - chemistry | Protein Conformation | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | CD4 Antigens - metabolism | BASIC BIOLOGICAL SCIENCES | PNAS Plus | Biological Sciences
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10. Full Text CD4 mimetics sensitize HIV-1-infected cells to ADCC
by Jonathan Richard and Maxime Veillette and Nathalie Brassard and Shilpa S. Iyer and Michel Roger and Loïc Martin and Marzena Pazgier and Arne Schön and Ernesto Freire and Jean-Pierre Routy and Amos B. Smith and Jongwoo Park and David M. Jones and Joel R. Courter and Bruno N. Melillo and Daniel E. Kaufmann and Beatrice H. Hahn and Sallie R. Permar and Barton F. Haynes and Navid Madani and Joseph G. Sodroski and Andrés Finzi
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2015, Volume 112, Issue 20, pp. E2687 - E2694
HIV-1-infected cells presenting envelope glycoproteins (Env) in the CD4-bound conformation on their surface are preferentially targeted by antibody-dependent... 
HIV-1 | gp120 | CD4 mimetics | ADCC | Envelope glycoproteins | MULTIDISCIPLINARY SCIENCES | HUMAN-IMMUNODEFICIENCY-VIRUS | MINIPROTEINS | envelope glycoproteins | ENVELOPE | CYTOTOXICITY-MEDIATING ANTIBODIES | HIV-1 ENTRY | BINDING | NEUTRALIZATION | STRUCTURE-BASED DESIGN | EPITOPES | Recombinant Proteins - metabolism | CD4 Antigens - immunology | HIV Infections - prevention & control | Mutagenesis, Site-Directed | Humans | Antibody-Dependent Cell Cytotoxicity - immunology | env Gene Products, Human Immunodeficiency Virus - metabolism | CD4-Positive T-Lymphocytes - immunology | HIV-1 - immunology | Flow Cytometry | Recombinant Proteins - immunology | HEK293 Cells | HIV Infections - transmission | Protein Conformation | CD4 Antigens - metabolism | Immune response | Development and progression | Genetic aspects | Glycoproteins | Regulation | Properties | HIV infection | Biological Sciences | PNAS Plus
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11. Full Text Stoichiometric Analyses of Soluble CD4 to Native-like HIV-1 Envelope by Single-Molecule Fluorescence Spectroscopy
by Agrawal, Parul and DeVico, Anthony L and Foulke, James S and Lewis, George K and Pazgier, Marzena and Ray, Krishanu
Cell Reports, ISSN 2211-1247, 10/2019, Volume 29, Issue 1, pp. 176 - 186.e4
Analyses of HIV-1 envelope (Env) binding to CD4, and the conformational changes the interactions induce, inform the molecular mechanisms and factors governing... 
soluble CD4 | single-molecule fluorescence | cooperativity | HIV-1 Env trimers | stoichiometric analyses | association kinetics | ligand binding | INFECTIONS | CONTACT | STATES | ENTRY | GLYCOPROTEIN TRIMERS | IMMUNODEFICIENCY-VIRUS TYPE-1 | SURFACE | CONFORMATIONAL DYNAMICS | CRYO-EM STRUCTURE | ELECTRON TOMOGRAPHY | CELL BIOLOGY
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12. Epitope specificity of human immunodeficiency virus-1 antibody dependent cellular cytotoxicity [ADCC] responses
by Pollara, Justin and Bonsignori, Mattia and Moody, M. Anthony and Pazgier, Marzena and Haynes, Barton F and Ferrari, Guido
Current HIV Research, ISSN 1570-162X, 07/2013, Volume 11, Issue 5, pp. 378 - 387
Antibody dependent cellular cytotoxicity [ADCC] has been suggested to play an important role in control of Human Immunodeficiency Virus-1 [HIV-1] viral load... 
HIV-1 | Monoclonal antibodies | AIDS vaccines | Epitope | Humoral responses | Antibody dependent cellular cytotoxicity | humoral responses | INFECTIOUS DISEASES | FC-GAMMA RECEPTORS | MEDIATED CYTOTOXICITY | CD4 BINDING-SITE | HIV-1 VACCINE EFFICACY | EFFECTOR FUNCTION | HUMAN MONOCLONAL-ANTIBODY | ENVELOPE GLYCOPROTEIN | IMMUNOLOGY | VIROLOGY | antibody dependent cellular cytotoxicity | STRUCTURAL BASIS | BROADLY NEUTRALIZING ANTIBODY | epitope | GP41 ANTIBODIES | monoclonal antibodies | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | HIV Infections - prevention & control | HIV-1 - immunology | Antibody Specificity - immunology | HIV Antibodies - immunology | HIV Envelope Protein gp41 - immunology | Humans | AIDS Vaccines - immunology | Antibody-Dependent Cell Cytotoxicity - immunology | Epitopes, T-Lymphocyte - immunology
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13. Full Text Structural basis for epitopes in the gp120 cluster a region that invokes potent effector cell activity
by Tolbert, William D and Tolbert, William D and Sherburn, Rebekah T and Sherburn, Rebekah T and Van, Verna and Van, Verna and Pazgier, Marzena and Pazgier, Marzena
Viruses, ISSN 1999-4915, 01/2019, Volume 11, Issue 1, p. 69
While a number of therapeutic options to control the progression of human immunodeficiency virus (HIV-1) now exist, a broadly effective preventive vaccine is... 
A32 | C11 | Vaccine | HIV | Structure | ADCC | CRYSTAL-STRUCTURE | ENVELOPE GLYCOPROTEIN | MONOCLONAL-ANTIBODY | structure | ANTIGENIC PROPERTIES | HIV-1 GP120 | vaccine | VIROLOGY | BROADLY NEUTRALIZING ANTIBODIES | CD4-INDUCED EPITOPES | IMMUNODEFICIENCY-VIRUS TYPE-1 | CYTOTOXICITY-MEDIATING ANTIBODIES | CRYO-EM STRUCTURE
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14. Full Text Through the Looking Glass, Mechanistic Insights from Enantiomeric Human Defensins
by Gang Wei and Erik de Leeuw and Marzena Pazgier and Weirong Yuan and Guozhang Zou and Jianfeng Wang and Bryan Ericksen and Wei-Yue Lu and Robert I. Lehrer and Wuyuan Lu
Journal of Biological Chemistry, ISSN 0021-9258, 10/2009, Volume 284, Issue 42, pp. 29180 - 29192
Despite the small size and conserved tertiary structure of defensins, little is known at a molecular level about the basis of their functional versatility. For... 
ANTHRAX LETHAL TOXIN | D-AMINO ACIDS | HUMAN BETA-DEFENSINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CONSERVED SALT BRIDGE | LIPID-II | ESCHERICHIA-COLI | HUMAN ALPHA-DEFENSINS | ANTIMICROBIAL PEPTIDES | HUMAN NEUTROPHIL DEFENSINS | INNATE IMMUNITY | Surface Plasmon Resonance | Antigens, Bacterial - chemistry | alpha-Defensins - chemistry | Stereoisomerism | Aminobutyrates - chemistry | Humans | Alanine - chemistry | Cysteine - chemistry | Bacterial Toxins - chemistry | Bacterial Toxins - antagonists & inhibitors | Crystallography, X-Ray - methods | Microbial Sensitivity Tests | Animals | Escherichia coli - metabolism | Mice | Kinetics | Staphylococcus aureus - metabolism | Protein Structure and Folding
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