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Journal of the American Chemical Society, ISSN 0002-7863, 01/2003, Volume 125, Issue 1, pp. 173 - 186
Journal Article
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
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
Molecules, ISSN 1420-3049, 05/2017, Volume 22, Issue 5, p. 754
Amarogentin, a secoiridoid glycoside that is mainly extracted from Swertia and Gentiana roots, has been suggested to exhibit many biological effects, including... 
Mitogen-activated protein kinase | Liver fibrosis | α-smoothmuscle actin | Carbon tetrachloride | Amarogentin | amarogentin | OXIDATIVE STRESS | ACTIVATION | RATS | CHEMISTRY, ORGANIC | carbon tetrachloride | MODEL | MESSENGER-RNA LEVELS | mitogen-activated protein kinase | liver fibrosis | HEPATIC STELLATE CELLS | INHIBITION | COLCHICINE | alpha-smoothmuscle actin | SIGNAL-REGULATED KINASE | MODULATION | Albumins - chemistry | Plant Extracts - chemistry | Antioxidants - chemistry | Oxidative Stress | Carbon Tetrachloride | Humans | Malondialdehyde - chemistry | Liver Cirrhosis - chemically induced | Dose-Response Relationship, Drug | Tissue Distribution | Iridoids - chemistry | Actins - chemistry | Phytotherapy | Glycosides - chemistry | Hydroxyproline - chemistry | Cell Line | Liver Cirrhosis - drug therapy | Down-Regulation | Gentiana - chemistry | Mice, Inbred C57BL | Swertia - chemistry | Nucleotides, Cyclic - chemistry | Animals | Iridoids - pharmacology | Plant Roots - chemistry | Iridoids - therapeutic use | Mice | Transcription factors | Liver | Roots | Hydroxyproline | Guanosine | Smooth muscle | Superoxide dismutase | Biochemistry | Kinases | Assaying | Signal transduction | Biological effects | Actin | Cyclic GMP | Peroxidase | Glutathione | Glutathione peroxidase | Retarding | Alanine | Diabetes mellitus | c-Jun protein | Albumin | MAP kinase | Olive oil | Carbon | Malondialdehyde | Signaling | Protein kinase | Fibrosis | Alanine transaminase | Aspartate aminotransferase | Fats and oils | Colchicine | Tumors
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 09/2004, Volume 126, Issue 37, pp. 11484 - 11499
We have earlier reported the synthesis and antisense properties of the conformationally constrained oxetane-C and -T containing oligonucleotides, which have... 
RNA HYBRID DUPLEX | STEREOCHEMICAL ASSIGNMENTS | BIOLOGICAL-ACTIVITY | CARBOCYCLIC THYMIDINE | NUCLEIC-ACID ANALOGS | MODIFIED ANTISENSE OLIGONUCLEOTIDES | BICYCLIC NUCLEOSIDES | CONFORMATIONALLY LOCKED NUCLEOSIDES | SUGAR RING | CHEMISTRY, MULTIDISCIPLINARY | H CLEAVAGE | Oligonucleotides - chemistry | Humans | Molecular Sequence Data | Cytidine - analogs & derivatives | Nucleic Acid Heteroduplexes - metabolism | Ethers, Cyclic - metabolism | Thermodynamics | Ethers, Cyclic - chemistry | Deoxyribonuclease I - chemistry | Guanosine - chemistry | Base Sequence | Adenosine - chemistry | Nucleic Acid Conformation | Circular Dichroism | Thymidine - chemistry | RNA - metabolism | Guanosine - analogs & derivatives | Cytidine - chemistry | Models, Molecular | RNA - chemistry | Oligonucleotides - chemical synthesis | Nucleic Acid Heteroduplexes - chemistry | Deoxyribonuclease I - metabolism | Oligonucleotides - metabolism | Thymidine - analogs & derivatives | Adenosine - analogs & derivatives | Ribonuclease H - chemistry | Kinetics | Oligonucleotides - blood | Ribonuclease H - metabolism | Adenosine | DNA microarrays | Research | Chemical properties | Guanosine | Models; Molecular | Deoxyribonuclease I/chemistry/metabolism | Oligonucleotides/blood/chemical synthesis/chemistry/metabolism | RNA/chemistry/metabolism | Cytidine/analogs & derivatives/chemistry | Guanosine/analogs & derivatives/chemistry | Thymidine/analogs & derivatives/chemistry | Adenosine/analogs & derivatives/chemistry | Ethers; Cyclic/chemistry/metabolism | Nucleic Acid Heteroduplexes/chemistry/metabolism | Research Support; Non-U.S. Gov't | Ribonuclease H; Calf Thymus/chemistry/metabolism
Journal Article
Nature Communications, ISSN 2041-1723, 02/2015, Volume 6, Issue 1, pp. 6148 - 6148
Formate dehydrogenases (FDHs) are of interest as they are natural catalysts that sequester atmospheric CO2, generating reduced carbon compounds with possible... 
