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Science (American Association for the Advancement of Science), ISSN 1095-9203, 2010, Volume 329, Issue 5998, pp. 1492 - 1499
Journal Article
Science, ISSN 0036-8075, 07/2011, Volume 333, Issue 6038, pp. 37 - 37
Voorhees et al. (Reports, 5 November 2010, p. 835) determined the structure of elongation factor Tu (EF-Tu) and aminoacyl-transfer RNA bound to the ribosome... 
MULTIDISCIPLINARY SCIENCES | Protons | Guanosine Triphosphate - analogs & derivatives | Phosphates - chemistry | Models, Molecular | Ribosomes - metabolism | Guanosine Triphosphate - metabolism | Peptide Elongation Factor Tu - chemistry | Histidine - metabolism | GTP Phosphohydrolases - chemistry | Hydrolysis | Peptide Elongation Factor Tu - metabolism | RNA, Ribosomal, 23S - chemistry | Phosphates - metabolism | GTP Phosphohydrolases - metabolism | Hydrogen Bonding | RNA, Bacterial - chemistry | RNA, Transfer, Amino Acyl - metabolism | Water - chemistry | Hydrophobic and Hydrophilic Interactions | Guanosine Triphosphate - chemistry | Histidine - chemistry | RNA, Ribosomal, 23S - metabolism | RNA, Bacterial - metabolism | Phosphates | Ribonucleic acid--RNA | Guanosine Triphosphate: chemistry | RNA | Ribosomal | 23S: chemistry | Phosphates: metabolism | GTP Phosphohydrolases: chemistry | Bacterial: chemistry | Biologi | Natural Sciences | GTP Phosphohydrolases: metabolism | Biological Sciences | Water: chemistry | Phosphates: chemistry | Histidine: metabolism | Guanosine Triphosphate: metabolism | Guanosine Triphosphate: analogs & derivatives | 23S: metabolism | Ribosomes: metabolism | Naturvetenskap | Peptide Elongation Factor Tu: chemistry | Histidine: chemistry | Amino Acyl: metabolism | Bacterial: metabolism | Transfer | Peptide Elongation Factor Tu: metabolism
Journal Article
Journal Article
The Plant cell, ISSN 1532-298X, 2017, Volume 29, Issue 3, pp. 543 - 559
Stomata play an important role in preinvasive defense responses by limiting pathogen entry into leaves. Although the stress hormones salicylic acid (SA) and... 
RESEARCH ARTICLES | BIOCHEMISTRY & MOLECULAR BIOLOGY | PSEUDOMONAS-SYRINGAE | TRANSCRIPTIONAL ANALYSIS | PLANT INNATE IMMUNITY | NADPH OXIDASE RBOHD | GUARD-CELL | PLANT SCIENCES | CELL BIOLOGY | SALICYLIC-ACID | APOPLASTIC OXIDATIVE BURST | YEAST ELICITOR | PV. TOMATO DC3000 | ABSCISIC-ACID | Arabidopsis Proteins - genetics | Histidine Kinase - metabolism | Reactive Oxygen Species - metabolism | Pathogen-Associated Molecular Pattern Molecules - metabolism | Salicylic Acid - metabolism | NADPH Oxidases - metabolism | Arabidopsis - immunology | Plant Stomata - metabolism | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Plant Stomata - immunology | Pseudomonas syringae - pathogenicity | Arabidopsis - metabolism | Arabidopsis Proteins - metabolism | DNA-Binding Proteins - metabolism | Transcription Factors - metabolism | Arabidopsis - microbiology | Histidine Kinase - genetics | NADPH Oxidases - genetics | Peroxidases - metabolism | Abscisic Acid - metabolism | Cytokinins - metabolism | Peroxidases - genetics | Plant Stomata - microbiology | Arabidopsis thaliana | Cytokinins | Reactive oxygen species | Plant defenses | Analysis | Physiological aspects | Homeostasis | Transcription | Gene regulation | Plant resistance | Hormones | Immunity | NAD(P)H oxidase | Leaves | Signal transduction | Histidine | Abscisic acid | Bacteria | Genetics | Peroxidase | Tomatoes | Pathogens | Salicylic acid | Oxygen | Stomata | Guard cells | Pharmacology | Gene expression | Signaling | Zeatin | Acids
Journal Article
Neuroscience, ISSN 0306-4522, 2005, Volume 130, Issue 1, pp. 165 - 183
The circadian clock housed in the suprachiasmatic nucleus (SCN) controls various circadian rhythms including daily sleep–wake cycles. Using dual tract-tracing,... 
