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BMC Biotechnology, ISSN 1472-6750, 08/2018, Volume 18, Issue 1, pp. 47 - 11
Background: Ricin A chain (RTA) and Pokeweed antiviral proteins (PAPs) are plant-derived N-glycosidase ribosomal-inactivating proteins (RIPs) isolated from... 
Ribosome-inactivating proteins | Antiviral agent | Hepatitis B virus | Ricin | Fusion proteins | Pokeweed antiviral protein | ISOFORMS | ANTI-CD19 | PEPTIDE | PREDICTION | REPLICATION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | RESISTANCE | INFECTION | SPECTRUM | LINEAGE | Recombinant Fusion Proteins - biosynthesis | Ribosome Inactivating Proteins, Type 1 - genetics | Antiviral Agents - pharmacology | Plant Proteins - pharmacology | Recombinant Fusion Proteins - pharmacology | Ribosome Inactivating Proteins, Type 1 - biosynthesis | Ribosome Inactivating Proteins, Type 1 - pharmacology | Ricin - biosynthesis | Ricin - pharmacology | Hepatitis B virus - drug effects | Plant Proteins - genetics | Escherichia coli - genetics | Recombinant Fusion Proteins - genetics | Protein Biosynthesis - drug effects | Ricin - genetics | Plant Proteins - biosynthesis | Medical virology | Physiological aspects | Lectins | Pokeweed | Chemical properties | Research | Virus research | Health aspects | Seeds | Toxicity | Protein purification | Leukemia | Chronic infection | Cytotoxicity | Viruses | Servers | Assaying | Transgenic plants | Proteins | Hepatitis | Lysates | Leaves | E coli | Inclusion bodies | Antiviral activity | Biocompatibility | Inhibition | Fusion protein | N-glycosidase | Deoxyribonucleic acid--DNA | Antiviral agents | Protein biosynthesis | Steric hindrance | Plants | Protein synthesis | Gel filtration | Viability | Hepatitis B
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2010, Volume 395, Issue 5, pp. 897 - 907
Ribosome-inactivating proteins (RIPs) are -glycosidases that depurinate a specific adenine residue in the conserved sarcin/ricin loop of ribosomal RNA. This... 
protein–protein interaction | maize ribosome-inactivating protein | ribosomal stalk protein P2 | NMR | translation inhibition | protein-protein interaction | ALPHA-SARCIN | RNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CHEMICAL-SHIFT | N-GLYCOSIDASE ACTIVITY | PROENZYME ACTIVATION | EUKARYOTIC RIBOSOMES | POKEWEED ANTIVIRAL PROTEIN | PLANTS | RICIN A-CHAIN | Ribosomal Proteins - chemistry | Zea mays - chemistry | Molecular Sequence Data | Crystallography, X-Ray | Phosphoproteins - metabolism | Phosphoproteins - chemistry | Ribosomal Proteins - metabolism | Plant Proteins - chemistry | Nuclear Magnetic Resonance, Biomolecular | Plant Proteins - metabolism | Protein Interaction Domains and Motifs | Zea mays - metabolism | Binding Sites | Recombinant Proteins - metabolism | Ribosome Inactivating Proteins - chemistry | Amino Acid Sequence | Zea mays - genetics | Ribosome Inactivating Proteins - genetics | Ribosomal Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Phosphoproteins - genetics | Static Electricity | Ribosome Inactivating Proteins - metabolism | Sequence Homology, Amino Acid | Plant Proteins - genetics | Protein Conformation | Mutation | Purines | Antiviral agents | Ribosomal proteins | Ribosomal RNA | Lectins | Corn | Protein biosynthesis | Protein binding
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2016, Volume 11, Issue 7, p. e0159653
In contrast to conventional antibiotics, which microorganisms can readily evade, it is nearly impossible for a microbial strain that is sensitive to... 
