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1. Full Text Stereospecific targeting of MTH1 by (S)-crizotinib as an anticancer strategy
by Huber, Kilian V M and Huber, Kilian V.M and Salah, Eidarus and Salah, Eidarus and Radic, Branka and Radic, Branka and Gridling, Manuela and Gridling, Manuela and Elkins, Jonathan M and Elkins, Jonathan M and Stukalov, Alexey and Stukalov, Alexey and Jemth, Ann-Sofie and Jemth, Ann-Sofie and Göktürk, Camilla and Göktürk, Camilla and Sanjiv, Kumar and Sanjiv, Kumar and Strömberg, Kia and Strömberg, Kia and Pham, Therese and Pham, Therese and Berglund, Ulrika Warpman and Berglund, Ulrika Warpman and Colinge, Jacques and Colinge, Jacques and Bennett, Keiryn L and Bennett, Keiryn L and Loizou, Joanna I and Loizou, Joanna I and Helleday, Thomas and Helleday, Thomas and Knapp, Stefan and Knapp, Stefan and Superti-Furga, Giulio and Superti-Furga, Giulio
Nature, ISSN 0028-0836, 2014, Volume 508, Issue 7495, pp. 222 - 227
Activated RAS GTPase signalling is a critical driver of oncogenic transformation and malignant disease. Cellular models of RAS-dependent cancers have been used... 
CELL LUNG-CANCER | RAS-TRANSFORMATION | OVEREXPRESSION | OXIDATIVE STRESS | HMTH1 | MESSENGER-RNA | GENE | MULTIDISCIPLINARY SCIENCES | HUMAN MUTT HOMOLOG | TUMORIGENESIS | SMALL-MOLECULE INHIBITION | ras Proteins - genetics | Colonic Neoplasms - genetics | Proto-Oncogene Proteins p21(ras) | Pyridines - chemistry | Colonic Neoplasms - drug therapy | Humans | Substrate Specificity | DNA Breaks, Single-Stranded - drug effects | Protein Kinase Inhibitors - chemistry | Pyrazoles - chemistry | Phosphoric Monoester Hydrolases - biosynthesis | DNA Repair Enzymes - metabolism | Female | Antineoplastic Agents - pharmacology | DNA Repair Enzymes - antagonists & inhibitors | Homeostasis - drug effects | Aminoquinolines - pharmacology | DNA Repair Enzymes - chemistry | Disease Models, Animal | Phosphoric Monoester Hydrolases - antagonists & inhibitors | Pyrazoles - pharmacology | Crystallization | Models, Molecular | Proto-Oncogene Proteins - genetics | Antineoplastic Agents - chemistry | Mice, SCID | Nucleotides - metabolism | Xenograft Model Antitumor Assays | Animals | Colonic Neoplasms - pathology | DNA Repair | DNA Repair Enzymes - biosynthesis | Proteomics | Protein Conformation | Mice | Protein Kinase Inhibitors - pharmacology | Pyridines - pharmacology | Phosphoric Monoester Hydrolases - metabolism | Phosphoric Monoester Hydrolases - chemistry | Crizotinib | Enzymes | Colon cancer | Physiological aspects | Genetic aspects | Research | Nucleotides | Studies | Oxidative stress | Inhibitor drugs | Medical prognosis | Homeostasis | Mutation | Kinases | Experiments | Cancer | Index Medicus | Life Sciences | crizotinib | cancer | stereoselectivity | MTH1 | DNA repair | drug
