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Science, ISSN 0036-8075, 5/2001, Volume 292, Issue 5518, pp. 897 - 902
Crystal structures of the 30S ribosomal subunit in complex with messenger RNA and cognate transfer RNA in the A site, both in the presence and absence of the... 
Messenger RNA | Hydrogen bonds | RNA | Antibiotics | Protein synthesis | Ribosomes | Crystals | Research Articles | Codons | Anticodon | Transfer RNA | P-SITE | ANGSTROM RESOLUTION | ELONGATION-FACTOR TU | ESCHERICHIA-COLI RIBOSOME | AMINOACYL-TRANSFER-RNA | PHENYLALANINE TRANSFER-RNA | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | A-SITE | 70S RIBOSOME | DNA-REPLICATION | Codon - metabolism | Anticodon - metabolism | Protein Biosynthesis | Peptide Chain Elongation, Translational | RNA, Transfer, Phe - chemistry | Anticodon - chemistry | RNA, Transfer, Amino Acid-Specific - metabolism | Ribosomes - metabolism | Thermus thermophilus - metabolism | Crystallography, X-Ray | Thermus thermophilus - ultrastructure | Guanosine Triphosphate - metabolism | RNA, Messenger - metabolism | Paromomycin - pharmacology | Thermodynamics | Nucleic Acid Conformation | RNA, Transfer - chemistry | Binding Sites | RNA, Bacterial - metabolism | RNA, Ribosomal, 16S - metabolism | RNA, Transfer, Phe - metabolism | Thermus thermophilus - chemistry | RNA, Transfer - metabolism | Ribosomes - chemistry | Models, Molecular | Anti-Bacterial Agents - metabolism | Peptide Elongation Factor Tu - metabolism | RNA, Transfer, Amino Acid-Specific - chemistry | RNA, Ribosomal, 16S - chemistry | Ribosomes - ultrastructure | Codon - chemistry | Base Pairing | Hydrogen Bonding | RNA, Bacterial - chemistry | RNA, Messenger - chemistry | Anti-Bacterial Agents - pharmacology | Paromomycin - metabolism | Protein research | Usage | Polypeptides | Amino acids | Research | Molecular biology | Statistics | Ribonucleic acid--RNA | Ribonucleic acid
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 3/2004, Volume 164, Issue 5, pp. 769 - 779
All ligands of the epidermal growth factor receptor (EGFR), which has important roles in development and disease, are released from the membrane by proteases.... 
EGF receptor | Growth factor signaling | EGF receptor ligands | ADAMs | Ectodomain shedding | CELLS | ectodomain shedding | HB-EGF | TACE | PROTEIN-COUPLED RECEPTORS | ALPHA-CONVERTING-ENZYME | growth factor signaling | MICE LACKING | FAMILY | CELL BIOLOGY | EPIDERMAL-GROWTH-FACTOR | TGF-ALPHA | METALLOPROTEASE-DISINTEGRIN | ADAM17 Protein | Metalloendopeptidases - genetics | Phenylalanine - analogs & derivatives | Glycoproteins - metabolism | Metalloendopeptidases - metabolism | Thiophenes - metabolism | Epiregulin | Amphiregulin | Disintegrins - genetics | ADAM12 Protein | Intercellular Signaling Peptides and Proteins - metabolism | Receptor, Epidermal Growth Factor - metabolism | EGF Family of Proteins | Embryo, Mammalian - anatomy & histology | Aspartic Acid Endopeptidases | Amyloid Precursor Protein Secretases | Muscle Proteins - metabolism | Membrane Proteins - metabolism | Transforming Growth Factor alpha - metabolism | Fibroblasts - metabolism | Tetradecanoylphorbol Acetate - metabolism | Protein Structure, Tertiary | Endopeptidases - metabolism | Phenylalanine - metabolism | Disintegrins - metabolism | Membrane Proteins - genetics | Cells, Cultured | Epidermal Growth Factor - metabolism | Genotype | Protease Inhibitors - metabolism | ADAM Proteins | Mice, Knockout | Muscle Proteins - genetics | Heparin-binding EGF-like Growth Factor | Animals | Endopeptidases - genetics | Betacellulin | Ligands | Fibroblasts - cytology | Mice | Cytology | Research | EGF receptor; EGF receptor ligands; ADAMs; ectodomain shedding; growth factor signaling
Journal Article
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2011, Volume 6, Issue 10, p. e26214
Ecological performance is all about timing and the endogenous clock that allows the entrainment of rhythms and anticipation of fitness-determining events is... 