PHARMACEUTICAL PROTEINS | APOPTOSIS | IN-VITRO | PEPTIDES | AGROBACTERIUM-RHIZOGENES | MULTIDISCIPLINARY SCIENCES | GENE-EXPRESSION | GLOBULAR-PROTEINS | THERMOSTABILITY | RIBOSOME-INACTIVATING PROTEINS | CULTURES | Anti-HIV Agents - pharmacology | Temperature | Escherichia coli - drug effects | Ribosome Inactivating Proteins, Type 2 - chemistry | Plant Roots - genetics | Microbial Sensitivity Tests | Recombinant Proteins - isolation & purification | Plants, Genetically Modified | Plasmids - genetics | Conserved Sequence | Protein Interaction Domains and Motifs | Ribosome Inactivating Proteins, Type 2 - pharmacology | Protein Stability | Gene Order | Amino Acid Sequence | Gene Expression | Position-Specific Scoring Matrices | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Recombinant Proteins - pharmacology | Tobacco - genetics | Ribosome Inactivating Proteins, Type 2 - genetics | Hydrophobic and Hydrophilic Interactions | Antineoplastic Agents, Phytogenic - pharmacology | Hydrogen-Ion Concentration | Ribosome Inactivating Proteins, Type 2 - isolation & purification | Care and treatment | Analysis | Genetic engineering | Genetic aspects | Research | HIV (Viruses) | Tobacco (Plant) | Health aspects | Infection control | Cancer | Cell culture | Hairy root | Antimicrobial activity | Peptides | Pathogenesis | Roots | Transgenic | Amino acids | Kinases | pH effects | Anticancer properties | Proteins | Microorganisms | Ribosome-inactivating protein | Antitumor agents | Human immunodeficiency virus--HIV | Antibacterial activity | Bacteria | Recombinant | Enzymes | Preservatives | Gravy | Thermophilic microorganisms | Stability analysis | Aliphatic compounds | Cost control | Antibiotics | Lectins | HIV | Human immunodeficiency virus
Journal Article
The New England Journal of Medicine, ISSN 0028-4793, 07/2017, Volume 377, Issue 1, pp. 52 - 61
CD55 prevents convertase enzyme formation in the complement cascade, acting as a brake on complement activation. Inactivating mutations in CD55 result in... 
Protein-Losing Enteropathies | Complement Activation | Intestine, Small | T-Lymphocytes | Humans | Child, Preschool | Complement Inactivating Agents | Infant | Male | Immunoglobulin A | Thrombosis | Syndrome | Journal Article | Complement System Proteins | Homozygote | Pedigree | Statistics, Nonparametric | Female | Mutation | CD55 Antigens | Child | MEDICINE, GENERAL & INTERNAL | ACTIVATION | INFLAMMATORY-BOWEL-DISEASE | HEMOLYTIC-UREMIC SYNDROME | CELL RESPONSES | COMPLEMENT REGULATORY PROTEIN | INAB PHENOTYPE | DECAY-ACCELERATING FACTOR | PAROXYSMAL-NOCTURNAL HEMOGLOBINURIA | MEMBRANOPROLIFERATIVE GLOMERULONEPHRITIS | T-CELLS | Intestine, Small - pathology | CD55 Antigens - genetics | Protein-Losing Enteropathies - genetics | Complement System Proteins - metabolism | CD55 Antigens - blood | Complement Activation - genetics | T-Lymphocytes - metabolism | Complement Inactivating Agents - pharmacology | Protein-Losing Enteropathies - complications | Immunoglobulin A - blood | Thrombosis - genetics | Complement Activation - drug effects | Proteins | Molecular targeted therapy | Gene mutations | Gastrointestinal diseases | Analysis | Homeostasis | Research | Blood clot | Gastrointestinal tract diseases | Complement component C5a | Lymphocytes T | Cell activation | Immunology | Pain | Intestine | Hepatology | Gastroenterology | Malabsorption | Thromboembolism | Digestive tract | Age | Edema | Medical research | Lymphatic system | Hypersensitivity | Diarrhea | Inflammation | Heredity | Protein deficiency | Patients | Hereditary diseases | Complement activation | Infectious diseases | Decay-accelerating factor
Journal Article
Protein Science, ISSN 0961-8368, 03/2013, Volume 22, Issue 3, pp. 280 - 286
The full or partial unfolding of proteins is widely believed to play an essential role in three‐dimensional domain swapping. However, there is little research... 
