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hydrogen-ion concentration (11) 11
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amino acids (10) 10
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1. Full Text Novel bacterial lipoprotein structures conserved in low-GC content gram-positive bacteria are recognized by toll-like receptor 2
by Kurokawa, Kenji and Ryu, Kyoung-Hwa and Ichikawa, Rie and Masuda, Akiko and Kim, Min-Su and Lee, Hanna and Chae, Jun-Ho and Shimizu, Takashi and Saitoh, Tatsuya and Kuwano, Koichi and Akira, Shizuo and Dohmae, Naoshi and Nakayama, Hiroshi and Lee, Bok Luel
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
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2. Full Text HIV-1 Gag p17 presented as virus-like particles on the E2 scaffold from Geobacillus stearothermophilus induces sustained humoral and cellular immune responses in the absence of IFNγ production by CD4+ T cells
by Caivano, Antonella and Doria-Rose, Nicole A and Buelow, Benjamin and Sartorius, Rossella and Trovato, Maria and D'Apice, Luciana and Domingo, Gonzalo J and Sutton, William F and Haigwood, Nancy L and De Berardinis, Piergiuseppe
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)
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3. Full Text Multimeric scaffolds displaying the HIV-1 Envelope mper induce mper-specific antibodies and cross-neutralizing antibodies when Co-Immunized with gp160 DNA
by Krebs, Shelly J and McBurney, Sean P and Kovarik, Dina N and Waddell, Chelsea D and Jaworski, J. Pablo and Sutton, William F and Gomes, Michelle M and Trovato, Maria and Waagmeester, Garret and Barnett, Susan J and DeBerardinis, Piergiuseppe and Haigwood, Nancy L
PLoS ONE, ISSN 1932-6203, 12/2014, Volume 9, Issue 12, p. e113463
Developing a vaccine that overcomes the diversity of HIV-1 is likely to require a strategy that directs antibody (Ab) responses toward conserved regions of the... 
INTERMOLECULAR DISULFIDE BOND | PROXIMAL EXTERNAL REGION | MULTIDISCIPLINARY SCIENCES | VARIABLE REGIONS | PASSIVE TRANSFER | IMMUNODEFICIENCY-VIRUS TYPE-1 | DEHYDROGENASE MULTIENZYME COMPLEX | VACCINE EFFICACY | MONOCLONAL-ANTIBODIES | BACILLUS-STEAROTHERMOPHILUS | IMMUNOLOGICAL CHARACTERIZATION | HIV-1 - metabolism | Rabbits | HIV Envelope Protein gp41 - genetics | Enzyme-Linked Immunosorbent Assay | Electrophoresis, Polyacrylamide Gel | AIDS Vaccines - immunology | Biolistics | Neutralization Tests | DNA Primers - genetics | Blotting, Western | Antibodies, Neutralizing - immunology | Animals | Analysis of Variance | Plasmids - genetics | HIV Envelope Protein gp160 - genetics | Antibodies, Viral - immunology | Bacterial Proteins - metabolism | HIV Envelope Protein gp160 - immunology | Geobacillus stearothermophilus | Viral antibodies | Antibodies | Vaccines | HIV (Viruses) | Vaccination | DNA | Immunization | Immune response | Glycoprotein gp41 | Particulates | Viruses | DNA vaccines | Immunodominance | Glycoprotein gp160 | E2 protein | Acquired immune deficiency syndrome--AIDS | Human immunodeficiency virus--HIV | Neutralizing | Scaffolds | Target detection | Deoxyribonucleic acid--DNA | Immune system | AIDS | HIV | Acquired immune deficiency syndrome | Deoxyribonucleic acid | Human immunodeficiency virus
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4. Full Text Comparative analysis of new innovative vaccine formulations based on the use of procaryotic display systems
by D’Apice, Luciana and Sartorius, Rossella and Caivano, Antonella and Mascolo, Dina and Del Pozzo, Giovanna and Di Mase, Donatella Scotto and Ricca, Ezio and Pira, Giuseppina Li and Manca, Fabrizio and Malanga, Donatella and De Palma, Raffaele and De Berardinis, Piergiuseppe
Vaccine, ISSN 0264-410X, 2006, Volume 25, Issue 11, pp. 1993 - 2000
Abstract A T helper epitope was expressed in three innovative delivery vehicles recently developed in our laboratories and based respectively, on the... 