CIRCADIAN CLOCK | MOLECULAR-INTERACTIONS | ARABIDOPSIS ROOTS | INSECT HERBIVORES | BIOLOGY | GENE-EXPRESSION | MANDUCA-SEXTA LEPIDOPTERA | TYROSINE DECARBOXYLASE | JASMONIC ACID | AMINO-ACID CONTENT | DITERPENE GLYCOSIDES | Disaccharides - metabolism | Plant Roots - genetics | Manduca - metabolism | RNA, Messenger - metabolism | Plant Roots - drug effects | Plant Roots - physiology | Plant Leaves - drug effects | Tobacco - physiology | Phenylalanine - metabolism | Plant Roots - metabolism | Tobacco - metabolism | Larva - metabolism | RNA, Messenger - genetics | Circadian Rhythm - genetics | Tobacco - drug effects | Herbivory | Fatty Acids, Unsaturated - metabolism | Organ Specificity | Polyamines - metabolism | Oxylipins - metabolism | Tyrosine - metabolism | Animals | Plant Leaves - genetics | Plant Leaves - metabolism | Genes, Plant - genetics | Glycosides - metabolism | Tobacco - genetics | Cyclopentanes - metabolism | Mechanical Phenomena | Plant Leaves - physiology | Metabolites | Animal behavior | Analysis | Physiological aspects | Liquid chromatography | Mass spectrometry | Health aspects | Larvae | Roots | Tissues | Accumulation | Leaves | Entrainment | Drought | Jasmonic acid | Tyrosine | Tyramine | Stresses | Plants (botany) | Computer simulation | Phenylalanine | Mass spectroscopy | Ions | Rhythms | Circadian rhythm | Metabolism | Diurnal | Tobacco | Acids | Insects | Herbivores | Fitness
Journal Article
Journal Article
Annual Review of Biochemistry, ISSN 0066-4154, 6/2016, Volume 85, pp. 485 - 514
Radical S -adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Of... 
S | tRNA modifications | radicals | Elongator | iron-sulfur cluster | adenosylmethionine | viperin | lipoic acid | molybdenum cofactor | Lipoic acid | Molybdenum cofactor | Viperin | TRNA modifications | Iron-sulfur cluster | S-adenosylmethionine | Radicals | IRON-SULFUR PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOCHONDRIAL TRANSFER-RNAS | ANTIVIRAL PROTEIN VIPERIN | AMYOTROPHIC-LATERAL-SCLEROSIS | ADENOSYL-L-METHIONINE | LIPOIC ACID BIOSYNTHESIS | HEPATITIS-C VIRUS | PHENYLALANINE TRANSFER-RNA | MOLYBDENUM COFACTOR DEFICIENCY | GENOME-WIDE ASSOCIATION | Diabetes Mellitus, Type 2 - genetics | Humans | Histone Acetyltransferases - genetics | Iron-Sulfur Proteins - genetics | Intracellular Signaling Peptides and Proteins - metabolism | Thioctic Acid - metabolism | Heart Defects, Congenital - genetics | tRNA Methyltransferases - genetics | Heart Defects, Congenital - enzymology | Histone Acetyltransferases - metabolism | Nuclear Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | tRNA Methyltransferases - metabolism | Gene Expression | Metal Metabolism, Inborn Errors - genetics | Neurodegenerative Diseases - pathology | Oxidoreductases - metabolism | Oxidoreductases - genetics | Diabetes Mellitus, Type 2 - enzymology | Heart Defects, Congenital - pathology | Metal Metabolism, Inborn Errors - pathology | Neurodegenerative Diseases - genetics | Nuclear Proteins - metabolism | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Proteins - genetics | Proteins - metabolism | Metal Metabolism, Inborn Errors - enzymology | Iron-Sulfur Proteins - metabolism | Diabetes Mellitus, Type 2 - pathology | Mutation | S-Adenosylmethionine - metabolism | Neurodegenerative Diseases - enzymology | Health aspects | Methionine
Journal Article