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2. Full Text MTH1 inhibition eradicates cancer by preventing sanitation of the dNTP pool
by Gad, Helge and Gad, Helge and Koolmeister, Tobias and Koolmeister, Tobias and Jemth, Ann-Sofie and Jemth, Ann-Sofie and Eshtad, Saeed and Eshtad, Saeed and Jacques, Sylvain A and Jacques, Sylvain A and Ström, Cecilia E and Ström, Cecilia E and Svensson, Linda M and Svensson, Linda M and Schultz, Niklas and Schultz, Niklas and Lundbäck, Thomas and Lundbäck, Thomas and Einarsdottir, Berglind Osk and Einarsdottir, Berglind Osk and Saleh, Aljona and Saleh, Aljona and Göktürk, Camilla and Göktürk, Camilla and Baranczewski, Pawel and Baranczewski, Pawel and Svensson, Richard and Svensson, Richard and Berntsson, Ronnie P-A and Berntsson, Ronnie P.-A and Gustafsson, Robert and Gustafsson, Robert and Strömberg, Kia and Strömberg, Kia and Sanjiv, Kumar and Sanjiv, Kumar and Jacques-Cordonnier, Marie-Caroline and Jacques-Cordonnier, Marie-Caroline and Desroses, Matthieu and Desroses, Matthieu and Gustavsson, Anna-Lena and Gustavsson, Anna-Lena and Olofsson, Roger and Olofsson, Roger and Johansson, Fredrik and Johansson, Fredrik and Homan, Evert J and Homan, Evert J and Loseva, Olga and Loseva, Olga and Bräutigam, Lars and Bräutigam, Lars and Johansson, Lars and Johansson, Lars and Höglund, Andreas and Höglund, Andreas and Hagenkort, Anna and Hagenkort, Anna and Pham, Therese and Pham, Therese and Altun, Mikael and Altun, Mikael and Gaugaz, Fabienne Z and Gaugaz, Fabienne Z and Vikingsson, Svante and Vikingsson, Svante and Evers, Bastiaan and Evers, Bastiaan and Henriksson, Martin and Henriksson, Martin and Vallin, Karl S A and Vallin, Karl S.A and Wallner, Olov A and Wallner, Olov A and Hammarström, Lars G.J and Hammarström, Lars G J and Wiita, Elisee and Wiita, Elisee and Almlöf, Ingrid and Almlöf, Ingrid and Kalderén, Christina and Kalderén, Christina and Axelsson, Hanna and Axelsson, Hanna and Djureinovic, Tatjana and Djureinovic, Tatjana and Puigvert, Jordi Carreras and Puigvert, Jordi Carreras and Häggblad, Maria and Häggblad, Maria and Jeppsson, Fredrik and Jeppsson, Fredrik and Martens, Ulf and Martens, Ulf and Lundin, Cecilia and Lundin, Cecilia and Lundgren, B and Lundgren, Bo and Granelli, Ingrid and Granelli, Ingrid and ... and Institutionen för medicin och hälsa and Avdelningen för läkemedelsforskning and Linköpings universitet and Hälsouniversitetet
Nature, ISSN 0028-0836, 2014, Volume 508, Issue 7495, pp. 215 - 221
Cancers have dysfunctional redox regulation resulting in reactive oxygen species production, damaging both DNA and free dNTPs. The MTH1 protein sanitizes... 
