2013, ISBN 3863353153, 79 pages
Book
Biochemistry, ISSN 0006-2960, 09/2016, Volume 55, Issue 36, pp. 5010 - 5020
The dependence of the conformation of the S-adenosylmethionine (SAM) II riboswitch on the concentration of added Mg2+ ions and SAM, individually and in...
NMR | CIRCULAR-DICHROISM | RNA | PREORGANIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CONFINEMENT | BIOCHEMICAL REACTIONS | ABSENCE | LIGAND | PROTEINS | BINDING | Usage | Analysis | Spectrum analysis | Conformational analysis | Research | Diffusion | Circular dichroism
NMR | CIRCULAR-DICHROISM | RNA | PREORGANIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CONFINEMENT | BIOCHEMICAL REACTIONS | ABSENCE | LIGAND | PROTEINS | BINDING | Usage | Analysis | Spectrum analysis | Conformational analysis | Research | Diffusion | Circular dichroism
Journal Article
Callaloo, ISSN 0161-2492, 2017, Volume 40, Issue 5, pp. 59 - 68
Mapping Sam Gilliam’s astonishingly resilient artistic career along a timeline, a linear trajectory of peaks and valleys marking his fecund and relatively...
Gilliam, Sam | Biography | African American artists | 1933 | 20th century | Painters | Color | Careers | African Americans | Politics | Painting
Gilliam, Sam | Biography | African American artists | 1933 | 20th century | Painters | Color | Careers | African Americans | Politics | Painting
Journal Article
36 p. ill.
Book
1976, xix, 178 p. ill., map.
Book
Nature, ISSN 0028-0836, 2013, Volume 498, Issue 7452, pp. 123 - 126
The identification of novel metabolites and the characterization of their biological functions are major challenges in biology. X-ray crystallography can...
METHYLTRANSFERASE | ENZYME | DATABASE | DNA | MULTIDISCIPLINARY SCIENCES | URIDINE-5-OXYACETIC ACID | CHORISMIC ACID | TIME | MODEL | PREPHENATE | REVEALS | Molecular Weight | Methyltransferases - metabolism | Protein Multimerization | Uridine - analogs & derivatives | Methyltransferases - genetics | Crystallography, X-Ray | S-Adenosylmethionine - chemistry | Methyltransferases - deficiency | One-Carbon Group Transferases - metabolism | RNA, Bacterial - genetics | RNA, Transfer - genetics | Cyclohexanecarboxylic Acids - metabolism | RNA, Transfer - chemistry | RNA, Bacterial - metabolism | Uridine - chemistry | Catalytic Domain | Biocatalysis | Escherichia coli - enzymology | Protein Structure, Secondary | RNA, Transfer - metabolism | Models, Molecular | Escherichia coli Proteins - metabolism | Biosynthetic Pathways | S-Adenosylmethionine - biosynthesis | One-Carbon Group Transferases - chemistry | Cyclohexenes - metabolism | S-Adenosylmethionine - analogs & derivatives | RNA, Bacterial - chemistry | Escherichia coli Proteins - genetics | Ligands | Uridine - metabolism | Escherichia coli Proteins - chemistry | S-Adenosylmethionine - metabolism | Physiological aspects | Research | Metabolites | Transferases | Transfer RNA | Enzymes | Nuclear magnetic resonance--NMR | E coli | Crystallization | Gram-negative bacteria
METHYLTRANSFERASE | ENZYME | DATABASE | DNA | MULTIDISCIPLINARY SCIENCES | URIDINE-5-OXYACETIC ACID | CHORISMIC ACID | TIME | MODEL | PREPHENATE | REVEALS | Molecular Weight | Methyltransferases - metabolism | Protein Multimerization | Uridine - analogs & derivatives | Methyltransferases - genetics | Crystallography, X-Ray | S-Adenosylmethionine - chemistry | Methyltransferases - deficiency | One-Carbon Group Transferases - metabolism | RNA, Bacterial - genetics | RNA, Transfer - genetics | Cyclohexanecarboxylic Acids - metabolism | RNA, Transfer - chemistry | RNA, Bacterial - metabolism | Uridine - chemistry | Catalytic Domain | Biocatalysis | Escherichia coli - enzymology | Protein Structure, Secondary | RNA, Transfer - metabolism | Models, Molecular | Escherichia coli Proteins - metabolism | Biosynthetic Pathways | S-Adenosylmethionine - biosynthesis | One-Carbon Group Transferases - chemistry | Cyclohexenes - metabolism | S-Adenosylmethionine - analogs & derivatives | RNA, Bacterial - chemistry | Escherichia coli Proteins - genetics | Ligands | Uridine - metabolism | Escherichia coli Proteins - chemistry | S-Adenosylmethionine - metabolism | Physiological aspects | Research | Metabolites | Transferases | Transfer RNA | Enzymes | Nuclear magnetic resonance--NMR | E coli | Crystallization | Gram-negative bacteria
Journal Article
2018, Methods in Enzymology, Volume 606, 71
The radical SAM superfamily contains over 100,000 homologous enzymes that catalyze a remarkably broad range of reactions required for life, including...