MOLYBDOPTERIN GUANINE DINUCLEOTIDE | XANTHINE-OXIDASE | FORMATE | MECHANISM | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | REDUCTASE | THALIANA PROVIDES INSIGHT | CARBON-DIOXIDE | DEHYDROGENASE | Molybdenum - chemistry | Molecular Chaperones - metabolism | Formates - chemistry | Hydrogenase - genetics | Molybdenum - metabolism | Protein Multimerization | Multienzyme Complexes - metabolism | Crystallography, X-Ray | Hydrogenase - chemistry | Molecular Chaperones - chemistry | Coenzymes - metabolism | Hydrogenase - metabolism | Carbon Cycle | Cloning, Molecular | Escherichia coli - metabolism | Guanosine Diphosphate - chemistry | Guanosine Diphosphate - metabolism | Coenzymes - chemistry | Binding Sites | Formates - metabolism | Sulfur - chemistry | Protein Structure, Tertiary | Sulfur - metabolism | Gene Expression | Biocatalysis | Carbon Dioxide - metabolism | Oxidation-Reduction | Protein Structure, Secondary | Molecular Chaperones - genetics | Models, Molecular | Formate Dehydrogenases - metabolism | Multienzyme Complexes - genetics | Escherichia coli - chemistry | Carbon-Sulfur Lyases - metabolism | Formate Dehydrogenases - genetics | Plasmids - metabolism | Multienzyme Complexes - chemistry | Formate Dehydrogenases - chemistry | Escherichia coli - genetics | Plasmids - chemistry | Protein Binding | Index Medicus | Life Sciences | Genetics | Cellular Biology | Biochemistry, Molecular Biology | Environmental Sciences
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2014, Volume 111, Issue 24, pp. 8895 - 8900
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2015, Volume 112, Issue 36, pp. 11247 - 11251
Computational chemistry predicts that atomic motions on the femtosecond timescale are coupled to transition-state formation (barrier-crossing) in human purine... 
Heavy enzymes | Transition state coupling | Born-Oppenheimer enzymes | Femtosecond dynamics | Pre-steady-state chemistry | femtosecond dynamics | SITE | pre-steady-state chemistry | MULTIDISCIPLINARY SCIENCES | transition state coupling | TRANSITION-STATE | ENZYMATIC-REACTION | MOTIONS | PROMOTING VIBRATIONS | heavy enzymes | PROTEIN DYNAMICS | PNP | DIHYDROFOLATE-REDUCTASE | CATALYTIC MECHANISM | Models, Chemical | Humans | Amino Acids - chemistry | Molecular Sequence Data | Chromatography, High Pressure Liquid | Histidine - metabolism | Amino Acids - genetics | Purine-Nucleoside Phosphorylase - genetics | Amino Acids - metabolism | Isotopes - chemistry | Tandem Mass Spectrometry | Ribosemonophosphates - chemistry | Guanosine - chemistry | Isotope Labeling | Purine-Nucleoside Phosphorylase - metabolism | Carbon Isotopes - chemistry | Amino Acid Sequence | Motion | Catalytic Domain | Biocatalysis | Deuterium - chemistry | Histidine - genetics | Models, Molecular | Binding Sites - genetics | Guanosine - metabolism | Nitrogen Isotopes - chemistry | Purine-Nucleoside Phosphorylase - chemistry | Kinetics | Histidine - chemistry | Ribosemonophosphates - metabolism | Physiological aspects | Amino acids | Purine nucleotides | Research | Phosphorylase | Atoms & subatomic particles | Enzymes | Chemistry | Isotopes | Biological Sciences | Born–Oppenheimer enzymes | pre–steady-state chemistry
Journal Article