TARGET | CELLS | OXIDATIVE STRESS | REPAIR | HMTH1 | PROTEIN | MULTIDISCIPLINARY SCIENCES | DNA-SYNTHESIS | MUTAGENIC SUBSTRATE | CELLULAR SENESCENCE | 8-OXOGUANINE | Neoplasms - metabolism | Humans | Molecular Conformation | Male | Molecular Targeted Therapy | Pyrimidines - chemistry | Pyrophosphatases - antagonists & inhibitors | Enzyme Inhibitors - pharmacokinetics | Enzyme Inhibitors - chemistry | DNA Repair Enzymes - metabolism | Oxidation-Reduction - drug effects | Female | Deoxyguanine Nucleotides - metabolism | Cell Death - drug effects | DNA Repair Enzymes - antagonists & inhibitors | DNA Repair Enzymes - chemistry | Phosphoric Monoester Hydrolases - antagonists & inhibitors | Cell Survival - drug effects | Catalytic Domain | Reproducibility of Results | Crystallization | Enzyme Inhibitors - pharmacology | Models, Molecular | Pyrimidines - pharmacology | Nucleotides - metabolism | Enzyme Inhibitors - therapeutic use | Neoplasms - drug therapy | Xenograft Model Antitumor Assays | Animals | Pyrimidines - therapeutic use | Pyrimidines - pharmacokinetics | Mice | DNA Damage | Neoplasms - pathology | Phosphoric Monoester Hydrolases - metabolism | Phosphoric Monoester Hydrolases - chemistry | Prevention | Deoxyribonucleotides | DNA damage | Cancer cells | Physiological aspects | Research | Binding proteins | Cancer | Cytotoxicity | Kinases | Cancer therapies | Defects | Proteins | Genotype & phenotype | Mutagenesis | Rodents | Cell cycle | Mutation | Deoxyribonucleic acid--DNA | Tumors | Apoptosis | Index Medicus | Medical and Health Sciences | MEDICINE | Medicin och hälsovetenskap | MEDICIN
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3. Full Text The Sac1 Domain of SYNJ1 Identified Mutated in a Family with Early‐Onset Progressive Parkinsonism with Generalized Seizures
by Krebs, Catharine E and Karkheiran, Siamak and Powell, James C and Cao, Mian and Makarov, Vladimir and Darvish, Hossein and Di Paolo, Gilbert and Walker, Ruth H and Shahidi, Gholam Ali and Buxbaum, Joseph D and De Camilli, Pietro and Yue, Zhenyu and Paisán‐Ruiz, Coro
Human Mutation, ISSN 1059-7794, 09/2013, Volume 34, Issue 9, pp. 1200 - 1207
This study aimed to elucidate the genetic causes underlying early‐onset P arkinsonism ( EOP ) in a consanguineous I ranian family. To attain this, homozygosity... 
whole‐exome sequencing | arkinsonism | SYNJ | homozygosity mapping | autosomal recessive | Homozygosity mapping | SYNJ1 | Whole-exome sequencing | Autosomal recessive Parkinsonism | whole-exome sequencing | GENETICS & HEREDITY | autosomal recessive Parkinsonism | Epilepsy, Generalized - genetics | Phosphoric Monoester Hydrolases - genetics | Humans | Genotype | Male | Phylogeny | Genes, Recessive | Sequence Analysis, DNA | Brain - metabolism | Exome | Parkinsonian Disorders - metabolism | Sequence Alignment | Epilepsy, Generalized - metabolism | Age of Onset | HEK293 Cells | Adult | Female | Parkinsonian Disorders - genetics | Consanguinity | Polymorphism, Single Nucleotide | Phosphoric Monoester Hydrolases - metabolism | Phosphoric Monoester Hydrolases - chemistry | Inositol | Parkinson's disease | Seizures (Medicine) | Glutamine | Phosphatase | Mutation | Index Medicus | autosomal recessive parkinsonism | whole exome sequencing
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4. Full Text The human DEPhOsphorylation database DEPOD: A 2015 update
by Duan, Guangyou and Li, Xun and Köhn, Maja
Nucleic Acids Research, ISSN 0305-1048, 01/2015, Volume 43, Issue 1, pp. D531 - D535
Phosphatases are crucial enzymes in health and disease, but the knowledge of their biological roles is still limited. Identifying substrates continues to be a... 
PROTEIN | MOLECULAR INTERACTION DATABASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOURCE | Phosphoric Monoester Hydrolases - classification | Databases, Protein | Humans | Phosphoprotein Phosphatases - metabolism | Protein Processing, Post-Translational | Internet | Phosphoric Monoester Hydrolases - metabolism | Phosphoric Monoester Hydrolases - chemistry | Index Medicus | Database Issue
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5. Full Text A large-scale method to measure absolute protein phosphorylation stoichiometries
by Wu, Ronghu and Haas, Wilhelm and Dephoure, Noah and Huttlin, Edward L and Zhai, Bo and Sowa, Mathew E and Gygi, Steven P
Nature Methods, ISSN 1548-7091, 08/2011, Volume 8, Issue 8, pp. 677 - 683
The functional role of protein phosphorylation is impacted by its fractional stoichiometry. Thus, a comprehensive strategy to study phosphorylation dynamics... 
