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The Journal of biological chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 40, pp. 15429 - 15438
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Humans | Substrate Specificity | Crystallography, X-Ray | Chitinases - metabolism | Isoenzymes - chemistry | beta-N-Acetylhexosaminidases - chemistry | Berberine - metabolism | Chitinases - genetics | Isoenzymes - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | beta-N-Acetylhexosaminidases - genetics | Binding Sites | Moths - chemistry | Chitinases - chemistry | Berberine - chemistry | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Chitinases - antagonists & inhibitors | Gene Expression | Genetic Vectors - chemistry | Isoenzymes - genetics | beta-N-Acetylhexosaminidases - metabolism | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | beta-N-Acetylhexosaminidases - antagonists & inhibitors | Recombinant Proteins - genetics | Medicine, Chinese Traditional - methods | Glycoside Hydrolase Inhibitors - chemistry | Static Electricity | Saccharomyces cerevisiae - chemistry | Animals | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Saccharomyces cerevisiae - enzymology | Quinazolinones - chemistry | Kinetics | Quinazolinones - metabolism | Moths - enzymology | Isoenzymes - antagonists & inhibitors | Index Medicus | glycoside hydrolase | chitinase | β-N-acetyl-D-hexosaminidase | inhibitor | protein crystallization | insect | Enzymology | human | berberine
Journal Article
Molecular cell, ISSN 1097-2765, 10/2016, Volume 64, Issue 2, pp. 307 - 319
crystal structure | U2AF65 | SF3b | SF3B1 | cancer-related mutations | pre-mRNA splicing | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Oncogene Proteins - genetics | Spliceosomes - chemistry | Baculoviridae - metabolism | Humans | Baculoviridae - genetics | Crystallography, X-Ray | RNA Splicing Factors - chemistry | Moths | Neoplasm Proteins - metabolism | Phosphoproteins - metabolism | Phosphoproteins - chemistry | Protein Subunits - metabolism | RNA Splicing Factors - metabolism | Spliceosomes - metabolism | RNA Splicing | Cloning, Molecular | Protein Interaction Domains and Motifs | Neoplasm Proteins - genetics | Binding Sites | Genes, Tumor Suppressor | Protein Subunits - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Oncogene Proteins - chemistry | Oncogene Proteins - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Recombinant Proteins - genetics | Spliceosomes - ultrastructure | Phosphoproteins - genetics | RNA Splicing Factors - genetics | Splicing Factor U2AF - genetics | Animals | Protein Conformation, beta-Strand | Protein Binding | Splicing Factor U2AF - chemistry | Protein Subunits - chemistry | HeLa Cells | Mutation | Splicing Factor U2AF - metabolism | Crosslinked polymers | RNA | Crystals | Genetic aspects | Structure | Binding proteins | Mass spectrometry | Cancer | Protein binding | Index Medicus
Journal Article
Scientific reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 2386 - 9
Journal Article
Protein science, ISSN 0961-8368, 08/2017, Volume 26, Issue 8, pp. 1627 - 1638
Vigna unguiculata subsp. cylindrica | apyrase | ATP hydrolysis | Dolichos biflorus | NTPDase | Trifolium repens | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Vigna - chemistry | Adenosine Monophosphate - chemistry | Phosphates - chemistry | Substrate Specificity | Crystallography, X-Ray | Isoenzymes - chemistry | Toxoplasma - enzymology | Trifolium - chemistry | Trifolium - enzymology | Toxoplasma - chemistry | Isoenzymes - metabolism | Plant Proteins - chemistry | Adenosine Triphosphate - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Vigna - enzymology | Plant Proteins - metabolism | Protein Interaction Domains and Motifs | Legionella pneumophila - enzymology | Legionella pneumophila - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Adenosine Monophosphate - metabolism | Isoenzymes - genetics | Apyrase - metabolism | Models, Molecular | Rats | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Manganese - chemistry | Sequence Homology, Amino Acid | Plant Proteins - genetics | Phosphates - metabolism | Sequence Alignment | Animals | Manganese - metabolism | Protein Conformation, beta-Strand | Escherichia coli - genetics | Apyrase - genetics | Protein Binding | Apyrase - chemistry | Kinetics | Adenosine Triphosphate - chemistry | Nucleosides | Enzymes | Nucleotides | Structure | Analysis | Crystals | Phosphates | AMP | Adenine | Data processing | Reaction kinetics | Butterflies & moths | Catalysis | Legionnaires' disease bacterium | Crystal structure | Manganese | Index Medicus
Journal Article
10.