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Nature, ISSN 0028-0836, 12/2016, Volume 540, Issue 7631, pp. 80 - 85
In all domains of life, selenocysteine (Sec) is delivered to the ribosome by selenocysteine-specific tRNA (tRNA(Sec)) with the help of a specialized... 
EF-TU | AMINOACYL-TRANSFER-RNA | MESSENGER-RNA | RECOGNITION | FACTOR-TU | CRYSTAL-STRUCTURE | ACTIVE-ROLE | MULTIDISCIPLINARY SCIENCES | HYDROLYSIS | BINDING | SELENOCYSTEINE INCORPORATION | Selenocysteine - metabolism | Protein Biosynthesis | Ribosome Subunits, Large, Bacterial - metabolism | Codon, Terminator - genetics | Bacterial Proteins - chemistry | RNA, Transfer, Amino Acid-Specific - metabolism | Ribosomes - metabolism | GTP Phosphohydrolases - ultrastructure | Ribosomes - enzymology | Escherichia coli - metabolism | Protein Domains | Nucleic Acid Conformation | Binding Sites | Codon, Terminator - chemistry | Ribosome Subunits, Small, Bacterial - metabolism | Endoribonucleases - metabolism | Ribosome Subunits, Large, Bacterial - ultrastructure | Ribosomes - chemistry | Models, Molecular | RNA, Transfer, Amino Acid-Specific - genetics | Escherichia coli - chemistry | Codon, Terminator - metabolism | Cryoelectron Microscopy | RNA, Transfer, Amino Acid-Specific - chemistry | Ribosome Subunits, Small, Bacterial - ultrastructure | Ribosomes - ultrastructure | GTP Phosphohydrolases - metabolism | Ricin - metabolism | Escherichia coli - genetics | Ribosome Subunits, Large, Bacterial - chemistry | Protein Binding | Bacterial Proteins - metabolism | Bacterial Proteins - ultrastructure | Enzyme Activation | RNA, Transfer, Amino Acid-Specific - ultrastructure | Ribosome Subunits, Small, Bacterial - chemistry | Escherichia coli - ultrastructure | Fungal Proteins - metabolism | Physiological aspects | Protein research | Protein biosynthesis | Research | Guanosine triphosphatase | Ribosomes | Enzymes | E coli | Ribonucleic acid--RNA | Crystal structure
Journal Article
PLoS biology, ISSN 1544-9173, 11/2018, Volume 16, Issue 11, pp. e2006951 - e2006951
Glycosylation is a fundamental modification of proteins and membrane lipids. Toxins that utilize glycans as their receptors have served as powerful tools to... 
SPHINGOLIPID METABOLISM | LAPTM4B | CLONING | RETROGRADE TRANSPORT | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | BIOLOGY | MEMBRANE-PROTEIN | DISORDERS | REQUIRES | MULTIDRUG-RESISTANCE | EXPRESSION | Shiga Toxins - genetics | Trihexosylceramides - metabolism | Humans | Oncogene Proteins - metabolism | Glycosylation | Golgi Apparatus - physiology | Glycolipids - metabolism | Endosomes - metabolism | Membrane Transport Proteins - physiology | Protein Transport | Bacterial Toxins - metabolism | Shiga Toxins - metabolism | Glycosphingolipids | Trihexosylceramides - physiology | Ricin - metabolism | CRISPR-Cas Systems | HEK293 Cells | Golgi Apparatus - metabolism | Membrane Transport Proteins - metabolism | Ricin - genetics | Membrane Proteins - metabolism | HeLa Cells | Genome-Wide Association Study - methods | Loss of Function Mutation - genetics | Globotriaosylceramide | Health sciences | Toxicity | Trafficking | Lipids | Homology | Biology | Biochemistry | Genomes | Biosynthesis | Urology | Medical schools | Defects | Cell adhesion & migration | Proteins | Receptors | Polysaccharides | Surgery | University colleges | Crystal structure | CRISPR | Therapeutic applications | Ricin | Mass spectroscopy | Screens | Golgi apparatus | Membrane proteins | Domains | Hospitals | Insects | Glycolipids | Scientific imaging | Toxins | Mass spectrometry | Endoplasmic reticulum | Binding sites | Index Medicus
Journal Article
Toxicology Letters, ISSN 0378-4274, 09/2016, Volume 258, pp. 11 - 19
The plant-derived toxins ricin and abrin, operate by site-specific depurination of ribosomes, which in turn leads to protein synthesis arrest. The clinical... 
Abrin | Ricin | Depurination | 28SrRNA | Lung | ACTIVATED PROTEIN-KINASE | RNA | MACROPHAGES | SHIGA TOXIN | DEOXYNIVALENOL | HUMAN POLYMORPHONUCLEAR LEUKOCYTES | CHAIN | TOXICOLOGY | RIBOSOME-INACTIVATING PROTEINS | RIBOTOXIC STRESS-RESPONSE | Poisoning - metabolism | Protein Synthesis Inhibitors - chemistry | Respiratory Mucosa - drug effects | Poisoning - physiopathology | Pneumonia - prevention & control | RNA, Ribosomal, 28S - metabolism | Respiratory Insufficiency - etiology | Ribosomes - metabolism | Cytotoxins - administration & dosage | Ricinus - enzymology | Abrin - administration & dosage | Cytotoxins - toxicity | Abrin - isolation & purification | Protein Synthesis Inhibitors - administration & dosage | Respiratory Mucosa - pathology | Ribosomes - enzymology | Abrus - enzymology | Antitoxins - therapeutic use | Flow Cytometry | Respiratory Insufficiency - prevention & control | Abrin - toxicity | Cytotoxins - metabolism | Female | Lung - metabolism | Ricin - antagonists & inhibitors | Cytotoxins - antagonists & inhibitors | Lung - pathology | Pneumonia - etiology | Protein Synthesis Inhibitors - toxicity | Purines - metabolism | Poisoning - drug therapy | Lethal Dose 50 | Poisoning - pathology | Protein Synthesis Inhibitors - metabolism | Ricin - administration & dosage | Administration, Intranasal | Ricin - toxicity | Abrin - metabolism | Animals | Ricin - metabolism | Lung - drug effects | Ribosomes - drug effects | Mice | Respiratory Mucosa - metabolism | DNA, Complementary - metabolism | Lectins | Enzymes | Protein biosynthesis | Analysis | Index Medicus | Lungs | Catalysts | Catalytic activity | Exposure | Toxins | Intoxication | Damage
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 06/2012, Volume 419, Issue 3-4, pp. 125 - 138
The sarcin–ricin loop (SRL) is one of the longest conserved sequences in the 23S ribosomal RNA. The SRL has been accepted as crucial for the activity of the... 
