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PLoS Pathogens, ISSN 1553-7366, 09/2017, Volume 13, Issue 9, p. e1006614
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 02/2014, Volume 111, Issue 7, pp. E738 - E747
Journal Article
AMERICAN JOURNAL OF CANCER RESEARCH, ISSN 2156-6976, 2018, Volume 8, Issue 11, pp. 2150 - 2164
Prolactin-induced protein (PIP) is a small secreted glycoprotein carrying several N-linked carbohydrate chains. The expression of PIP is generally restricted... 
GCDFP-15 | HUMAN SEMINAL PLASMA | breast cancer | CD4-BINDING GLYCOPROTEIN | GCDFP-15 EXPRESSION | ACTIN-BINDING PROTEIN | gross cystic disease fluid protein 15 | PIP GENE | MOLECULAR PORTRAITS | ONCOLOGY | gp-17 | PIP | CYSTIC-DISEASE FLUID | GENE-EXPRESSION | GLYCOPROTEIN EP-GP | prolactin-induced protein | INDUCIBLE PROTEIN
Journal Article
Journal Article
Immunobiology, ISSN 0171-2985, 11/2019, Volume 224, Issue 6, pp. 811 - 816
The Prolactin Inducible Protein (PIP) is a 15 kDa protein secreted by normal apocrine glands, including salivary, lacrimal and sweat glands. PIP levels are... 
Bacteria | Biological function | Host defense | Cytokines | Breast diseases | Immunoregulation | HUMAN SEMINAL PLASMA | CD4-BINDING GLYCOPROTEIN | IMMUNOLOGY | GCDFP-15 EXPRESSION | IDENTIFICATION | CANCER | APOLIPOPROTEIN-D | INTERLEUKIN-1-ALPHA | SUBMAXILLARY-GLAND PROTEIN | BREAST-TUMOR | GENE-EXPRESSION
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
Immunity, ISSN 1074-7613, 08/2018, Volume 49, Issue 2, pp. 301 - 311.e5
An important class of HIV-1 broadly neutralizing antibodies, termed the VRC01 class, targets the conserved CD4-binding site (CD4bs) of the envelope... 
HIV-1 | eOD-GT8 | glycan masking | VRC01-class precursors | neutralizing antibody | VRC01 | CD4-binding site | single-cell sorting | transgenic mouse | vaccination | AMINO-ACID | IMMUNOGENICITY | VIRUS | STRUCTURAL BASIS | BROADLY NEUTRALIZING ANTIBODY | VACCINE DESIGN | BINDING-SITE | GP120 | IMMUNOLOGY | X-SER/THR SEQUON | ANTIGENIC DETERMINANTS | CD4 Antigens - immunology | Cell Line | HIV Infections - prevention & control | Binding Sites, Antibody - immunology | Humans | Mice, Inbred C57BL | AIDS Vaccines - immunology | Broadly Neutralizing Antibodies | Male | Mice, Transgenic | Gene Knock-In Techniques | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | Animals | HIV Antibodies - immunology | Polysaccharides - chemistry | Female | Mice | Immunoglobulin Heavy Chains - immunology | Antibodies, Monoclonal - immunology | Medical research | Immune response | Vaccination | Antibodies | B cells | HIV (Viruses) | Viral antibodies | Polysaccharides | Analysis | Islamic law | Resveratrol | Medicine, Experimental | Genetic engineering | Antigenic determinants | Immunoglobulin G | Clinical trials | Vaccines | Experiments | Nanoparticles | Proteins | Acquired immune deficiency syndrome--AIDS | Precursors | Human immunodeficiency virus--HIV | Masking | Crystal structure | Immunoglobulins | Statistical analysis | Glycoprotein | Priming | Epitopes | Glycan | Mutants | CD4 antigen | N-linked glycans | Lymphocytes B | Software | Mutation | Binding sites
Journal Article