orexin/hypocretin | dual tract-tracing | immunohistochemistry | aminergic | cholinergic | EFFERENT PROJECTIONS | PHASEOLUS-VULGARIS-LEUKOAGGLUTININ | DORSOMEDIAL HYPOTHALAMIC NUCLEUS | FOS EXPRESSION | SUBPARAVENTRICULAR ZONE | NEUROSCIENCES | LOCUS COERULEUS | PARAVENTRICULAR NUCLEUS | VENTROLATERAL PREOPTIC NUCLEUS | ANTEROGRADE TRANSPORT | RAPHE NUCLEI | Tyrosine 3-Monooxygenase - metabolism | Rats, Wistar | Male | Intracellular Signaling Peptides and Proteins - metabolism | Preoptic Area - metabolism | Choline O-Acetyltransferase - metabolism | Neuropeptide Y - metabolism | Biotin - metabolism | Suprachiasmatic Nucleus - metabolism | Functional Laterality - physiology | Neurons - metabolism | Paraventricular Hypothalamic Nucleus - anatomy & histology | Dextrans - metabolism | Orexins | Cholera Toxin - metabolism | Histidine Decarboxylase - metabolism | Rats | Dorsomedial Hypothalamic Nucleus - anatomy & histology | Neuropeptides - metabolism | Circadian Rhythm - physiology | Dorsomedial Hypothalamic Nucleus - metabolism | Suprachiasmatic Nucleus - anatomy & histology | Immunohistochemistry - methods | Arousal - physiology | Neural Pathways - anatomy & histology | Animals | Cell Count - methods | Serotonin - metabolism | Paraventricular Hypothalamic Nucleus - metabolism | Neural Pathways - metabolism | Preoptic Area - anatomy & histology | Biotin - analogs & derivatives
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2009, Volume 326, Issue 5957, pp. 1231 - 1235
Loss-of-function genetic screens in model organisms have elucidated numerous biological processes, but the diploid genome of mammalian cells has precluded... 
Haploidy | B lymphocytes | Genes | Cell lines | Medical genetics | Cell cycle | HeLa cells | Toxins | Genetic screening | Human genetics | Research Article | TARGET | PROTEIN | ADP-RIBOSYLATING TOXINS | DIPHTHAMIDE | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | INFLUENZA | RECEPTOR | IDENTIFICATION | SACCHAROMYCES-CEREVISIAE | DIPHTHERIA-TOXIN | ADP Ribose Transferases - toxicity | Histidine - analogs & derivatives | Genetic Testing | Humans | N-Acylneuraminate Cytidylyltransferase - genetics | Adenosine Diphosphate Ribose - metabolism | Bacterial Toxins - toxicity | Molecular Sequence Data | Diphtheria Toxin - toxicity | N-Acylneuraminate Cytidylyltransferase - metabolism | Exotoxins - metabolism | Antigens, Bacterial - toxicity | Monosaccharide Transport Proteins - metabolism | ADP Ribose Transferases - metabolism | Monosaccharide Transport Proteins - genetics | Virulence Factors - toxicity | Amino Acid Sequence | Histidine - biosynthesis | Influenza A Virus, H1N1 Subtype - pathogenicity | Biosynthetic Pathways | Diphtheria Toxin - metabolism | Host-Pathogen Interactions | Proteins - genetics | Bacterial Toxins - metabolism | Proteins - metabolism | Cell Line, Tumor | Exotoxins - toxicity | Virulence Factors - metabolism | Mutagenesis, Insertional | Proteins - chemistry | Antigens, Bacterial - metabolism | Peptide Elongation Factor 2 - metabolism | Research | Mutagenesis | Methods | Testing | Models | Cellular biology | Medical screening | Genomics | Influenza | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2017, Volume 292, Issue 34, pp. 14250 - 14257
The histidine-phosphorylatable phosphocarrier protein (HPr) is an essential component of the sugar-transporting phosphotransferase system (PTS) in many... 