ribosome | peptide bond | tRNA selection | translocation | GTP hydrolysis | ALPHA-SARCIN | AMINOACYL-TRANSFER-RNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | FACTOR TU | AFFINITY PURIFICATION | CODON-RECOGNITION | CONFORMATIONAL-CHANGES | EUKARYOTIC RIBOSOMES | EF-G | PEPTIDYL-TRANSFER-RNA | Protein Biosynthesis | Peptide Chain Elongation, Translational | Ribosomes - metabolism | Guanosine Triphosphate - metabolism | RNA, Messenger - metabolism | RNA, Ribosomal - genetics | RNA, Ribosomal, 23S - genetics | Peptide Elongation Factor Tu - genetics | Conserved Sequence | Peptide Elongation Factor G - chemistry | RNA, Bacterial - genetics | Nucleic Acid Conformation | Binding Sites | RNA, Bacterial - metabolism | Endoribonucleases - metabolism | Protein Structure, Secondary | RNA, Transfer - metabolism | RNA, Ribosomal - metabolism | Peptide Elongation Factor G - genetics | Peptide Elongation Factor Tu - chemistry | Peptide Elongation Factor Tu - metabolism | RNA, Ribosomal, 23S - chemistry | Ribosomes - genetics | Ricin - metabolism | Escherichia coli - genetics | RNA, Bacterial - chemistry | Peptide Elongation Factor G - metabolism | Protein Binding | Mutation | RNA, Ribosomal, 23S - metabolism | Fungal Proteins - metabolism | Hydrolysis | Peptides | RNA | Ribosomal RNA | Analysis | Lectins | Protein biosynthesis | Transfer RNA
Journal Article
Cellular Microbiology, ISSN 1462-5814, 07/2008, Volume 10, Issue 7, pp. 1468 - 1477
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 04/2015, Volume 112, Issue 16, pp. 5165 - 5170
Journal Article
Applied Microbiology and Biotechnology, ISSN 0175-7598, 11/2018, Volume 102, Issue 22, pp. 9585 - 9594
The specific targeting of immunotoxins enables their wide application in cancer therapy. The A-chain of the ricin protein (RTA) is an N-glycosidase that... 
Life Sciences | Biotechnology | Ricin A | Localization peptide | Microbiology | Recombinant immunotoxin | Microbial Genetics and Genomics | Cancer cell | HER2 | Specific targeting | ABRIN | ESCHERICHIA-COLI | TOXIC LECTINS | INCREASES | RICIN-A-CHAIN | GLUCOSE-REGULATED PROTEIN | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PHASE-I | EXPRESSION | CYTOTOXICITY | Lung Neoplasms - drug therapy | Receptor, ErbB-2 - genetics | Recombinant Fusion Proteins - pharmacology | Humans | Lung Neoplasms - metabolism | Receptor, ErbB-2 - metabolism | Endoplasmic Reticulum - metabolism | Immunotoxins - pharmacology | Recombinant Fusion Proteins - metabolism | Ovarian Neoplasms - genetics | Single-Chain Antibodies - metabolism | Single-Chain Antibodies - genetics | HEK293 Cells | Immunotoxins - metabolism | Female | Ovarian Neoplasms - metabolism | Receptor, ErbB-2 - antagonists & inhibitors | Ovarian Neoplasms - drug therapy | Lung Neoplasms - genetics | Endoplasmic Reticulum - genetics | Single-Chain Antibodies - pharmacology | Oligopeptides - genetics | Oligopeptides - metabolism | Amino Acid Motifs | Protein Transport | Ricin - pharmacology | Immunotoxins - genetics | Protein Sorting Signals - genetics | Ricin - metabolism | Cell Line, Tumor | Recombinant Fusion Proteins - genetics | Ricin - genetics | Single-Chain Antibodies - chemistry | Prevention | Antibody-toxin conjugates | Endoplasmic reticulum | Health aspects | Production processes | Cancer cells | rRNA 28S | Ovarian carcinoma | Toxicity | Ricin | Lung cancer | Adenine | Chains | ErbB-2 protein | Ovarian cancer | Anticancer properties | Proteins | Immunotoxins | Cell death | N-glycosidase | Immunofluorescence | Cytoplasm | Cancer | Recombinant | Index Medicus
Journal Article
Journal Article
Molecular Biology of the Cell, ISSN 1059-1524, 08/2010, Volume 21, Issue 15, pp. 2543 - 2554
We report that a toxic polypeptide retaining the potential to refold upon dislocation from the endoplasmic reticulum (ER) to the cytosol (ricin A chain; RTA)... 
Journal Article