BIOTIN SYNTHASE | S-ADENOSYLMETHIONINE | LIPOYL SYNTHASE | ENZYME | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | BIOCHEMICAL RESEARCH METHODS | SPORE PHOTOPRODUCT LYASE | LARGE-SCALE | PROTEIN FUNCTION | IRON-SULFUR CLUSTERS
BIOTIN SYNTHASE | S-ADENOSYLMETHIONINE | LIPOYL SYNTHASE | ENZYME | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | BIOCHEMICAL RESEARCH METHODS | SPORE PHOTOPRODUCT LYASE | LARGE-SCALE | PROTEIN FUNCTION | IRON-SULFUR CLUSTERS
Book Chapter
Methods in Enzymology, ISSN 0076-6879, 01/2018, Volume 606, pp. 1 - 71
The radical SAM superfamily contains over 100,000 homologous enzymes that catalyze a remarkably broad range of reactions required for life, including...
Sequence similarity networks | Phylogenetic representation | Radical SAM superfamily census | Subgroups and families in the radical SAM superfamily | Multiple domain structures of radical SAM superfamily enzymes | Structure–function mapping | Classification of Radical SAM enzymes by sequence similarity | classification of Radical SAM enzymes by sequence similarity | subgroups and families in the Radical SAM superfamily | sequence similarity networks | multiple domain structures of Radical SAM superfamily enzymes | structure-function mapping, phylogenetic representation
Sequence similarity networks | Phylogenetic representation | Radical SAM superfamily census | Subgroups and families in the radical SAM superfamily | Multiple domain structures of radical SAM superfamily enzymes | Structure–function mapping | Classification of Radical SAM enzymes by sequence similarity | classification of Radical SAM enzymes by sequence similarity | subgroups and families in the Radical SAM superfamily | sequence similarity networks | multiple domain structures of Radical SAM superfamily enzymes | structure-function mapping, phylogenetic representation
Conference Proceeding
RNA, ISSN 1355-8382, 03/2017, Volume 23, Issue 3, pp. 346 - 354
S-adenosylmethionine (SAM)-dependent methyltransferases regulate a wide range of biological processes through the modification of proteins, nucleic acids,...