COMPLEX | DOMAIN | PATHOGEN | glucosamine 6-phosphate deaminase | GLYCOGEN-PHOSPHORYLASE | adenylate kinase (ADK) | BIOCHEMISTRY & MOLECULAR BIOLOGY | glycolysis | phosphofructokinase | isomerase | adenylate kinase | Histidine phosphocarrier protein | GLUCOSAMINE-6-PHOSPHATE DEAMINASE | SUBSTRATE-BINDING | PYRUVATE-KINASE | REPRESSION | pyruvate kinase | protein-protein interaction | PHOSPHOENOLPYRUVATE | ALLOSTERIC ACTIVATION | Phosphorylation | Allosteric Regulation | Bacterial Proteins - chemistry | Pyruvate Kinase - chemistry | Isoenzymes - chemistry | Histidine - metabolism | Adenylate Kinase - chemistry | Recombinant Fusion Proteins - metabolism | Isoenzymes - metabolism | Adenylate Kinase - metabolism | Escherichia coli - metabolism | Escherichia coli Proteins - agonists | Protein Interaction Domains and Motifs | Binding Sites | Aldose-Ketose Isomerases - metabolism | Phosphoenolpyruvate Sugar Phosphotransferase System - chemistry | Phosphoenolpyruvate Sugar Phosphotransferase System - genetics | Recombinant Proteins - metabolism | Aldose-Ketose Isomerases - chemistry | Phosphofructokinase-2 - chemistry | Escherichia coli - enzymology | Pyruvate Kinase - metabolism | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | Recombinant Fusion Proteins - chemistry | Phosphofructokinase-2 - metabolism | Energy Metabolism | Phosphofructokinase-2 - genetics | Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism | Proteomics | Escherichia coli Proteins - genetics | Glycolysis | Bacterial Proteins - metabolism | Protein Conformation | Protein Processing, Post-Translational | Aldose-Ketose Isomerases - genetics | Enzyme Activation | Escherichia coli Proteins - chemistry | Adenylate Kinase - genetics | Pyruvate Kinase - genetics | Metabolism
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 45, pp. 18500 - 18517
Membrane tethering is a fundamental process essential for the compartmental specificity of intracellular membrane trafficking in eukaryotic cells. Rab-family... 
LOCALIZATION | SNARE PROTEINS | FUSION | SPECIFICITY | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | myosin | membrane tethering | liposome | MOLECULES | Rab | TRANSPORT | CARGO | Myo5 | SUPERFAMILY | membrane reconstitution | small GTPase | VESICLE | membrane trafficking | Myosin Heavy Chains - chemistry | Myosin Type V - chemistry | Succinates - chemistry | Intracellular Membranes - enzymology | Humans | Myosin Heavy Chains - genetics | rab GTP-Binding Proteins - agonists | rab GTP-Binding Proteins - genetics | Guanosine Triphosphate - metabolism | Isoenzymes - chemistry | Histidine - metabolism | Myosin Heavy Chains - metabolism | Protein Prenylation | Recombinant Fusion Proteins - metabolism | Endosomes - metabolism | Oleic Acids - metabolism | Isoenzymes - metabolism | Succinates - metabolism | Lysine - metabolism | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Acylation | rab GTP-Binding Proteins - metabolism | Lysine - analogs & derivatives | Peptide Fragments - metabolism | Myosin Type V - metabolism | Isoenzymes - genetics | Histidine - genetics | Recombinant Fusion Proteins - chemistry | Intracellular Membranes - chemistry | Protein Interaction Mapping | Peptide Fragments - chemistry | Myosin Type V - genetics | rab GTP-Binding Proteins - chemistry | Endosomes - enzymology | Protein Processing, Post-Translational | Kinetics | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Liposomes | Histidine - chemistry | Lysine - chemistry | Oleic Acids - chemistry | Intracellular Membranes - metabolism | Membrane Biology
Journal Article