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Journal Article
Journal Article
Acta crystallographica. Section F, Structural biology communications, ISSN 2053-230X, 2018, Volume 74, Issue 6, pp. 373 - 384
Nucleoside diphosphate kinases (NDKs) are implicated in a wide variety of cellular functions owing to their enzymatic conversion of NDP to NTP. NDK from ( NDK)... 
structural genomics | protein structure | Lyme disease | bacterial metabolism | Borrelia burgdorferi | protein crystallization | nucleoside diphosphate kinase | Seattle Structural Genomics Center for Infectious Disease | LYME-DISEASE SPIROCHETE | PROTEIN-PRODUCTION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-STRUCTURE | BIOCHEMICAL RESEARCH METHODS | CRYSTALLOGRAPHY | IDENTIFICATION | DICTYOSTELIUM | INFECTIOUS-DISEASE | TRANSPOSON MUTAGENESIS | BIOPHYSICS | LINEAR PLASMID-25 | GENOMICS CENTER | Adenosine Diphosphate - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Protein Structure, Secondary | Nucleoside-Diphosphate Kinase - metabolism | Adenosine Diphosphate - chemistry | Vanadates - chemistry | Mice, Inbred C3H | Vanadates - metabolism | Borrelia burgdorferi - enzymology | Animals | Nucleoside-Diphosphate Kinase - chemistry | Borrelia burgdorferi - genetics | Female | Mice | Adenosine Diphosphate - metabolism | Binding Sites | Nucleoside-Diphosphate Kinase - genetics | Data banks | Quaternary | Crystallization | Adenosine diphosphate | Infections | Kinases | Mutants | Vanadate | Proteins | Infectious diseases | Infectivity | Vanadates | Nucleosides | Ligands | Catalysis | Inhibition | Phosphohistidine | Nucleoside-diphosphate kinase | Protein structure | Structural analysis | Structure-function relationships
Journal Article
Circulation (New York, N.Y.), ISSN 1524-4539, 2013, Volume 127, Issue 24, pp. 2442 - 2451
BACKGROUND—Progerin is a mutant form of lamin A responsible for Hutchinson-Gilford progeria syndrome (HGPS), a premature aging disorder characterized by... 
Tissue-non specific alkaline phosphatase | Progerin | Pyrophosphate | Smooth | Vascular calcification | Hutchinson-Gilford progeria syndrome | Muscle | ATP | CALCIUM-PHOSPHATE DEPOSITION | AORTIC CALCIFICATION | CARDIAC & CARDIOVASCULAR SYSTEMS | progerin | ALKALINE-PHOSPHATASE | vascular calcification | MITOCHONDRIA | pyrophosphate | MUSCLE-CELL CALCIFICATION | tissue-non specific alkaline phosphatase | LAMIN | SMOOTH-MUSCLE | BISPHOSPHONATES | muscle | ARTERIAL CALCIFICATION | PERIPHERAL VASCULAR DISEASE | ATP RELEASE | smooth | Diphosphates - pharmacology | Diphosphates - metabolism | Muscle, Smooth, Vascular - metabolism | Alkaline Phosphatase - metabolism | Male | Aorta - metabolism | Progeria - metabolism | Progeria - drug therapy | Vascular Calcification - metabolism | Mice, Mutant Strains | Adenosine Triphosphate - metabolism | Mitochondria, Muscle - physiology | Disease Models, Animal | Muscle, Smooth, Vascular - drug effects | Aorta - drug effects | Mice, Inbred C57BL | Cells, Cultured | Treatment Outcome | Lamin Type A - metabolism | Vascular Calcification - drug therapy | Aorta - pathology | Muscle, Smooth, Vascular - pathology | Animals | Mice | Diphosphates - therapeutic use | Animal experimentation | Blood circulation disorders | Usage | Progeria | Drug therapy | Pyrophosphates | Health aspects | Risk factors
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2007, Volume 104, Issue 24, pp. 10022 - 10027
Bisphosphonate drugs (e.g., Fosamax and Zometa) are thought to act primarily by inhibiting farnesyl diphosphate synthase (FPPS), resulting in decreased... 
Enzymes | Yeasts | Electronic structure | Molecular structure | Terpenoids | Diphosphonates | Ligands | Biosynthesis | Diphosphates | Binding sites | Undecaprenyl diphosphate synthase | Geranylgeranyl diphosphate synthase | X-ray structure | Cell wall | FARNESYL DIPHOSPHATE SYNTHASE | POTENTIAL ROUTE | INHIBITION | MECHANISM | ISOPRENOID BIOSYNTHESIS | STRUCTURAL BASIS | NITROGEN-CONTAINING BISPHOSPHONATES | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | GERANYLGERANYL PYROPHOSPHATE SYNTHASE | DRUGS | Diphosphates - metabolism | Polyisoprenyl Phosphates - chemistry | Sesquiterpenes - metabolism | Models, Chemical | Stereoisomerism | Alkyl and Aryl Transferases - antagonists & inhibitors | Substrate Specificity | Crystallography, X-Ray | Isoenzymes - chemistry | Isoenzymes - metabolism | Transferases - metabolism | Farnesyltranstransferase - antagonists & inhibitors | Molecular Structure | Transferases - antagonists & inhibitors | Diterpenes - metabolism | Binding Sites | Dimerization | Diterpenes - chemistry | Alkyl and Aryl Transferases - chemistry | Sesquiterpenes - chemistry | Protein Structure, Secondary | Models, Molecular | Transferases - chemistry | Diphosphonates - metabolism | Polyisoprenyl Phosphates - metabolism | Farnesyltranstransferase - chemistry | Diphosphates - chemistry | Diphosphonates - chemistry | Hydrophobic and Hydrophilic Interactions | Saccharomyces cerevisiae - enzymology | Isoenzymes - antagonists & inhibitors | Usage | Research | X-ray spectroscopy | Plant cell walls | Guanosine triphosphatase | Biological Sciences | undecaprenyl diphosphate synthase | x-ray structure | geranylgeranyl diphosphate synthase | cell wall
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2013, Volume 342, Issue 6163, pp. 1235 - 1239
Journal Article
Journal Article