Wybutosine | tRNA | TYW3 | Structural biology | Methyltransferase | METHYLATION | methyltransferase | ACID | TRANSFER-RNA MODIFICATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | REPLACEMENT | NUCLEOTIDE | wybutosine | BIOSYNTHESIS | BINDING PROTEINS | structural biology | ANTICODON | WYBUTOSINE SYNTHESIZING ENZYME | Methyltransferases - metabolism | Archaeal Proteins - chemistry | Methyltransferases - genetics | Substrate Specificity | Crystallography, X-Ray | S-Adenosylmethionine - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Archaeal Proteins - genetics | Nucleosides - metabolism | Protein Interaction Domains and Motifs | Archaeal Proteins - metabolism | Recombinant Proteins - metabolism | Methyltransferases - chemistry | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Nucleosides - chemistry | Mutagenesis, Site-Directed | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Sulfolobus solfataricus - chemistry | Sulfolobus solfataricus - enzymology | Amino Acid Motifs | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Molecular Docking Simulation | Kinetics | S-Adenosylmethionine - metabolism | Index Medicus
Wybutosine | tRNA | TYW3 | Structural biology | Methyltransferase | METHYLATION | methyltransferase | ACID | TRANSFER-RNA MODIFICATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | REPLACEMENT | NUCLEOTIDE | wybutosine | BIOSYNTHESIS | BINDING PROTEINS | structural biology | ANTICODON | WYBUTOSINE SYNTHESIZING ENZYME | Methyltransferases - metabolism | Archaeal Proteins - chemistry | Methyltransferases - genetics | Substrate Specificity | Crystallography, X-Ray | S-Adenosylmethionine - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Archaeal Proteins - genetics | Nucleosides - metabolism | Protein Interaction Domains and Motifs | Archaeal Proteins - metabolism | Recombinant Proteins - metabolism | Methyltransferases - chemistry | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Nucleosides - chemistry | Mutagenesis, Site-Directed | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Sulfolobus solfataricus - chemistry | Sulfolobus solfataricus - enzymology | Amino Acid Motifs | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Molecular Docking Simulation | Kinetics | S-Adenosylmethionine - metabolism | Index Medicus
Journal Article
1991, 2 pp. ;Fiche:0.
Book
1991, [1]p.
Book
1786, volumes.
Book
Organic Letters, ISSN 1523-7060, 01/2013, Volume 15, Issue 2, pp. 414 - 417
The histone lysine monomethyltransferase SETD8 is an epigenetic regulator of cell cycle progression. Nahuoic acid A (1), a polyketide produced in culture by a...
Histone-Lysine N-Methyltransferase - antagonists & inhibitors | Streptomyces - chemistry | Polyketides - isolation & purification | Geologic Sediments - chemistry | Nuclear Magnetic Resonance, Biomolecular | Polyketides - chemistry | Molecular Structure | Polyketides - pharmacology
Histone-Lysine N-Methyltransferase - antagonists & inhibitors | Streptomyces - chemistry | Polyketides - isolation & purification | Geologic Sediments - chemistry | Nuclear Magnetic Resonance, Biomolecular | Polyketides - chemistry | Molecular Structure | Polyketides - pharmacology
Journal Article
New West Indian Guide, ISSN 1382-2373, 12/2018, Volume 92, Issue 3-4, pp. 355 - 356
Journal Article
Los Angeles Lawyer, ISSN 0162-2900, 09/2013, Volume 36, Issue 6, p. 8
Journal Article
Biochemistry, 09/2016, Volume 55, Issue 36, p. 5010
The dependence of the conformation of the S-adenosylmethionine (SAM) II riboswitch on the concentration of added Mg(2+) ions and SAM, individually and in...
Magnesium - chemistry | Riboswitch | Chelating Agents - chemistry | Protein Conformation | S-Adenosylmethionine - chemistry | Circular Dichroism | Methylamines - chemistry
Magnesium - chemistry | Riboswitch | Chelating Agents - chemistry | Protein Conformation | S-Adenosylmethionine - chemistry | Circular Dichroism | Methylamines - chemistry
Journal Article
CALLALOO, ISSN 0161-2492, 2017, Volume 40, Issue 5, pp. 59 - 68
Journal Article
20.
Full Text
Structure-guided discovery of carboxy-SAM as a novel metabolite modulating tRNA function
Nature, ISSN 0028-0836, 6/2013, Volume 498, Issue 7452, pp. 123 - 126
Identifying novel metabolites and characterizing their biological functions are major challenges of the post-genomic era. X-ray crystallography can reveal...
Journal Article
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