Allergy and Immunology | Filamentous bacteriophage fd | Pyruvate dehydrogenase | Macromolecular scaffolds | pyruvate dehydrogenase | MEDICINE, RESEARCH & EXPERIMENTAL | CELLS | CYTOLYTIC RESPONSES | RECOGNITION | COMPARTMENTS | IMMUNOLOGY | filamentous bacteriophage fd | VETERINARY SCIENCES | macromolecular scaffolds | PROTEINS | CLASS-II | MULTIENZYME COMPLEX | EPITOPES | ANTIGEN | Cell Line | Cell Proliferation | Humans | Bacterial Proteins - genetics | Vaccines - immunology | Epitopes, T-Lymphocyte - genetics | Geobacillus stearothermophilus - genetics | Bacteriophage M13 - immunology | Bacteriophage M13 - genetics | Vaccines - genetics | Spores, Bacterial - genetics | T-Lymphocytes, Helper-Inducer - immunology | Leukocytes, Mononuclear - immunology | Spores, Bacterial - immunology | T-Lymphocytes - immunology | Bacterial Proteins - immunology | Epitopes, T-Lymphocyte - immunology | Interleukin-2 - biosynthesis | Comparative analysis | Vaccines | Proteins | Antigens | Peptides | E coli | Lymphocytes | T cell receptors | Bacteriology | Chromatography | Immune system
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5. Full Text Apparent isocitrate lyase activity in Leishmania amazonensis
by Hernández-Chinea, Concepción and Maimone, Laura and Campos, Yelitza and Mosca, Walter and Romero, Pedro J
Acta Parasitologica, ISSN 1230-2821, 10/2017, Volume 62, Issue 4, pp. 701 - 707
Early reports have demonstrated the occurrence of glyoxylate cycle enzymes in several Leishmania species. However, these results have been underestimated... 
Medical Microbiology | isocitrate lyase | Parasitology | Biomedicine | Microbiology | promastigote | glyoxylate cycle | Ecology | malate synthase | Animal Systematics/Taxonomy/Biogeography | Leishmania amazonensis | MYCOBACTERIUM-TUBERCULOSIS | MACROPHAGES | PARASITOPHOROUS VACUOLES | MOONLIGHTING PROTEINS | VIRULENCE | MEXICANA | ENZYME | METABOLISM | PURIFICATION | PARASITOLOGY | Isocitrate Lyase - antagonists & inhibitors | Geobacillus stearothermophilus - enzymology | Isocitrate Lyase - genetics | Isocitrate Lyase - metabolism | Animals | Geobacillus stearothermophilus - immunology | Leishmania mexicana - enzymology | Antibodies, Bacterial - immunology | Mice | Gene Expression Regulation, Enzymologic - physiology | Isocitrate Lyase - immunology | Succinates - pharmacology | Leishmania | Lyases | Genetic aspects | Enzymes | Promastigotes | Antibodies | Immunoblotting | Genomes | Pattern recognition | Isocitrate lyase | Enzymatic activity | Malate | Malate synthase | Microtubules | Spectrophotometry | Immunofluorescence | Stains | Glyoxylate cycle | Cytoplasm
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6. Full Text Induction of specific T-helper and cytolytic responses to epitopes displayed on a virus-like protein scaffold derived from the pyruvate dehydrogenase multienzyme complex
by Domingo, Gonzalo J and Caivano, Antonella and Sartorius, Rossella and Barba, Pasquale and Bäckström, Malin and Piatier-Tonneau, Dominique and Guardiola, John and De Berardinis, Piergiuseppe and Perham, Richard N
Vaccine, ISSN 0264-410X, 2003, Volume 21, Issue 13, pp. 1502 - 1509
The icosahedral protein scaffold (1.5MDa) generated by self-assembly of the catalytic domains of the dihydrolipoyl acetyltransferase core of the pyruvate... 
Dihydrolipoyl acetyltransferase | Antigen presentation | CTL response | MEDICINE, RESEARCH & EXPERIMENTAL | DESIGN | antigen presentation | CELL EPITOPES | PARTICLES | IMMUNOLOGY | BACILLUS-STEAROTHERMOPHILUS | PROTECTIVE EFFICACY | dihydrolipoyl acetyltransferase | IMMUNIZATION | IMMUNOGENICITY | VETERINARY SCIENCES | EXPRESSION | DOMAINS | LYMPHOCYTES | T-Lymphocytes, Cytotoxic - immunology | Catalytic Domain | Geobacillus stearothermophilus - enzymology | HLA-A2 Antigen - immunology | Humans | Epitopes, T-Lymphocyte | Dihydrolipoyllysine-Residue Acetyltransferase | Animals | B-Lymphocytes - immunology | Antigen Presentation | Pyruvate Dehydrogenase Complex - immunology | Bacterial Proteins - immunology | Mice | Acetyltransferases - immunology | Antigens | Enzymes | Polypeptides | Dehydrogenases | T cell receptors | Vaccines | Proteins | Acquired immune deficiency syndrome--AIDS | E coli | Microscopy | Plasmids | Deoxyribonucleic acid--DNA | Symmetry
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7. Full Text Multiple Display of Peptides and Proteins on a Macromolecular Scaffold Derived from a Multienzyme Complex
by Domingo, Gonzalo J and Orru', Stefania and Perham, Richard N
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
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8. Full Text New recombinant vaccines based on the use of prokaryotic antigen-display systems
by De Berardinis, Piergiuseppe and Haigwood, Nancy L
Expert Review of Vaccines, ISSN 1476-0584, 12/2004, Volume 3, Issue 6, pp. 673 - 679
A major challenge in vaccine design has been to identify antigen presentation systems that elicit strong T- and B-cell responses. In the authors' laboratory,... 
