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Journal of Biological Chemistry, ISSN 0021-9258, 04/2012, Volume 287, Issue 16, pp. 13170 - 13181
Bacterial lipoproteins/lipopeptides inducing host innate immune responses are sensed by mammalian Toll-like receptor 2 (TLR2). These bacterial lipoproteins are... 
OUTER-MEMBRANE | TOLL-LIKE-RECEPTOR-1 | GENOME SEQUENCE | IHEYA RIDGE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | STAPHYLOCOCCUS-AUREUS | KAPPA-B | APOLIPOPROTEIN N-ACYLTRANSFERASE | BACILLUS | CUTTING EDGE | Geobacillus - immunology | Toll-Like Receptor 2 - genetics | Bacillus cereus - immunology | Toll-Like Receptor 6 - immunology | Toll-Like Receptor 6 - genetics | Streptococcus sanguis - metabolism | Bacillus subtilis - immunology | Gram-Positive Bacteria - immunology | Geobacillus - metabolism | Pneumonia, Mycoplasma - metabolism | Enterococcus faecalis - immunology | Toll-Like Receptor 6 - metabolism | Lactobacillus - immunology | Pneumonia, Mycoplasma - immunology | Mice, Inbred C57BL | Toll-Like Receptor 1 - metabolism | Bacillus cereus - metabolism | Macrophages, Peritoneal - immunology | Toll-Like Receptor 2 - metabolism | Lactobacillus - metabolism | Gram-Positive Bacteria - metabolism | Toll-Like Receptor 1 - genetics | Animals | Enterococcus faecalis - metabolism | Macrophages, Peritoneal - microbiology | Toll-Like Receptor 2 - immunology | Mice | Toll-Like Receptor 1 - immunology | Streptococcus sanguis - immunology | Bacillus subtilis - metabolism | Host-Pathogen Interactions | Toll-like Receptors (TLR) | Immunology | Low-GC Content | Innate Immunity | Mass Spectrometry (MS) | Lipoprotein | Gram-positive Bacteria
Journal Article
Virology, ISSN 0042-6822, 2010, Volume 407, Issue 2, pp. 296 - 305
Abstract We have constructed stable virus-like particles displaying the HIV-1 Gag(p17) protein as an N-terminal fusion with an engineered protein domain from... 
Infectious Disease | Gag (p17) | vaccine | HIV | E2 scaffold | Virus-like particles | Vaccine | NEUTRALIZING MONOCLONAL-ANTIBODIES | PROTECTION | RHINOVIRUS | BACILLUS-STEAROTHERMOPHILUS | IMMUNIZATION | CHIMERIC VIRUS | VIROLOGY | EXPRESSION | T-CELLS | IMMUNODEFICIENCY | HIV Antibodies - blood | Recombinant Fusion Proteins - immunology | env Gene Products, Human Immunodeficiency Virus - immunology | Humans | AIDS Vaccines - immunology | env Gene Products, Human Immunodeficiency Virus - metabolism | Geobacillus stearothermophilus - genetics | Acyltransferases - metabolism | Acyltransferases - genetics | Recombinant Fusion Proteins - metabolism | Geobacillus stearothermophilus - metabolism | Lymphocyte Activation - immunology | env Gene Products, Human Immunodeficiency Virus - genetics | Geobacillus stearothermophilus - immunology | Peptide Fragments - immunology | Female | Peptide Fragments - genetics | Virion - immunology | HIV-1 - metabolism | Geobacillus stearothermophilus - enzymology | Immunization | Peptide Fragments - metabolism | Mice, Inbred C57BL | Bacterial Proteins - genetics | CD4-Positive T-Lymphocytes - metabolism | Acyltransferases - immunology | HIV-1 - genetics | HIV-1 - immunology | Animals | B-Lymphocytes - immunology | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | T-Lymphocytes - immunology | Mice | Mice, Inbred BALB C | Genetic Vectors | Interferon-gamma - biosynthesis | Gag(p17)
Journal Article
PLoS ONE, ISSN 1932-6203, 12/2014, Volume 9, Issue 12, p. e113463
Journal Article
Vaccine, ISSN 0264-410X, 2006, Volume 25, Issue 11, pp. 1993 - 2000
Journal Article
Journal Article
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2001, Volume 305, Issue 2, pp. 259 - 267
The acyltransferase components (E2) from the family of 2-oxo acid dehydrogenase multienzyme complexes form large protein scaffolds, to which multiple copies of... 
