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Neurotherapeutics, ISSN 1933-7213, 1/2015, Volume 12, Issue 1, pp. 49 - 56
Between 20% and 25% of patients diagnosed with Alzheimer’s disease (AD) do not have amyloid burden as assessed by positron emission tomography imaging. Thus,... 
Neurology | Neurosciences | Biomedicine | Phosphodiesterase-4 | Alzheimer’s disease | neuroinflammation | PDE4 | Neurobiology | Acrodysostosis | Neurosurgery | ACRDY2 | Review
Journal Article
Nucleic Acids Research, ISSN 0305-1048, 9/2008, Volume 36, Issue 15, pp. 4883 - 4893
The DNA cleavage reaction of human topoisomerase IIα is critical to all of the physiological and pharmacological functions of the protein. While it has long... 
ANGSTROM RESOLUTION | LEAVING GROUP STABILIZATION | ACTIVE-SITE | RELIGATION REACTION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | HAMMERHEAD RIBOZYME | METAL-ION COORDINATION | SINGLE-STRANDED-DNA | POLYMERASE-I | Nucleic Acid Enzymes
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2002, Volume 99, Issue 24, pp. 15387 - 15392
We report the x-ray crystal structure of human topoisomerase I covalently joined to double-stranded DNA and bound to the clinically approved anticancer agent... 
Enzymes | Biological Sciences | Oxygen | Hydrogen bonds | DNA | Drug interactions | Chemical bases | Electron density | Carboxylates | Lactones | Crystal structure | RESISTANT | COMPLEX | INHIBITION | NUCLEIC-ACID | MULTIDISCIPLINARY SCIENCES | MUTATION | CRYSTAL-STRUCTURES | DNA TOPOISOMERASES | CANCER CELL-LINE | BINDING | ANTITUMOR DRUGS | Humans | DNA Topoisomerases, Type I - chemistry | Recombinant Fusion Proteins - physiology | Topoisomerase I Inhibitors | Crystallography, X-Ray | Drug Resistance, Neoplasm | Neoplasm Proteins - antagonists & inhibitors | Structure-Activity Relationship | Neoplasm Proteins - metabolism | Recombinant Fusion Proteins - metabolism | Topotecan - chemistry | Peptide Fragments - physiology | Enzyme Inhibitors - chemistry | Antineoplastic Agents - pharmacology | Molecular Structure | Neoplasm Proteins - genetics | Peptide Fragments - metabolism | Topotecan - pharmacology | DNA Topoisomerases, Type I - metabolism | DNA Topoisomerases, Type I - genetics | Enzyme Inhibitors - pharmacology | Models, Molecular | Neoplasm Proteins - chemistry | Intercalating Agents - pharmacology | DNA - metabolism | Recombinant Fusion Proteins - chemistry | Antineoplastic Agents - chemistry | Intercalating Agents - chemistry | Macromolecular Substances | DNA - chemistry | Peptide Fragments - chemistry | Hydrogen Bonding | Protein Binding | Protein Conformation | Mutation | Physiological aspects | Structure-activity relationship (Pharmacology) | Drug resistance | Drug therapy | Cancer | Drugs | Biochemistry | Deoxyribonucleic acid | Crystals
Journal Article
Cell, ISSN 0092-8674, 02/2012, Volume 148, Issue 3, pp. 421 - 433
Journal Article
Nature Biotechnology, ISSN 1087-0156, 01/2010, Volume 28, Issue 1, pp. 63 - 70
Phosphodiesterase 4 (PDE4), the primary cAMP-hydrolyzing enzyme in cells, is a promising drug target for a wide range of conditions. Here we present seven... 
CAMP-SPECIFIC PHOSPHODIESTERASE | PHOSPHORYLATION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PROTEIN-KINASE | GENE COMPOSER | SUNCUS-MURINUS | AMP-SPECIFIC PHOSPHODIESTERASE | INHIBITORS | CYCLIC-NUCLEOTIDE PHOSPHODIESTERASE | ROLIPRAM BINDING | ANTIDEPRESSANT DRUGS | Phosphodiesterase Inhibitors - therapeutic use | Phosphodiesterase Inhibitors - adverse effects | Humans | Molecular Sequence Data | Crystallography, X-Ray | Structure-Activity Relationship | Benzhydryl Compounds - chemistry | Benzhydryl Compounds - adverse effects | Phenylurea Compounds - adverse effects | Phenylurea Compounds - chemistry | Drug Design | Phosphodiesterase 4 Inhibitors | Behavior, Animal - drug effects | Biological Assay | Phosphodiesterase Inhibitors - chemistry | Benzhydryl Compounds - therapeutic use | Cyclic Nucleotide Phosphodiesterases, Type 4 - chemistry | Disease Models, Animal | Allosteric Regulation - drug effects | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Catalytic Domain | Models, Molecular | Phenylurea Compounds - therapeutic use | Phosphodiesterase Inhibitors - pharmacology | Vomiting - drug therapy | Cognition - drug effects | Animals | Benzhydryl Compounds - pharmacology | Mice | Phenylurea Compounds - pharmacology | Kinetics | Care and treatment | Schizophrenia | Physiological aspects | Genetic aspects | Cellular signal transduction | Cyclic adenylic acid | Research | Phosphodiesterases | Enzymes | Biotechnology | Cellular biology | Molecular biology | Cognitive ability | Crystal structure | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2012, Volume 109, Issue 49, pp. 19971 - 19976
Journal Article