filamentous bacteriophage | pyruvate dehydrogenase multienzyme complex | Pyruvate dehydrogenase multienzyme complex | Filamentous bacteriophage | Humans | Geobacillus stearothermophilus - genetics | Peptide Library | Pyruvate Dehydrogenase Complex - genetics | Bacteriophage M13 - immunology | Epitopes - genetics | Drug Delivery Systems | Epitopes - immunology | Bacteriophage M13 - genetics | Molecular Mimicry | Animals | Geobacillus stearothermophilus - immunology | Pyruvate Dehydrogenase Complex - immunology | Capsid Proteins - immunology | Vaccines, Synthetic - administration & dosage | Capsid Proteins - genetics | Vaccines | Antigenic determinants
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9. Full Text Antibiotic resistance mutations induced in growing cells of Bacillus-related thermophiles
by Suzuki, Hirokazu and Taketani, Tatsunari and Kobayashi, Jyumpei and Ohshiro, Takashi
Journal of Antibiotics, ISSN 0021-8820, 03/2018, Volume 71, Issue 3, pp. 382 - 389
Stress-induced mutagenesis can assist pathogens in generating drug-resistant cells during antibiotic therapy; however, if and how antibiotics induce... 
GEOBACILLUS-KAUSTOPHILUS HTA426 | DEOXYRIBONUCLEIC-ACID | COUPLING FACTOR | ESCHERICHIA-COLI | MICROBIOLOGY | MISMATCH REPAIR | IMMUNOLOGY | DNA-POLYMERASES | STATIONARY-PHASE MUTAGENESIS | CYTOSINE RESIDUES | RIFAMPIN RESISTANCE | SUBTILIS | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PHARMACOLOGY & PHARMACY | Mutation | Antibiotics | Mutagenesis | Deoxyribonucleic acid--DNA | Index Medicus
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10. Full Text A recombinant bacterial cell surface (S-layer)-major birch pollen allergen-fusion protein (rSbsC/Bet v1) maintains the ability to self-assemble into regularly structured monomolecular lattices and the functionality of the allergen
by Breitwieser, Andreas and Egelseer, Eva M and Moll, Dieter and Ilk, Nicola and Hotzy, Christoph and Bohle, Barbara and Ebner, Christof and Sleytr, Uwe B and Sára, Margit
Protein Engineering, ISSN 0269-2139, 3/2002, Volume 15, Issue 3, pp. 243 - 249
The mature crystalline bacterial cell surface (S-layer) protein SbsC of Bacillus stearothermophilus ATCC 12980 comprises amino acids 31–1099 and assembles into... 
Bacillus stearothermophilus | Recombinant fusion protein | Major birch pollen allergen | S-layer protein | MOLECULAR CHARACTERIZATION | STRAINS | SEQUENCE-ANALYSIS | S-LAYER PROTEINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | major birch pollen allergen | BACILLUS-STEAROTHERMOPHILUS ATCC-12980 | BET-V-1 | GENE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | WALL POLYMER | PURIFICATION | recombinant fusion protein | EXPRESSION | Recombinant Fusion Proteins - immunology | Antigens, Plant | Bacterial Proteins - genetics | Crystallization | Immunoblotting | Plant Proteins - immunology | Allergens - genetics | Recombinant Fusion Proteins - chemistry | Membrane Glycoproteins - genetics | Plant Proteins - genetics | Immunoglobulin E - immunology | Allergens - immunology | Protein Engineering | Recombinant Fusion Proteins - genetics | Geobacillus stearothermophilus
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11. Full Text Immunomagnetic detection of Bacillus stearothermophilus spores in food and environmental samples
by M R Blake and B C Weimer
Applied and Environmental Microbiology, ISSN 0099-2240, 05/1997, Volume 63, Issue 5, pp. 1643 - 1646
Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon... 