SARS‐CoV main protease | protein unfolding | domain swapping | thioredoxin | thermodynamics | protein folding | Cyanovirin‐N | kinetics | Cyanovirin-N | Thermodynamics | Protein folding | Domain swapping | Protein unfolding | Kinetics | Thioredoxin | SARS-CoV main protease | BIOCHEMISTRY & MOLECULAR BIOLOGY | STATE | DIMER | C-TERMINAL DOMAIN | INACTIVATING PROTEIN | Cysteine Endopeptidases - chemistry | Protein Unfolding | Bacterial Proteins - chemistry | Viral Proteins - metabolism | Cysteine Endopeptidases - metabolism | Thioredoxins - genetics | Protein Denaturation | Algal Proteins - genetics | Carrier Proteins - chemistry | Thioredoxins - metabolism | Thioredoxins - chemistry | Dimerization | Peptide Fragments - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Algal Proteins - chemistry | Oxidation-Reduction | Viral Proteins - chemistry | Bacterial Proteins - genetics | Mutant Proteins - genetics | Protein Refolding | Models, Molecular | Recombinant Proteins - chemistry | Viral Proteins - genetics | Mutant Proteins - metabolism | Carrier Proteins - genetics | Peptide Fragments - chemistry | Carrier Proteins - metabolism | Cysteine Endopeptidases - genetics | Mutant Proteins - chemistry | Bacterial Proteins - metabolism | Algal Proteins - metabolism | Amino Acid Substitution | Proteins | Proteases | Analysis | Denaturation
Journal Article
The Plant Journal, ISSN 0960-7412, 01/2011, Volume 65, Issue 2, pp. 218 - 229
Summary The fate of the type I ribosome‐inactivating protein (RIP) saporin when initially targeted to the endoplasmic reticulum (ER) in tobacco protoplasts has... 
signal peptide | toxicity | saporin | ricin | endoplasmic reticulum | ribosome‐inactivating protein | ribosome-inactivating protein | WILD-TYPE | B-CHAIN | VIRUS-RESISTANCE | QUALITY-CONTROL | PLANT SCIENCES | RICIN-A-CHAIN | SAPONARIA-OFFICINALIS | POKEWEED ANTIVIRAL PROTEIN | ENDOPLASMIC-RETICULUM | STORAGE VACUOLES | RNA N-GLYCOSIDASE | Ribosome Inactivating Proteins, Type 1 - genetics | Molecular Chaperones - metabolism | Protein Sorting Signals - physiology | Stress, Physiological | Endoplasmic Reticulum - metabolism | Molecular Sequence Data | Ribosomes - metabolism | Recombinant Fusion Proteins - metabolism | Protoplasts - metabolism | Plant Proteins - metabolism | Saponaria - genetics | Amino Acid Sequence | Endoplasmic Reticulum - genetics | Protein Synthesis Inhibitors - toxicity | Tobacco - metabolism | Molecular Chaperones - genetics | Saponaria - toxicity | Glycosylation | Protein Synthesis Inhibitors - metabolism | Protoplasts - drug effects | Protein Transport | Plant Proteins - genetics | Ribosome Inactivating Proteins, Type 1 - toxicity | Ribosome Inactivating Proteins, Type 1 - metabolism | Protein Sorting Signals - genetics | Tobacco - genetics | Gene Expression Regulation, Plant - physiology | Intracellular Space - metabolism | Protein Isoforms | Ribosomes - drug effects | Recombinant Fusion Proteins - genetics | Saponaria - metabolism | Lectins | Protein biosynthesis | Stress (Physiology) | Peptides | Proteins | Plant biology | Signal transduction | Tobacco | Cellular biology | Ribonucleic acid--RNA | Chaperones
Journal Article
Molecular Plant Pathology, ISSN 1464-6722, 02/2016, Volume 17, Issue 2, pp. 261 - 271
Journal Article