pyruvate dehydrogenase | multienzyme complex | peptide epitopes | macromolecular scaffolds | phage display | Macromolecular scaffolds | Pyruvate dehydrogenase | Phage display | Multienzyme complex | Peptide epitopes | FILAMENTOUS BACTERIOPHAGE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CIRCUMSPOROZOITE PROTEIN | FOREIGN PEPTIDES | CUBIC CORE | IMMUNOLOGICAL PROPERTIES | BACILLUS-STEAROTHERMOPHILUS | DEHYDROGENASE COMPLEXES | PHAGE-DISPLAY | GREEN-FLUORESCENT PROTEIN | Recombinant Fusion Proteins - immunology | Green Fluorescent Proteins | Molecular Weight | Peptides - genetics | Multienzyme Complexes - metabolism | Peptide Library | Epitopes - immunology | Peptides - metabolism | Base Sequence | Surface Properties | Protein Denaturation | Amino Acid Sequence | Rabbits | Geobacillus stearothermophilus - enzymology | Immunization | 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) | Peptides - immunology | Models, Molecular | Recombinant Fusion Proteins - chemistry | Pyruvate Dehydrogenase Complex - chemistry | Luminescent Proteins - genetics | Protein Conformation | Epitopes - chemistry | Ketone Oxidoreductases - metabolism | Epitopes - metabolism | Multienzyme Complexes - immunology | Molecular Sequence Data | Pyruvate Dehydrogenase Complex - genetics | Recombinant Fusion Proteins - metabolism | Pyruvate Dehydrogenase Complex - immunology | Plasmids - genetics | Luminescent Proteins - chemistry | Pyruvate Dehydrogenase Complex - metabolism | Peptides - chemistry | Electrophoresis, Polyacrylamide Gel | Plasmodium - genetics | Plasmodium - metabolism | Multienzyme Complexes - genetics | Epitopes - genetics | Ketone Oxidoreductases - genetics | Protein Folding | Proteins - immunology | Multienzyme Complexes - chemistry | Proteins - genetics | Animals | Proteins - metabolism | Ketone Oxidoreductases - immunology | Ketone Oxidoreductases - chemistry | Proteins - chemistry | Luminescent Proteins - metabolism | circumsporozoite protein
Journal Article
Journal of Antibiotics, ISSN 0021-8820, 03/2018, Volume 71, Issue 3, pp. 382 - 389
Journal Article
Journal Article
Journal Article
Biochemistry (Moscow), ISSN 0006-2979, 06/2006, Volume 71, Issue 6, pp. 685 - 691
Polyclonal antibodies produced after the immunization of a rabbit with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus stearothermophilus were... 
conformational states | antibodies | renaturation | glyceraldehyde-3-phosphate dehydrogenase | differential scanning calorimetry | inactivation | Life Sciences | Biochemistry, general | Microbiology | Biomedicine general | Bioorganic Chemistry | Antibodies | Differential scanning calorimetry | Glyceraldehyde-3-phosphate dehydrogenase | Conformational states | Inactivation | Renaturation | PROTEIN | PHOSPHORYLATING D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | OF-SITES REACTIVITY | PROBES | PURIFICATION | AFFINITY-CHROMATOGRAPHY | BINDING | SUBUNIT | Glyceraldehyde-3-Phosphate Dehydrogenases - immunology | Rabbits | Geobacillus stearothermophilus - enzymology | Antibodies - metabolism | Enzyme Inhibitors - metabolism | Multiprotein Complexes | Enzyme Inhibitors - pharmacology | Apoenzymes - immunology | Enzyme Activation - drug effects | Protein Folding | Antibodies - pharmacology | Animals | Holoenzymes - metabolism | Models, Biological | Apoenzymes - metabolism | Protein Denaturation | Glyceraldehyde-3-Phosphate Dehydrogenases - isolation & purification | Protein Binding | Bacterial Proteins - metabolism | Calorimetry, Differential Scanning | Protein Conformation | Bacterial Proteins - immunology | Glutaral - pharmacology | Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism | Proteins
Journal Article