K QU MICROBIOLOGY | K DB BIOTECHNOLOGY & APPLIED MICROBIOLOGY | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ESCHERICHIA-COLI | RAPID ISOLATION | SALMONELLA | MICROBIOLOGY | SEPARATION | Spores, Bacterial - isolation & purification | Milk - microbiology | Avidin - immunology | Enzyme-Linked Immunosorbent Assay | Soil Microbiology | Colony Count, Microbial | Food Microbiology | Immunomagnetic Separation - methods | Animals | Geobacillus stearothermophilus - immunology | Environmental Microbiology | Immunoglobulin G - immunology | Sensitivity and Specificity | Antibodies, Bacterial - immunology | Spores, Bacterial - immunology | Biotin - immunology | Bacillus (Bacteria) | Pathogenic microorganisms | Identification and classification | Analysis | Bacteriology | Methods
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12. Full Text The effects of a thermophile metabolite, tryptophol, upon protecting shrimp against white spot syndrome virus
by Zhu, Fei and Jin, Min
Fish and Shellfish Immunology, ISSN 1050-4648, 12/2015, Volume 47, Issue 2, pp. 777 - 781
White spot syndrome virus (WSSV) is a shrimp pathogen responsible for significant economic loss in commercial shrimp farms and until now, there has been no... 
Tryptophol | White spot syndrome virus | Thermophile metabolite | Shrimp | Marsupenaeus japonicus | FISHERIES | NATURAL-PRODUCTS | BACULOVIRUS | MARINE & FRESHWATER BIOLOGY | VETERINARY SCIENCES | IMMUNOLOGY | EXPERIMENTAL-INFECTION | Penaeidae - virology | Bacteriophages - drug effects | Metabolome | Geobacillus - virology | Dietary Supplements - analysis | Penaeidae - physiology | White spot syndrome virus 1 - drug effects | Animals | Animal Feed - analysis | Indoles - pharmacology | Bacteriophages - physiology | Geobacillus - metabolism | Aquaculture | Antiviral agents | Metabolites | Health aspects | Analysis | Aquaculture industry | Dietary supplements
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13. Full Text A DNA break inducer activates the anticodon nuclease RloC and the adaptive immunity in Acinetobacter baylyi ADP1
by Klaiman, Daniel and Steinfels-Kohn, Emmanuelle and Kaufmann, Gabriel
Nucleic Acids Research, ISSN 0305-1048, 01/2014, Volume 42, Issue 1, pp. 328 - 339
Double-stranded DNA breaks (DSB) cause bacteria to augment expression of DNA repair and various stress response proteins. A puzzling exception educes the... 
RESTRICTION-MODIFICATION SYSTEMS | CHROMOSOME | ENDONUCLEASE | DETERMINANTS | TRANSFER-RNA REPAIR | PRRC | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | ZINC-HOOK | POLYNUCLEOTIDE KINASE | LIGASE | Adaptive Immunity | Acinetobacter - enzymology | Acinetobacter - immunology | RNA, Transfer, Glu - metabolism | Enzyme Stability | RNA Cleavage | Adenosine Diphosphate - metabolism | Enzyme Activation | Geobacillus - enzymology | RNA, Transfer, Gln - metabolism | DNA Breaks, Double-Stranded | Ribonucleases - metabolism | Genome Integrity, Repair and
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14. Full Text Safety evaluation of a thermolysin enzyme produced from Geobacillus stearothermophilus
by Ke, Qingdong and Chen, Alice and Minoda, Masashi and Yoshida, Hiromichi
Food and Chemical Toxicology, ISSN 0278-6915, 09/2013, Volume 59, pp. 541 - 548
Thermolysin is a zinc metalloprotease that has potential uses in the food industry. The safety of thermolysin has not been demonstrated before, and therefore a... 
Thermolysin | Geobacillus stearothermophilus | Safety | Toxicity | Food | GENE | CLONING | FOOD SCIENCE & TECHNOLOGY | Geobacillus stearotherrnophilus | TOXICOLOGY | BACILLUS-STEAROTHERMOPHILUS | EXPRESSION | Antigens, Bacterial - adverse effects | Allergens - adverse effects | Bacterial Proteins - adverse effects | Cricetulus | Rats, Wistar | Male | Toxicity Tests, Acute | Micronucleus Tests | Allergens - administration & dosage | Geobacillus stearothermophilus - immunology | Mutagenicity Tests | Female | Cell Line | Cricetinae | Food Additives - administration & dosage | Geobacillus stearothermophilus - enzymology | Rats | Toxicity Tests, Subchronic | Antigens, Bacterial - administration & dosage | Mice, Inbred Strains | Rats, Sprague-Dawley | Bacterial Proteins - administration & dosage | Food Additives - adverse effects | No-Observed-Adverse-Effect Level | Animals | Thermolysin - adverse effects | Mice | Thermolysin - administration & dosage | Enzymes | Analysis | Safety and security measures | Index Medicus
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15. Full Text Antibodies to inactive conformations of glyceraldehyde-3-phosphate dehydrogenase inactivate the apo-and holoforms of the enzyme
by Arutiunova, E and Pleten, A and Nagradova, N and Muronetz, V
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
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