PHOSPHOPROTEOMICS | QUANTIFICATION | BIOCHEMICAL RESEARCH METHODS | QUANTITATIVE PROTEOMIC ANALYSIS | SITES | LABELING STRATEGY | IDENTIFICATION | MASS-SPECTROMETRY | ACCURACY | Phosphorylation - physiology | Isotope Labeling - methods | Phosphoric Monoester Hydrolases - metabolism | Proteome - chemistry | Mass Spectrometry - methods | Proteome - metabolism | Phosphoric Monoester Hydrolases - chemistry | Proteins | Biochemistry | Peptides | Isotopes | Index Medicus
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6. Full Text Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase
by Kai Xun Chan and Peter D. Mabbitt and Su Yin Phua and Jonathan W. Mueller and Nazia Nisar and Tamara Gigolashvili and Elke Stroeher and Julia Grassl and Wiebke Arlt and Gonzalo M. Estavillo and Colin J. Jackson and Barry J. Pogson
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2016, Volume 113, Issue 31, pp. E4567 - E4576
Intracellular signaling during oxidative stress is complex, with organelle-to-nucleus retrograde communication pathways ill-defined or incomplete. Here we... 
ARABIDOPSIS-THALIANA | redox regulation | PROTEIN-STRUCTURE | MULTIDISCIPLINARY SCIENCES | DROUGHT TOLERANCE | RESPONSES | retrograde signaling | drought stress | chloroplast | GLUTATHIONE | ALLOSTERIC INHIBITION | THIOREDOXIN | SINGLET OXYGEN | NORMAL-MODE ANALYSIS | stress sensing | Disulfides - metabolism | Amino Acid Sequence | Arabidopsis Proteins - genetics | Phosphoric Monoester Hydrolases - genetics | Arabidopsis - enzymology | Oxidation-Reduction | Oxidative Stress | Signal Transduction | Protein Multimerization | Substrate Specificity | Chloroplasts - metabolism | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Sequence Homology, Amino Acid | Arabidopsis Proteins - chemistry | Gene Expression Regulation, Plant | Adenosine Diphosphate - metabolism | Enzyme Activation | Phosphoric Monoester Hydrolases - metabolism | Glutathione | Phosphoric Monoester Hydrolases - chemistry | Oxidative stress | Signal transduction | Chloroplasts | Plant biology | Genetics | Photosynthesis | Stress response | Index Medicus | Biological Sciences | PNAS Plus
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7. Full Text Structural insight into filament formation by mammalian septins
by Wittinghofer, Alfred and Hauer, Florian and Sirajuddin, Minhajuddin and Macara, Ian G and Stark, Holger and Farkasovsky, Marian and Weyand, Michael and Kühlmann, Dorothee
Nature, ISSN 0028-0836, 09/2007, Volume 449, Issue 7160, pp. 311 - 315
Septins are GTP-binding proteins that assemble into homo- and hetero-oligomers and filaments. Although they have key roles in various cellular processes,... 
ORGANIZATION | SYSTEM | YEAST SEPTINS | COMPLEX | PROTEIN | SYMMETRY | MULTIDISCIPLINARY SCIENCES | SACCHAROMYCES | GENE FAMILY | CLASSIFICATION | GTP-BINDING | Cytoskeletal Proteins | Protein Structure, Tertiary | GTP-Binding Proteins - chemistry | Phosphoric Monoester Hydrolases - ultrastructure | Humans | Cell Cycle Proteins - metabolism | Septins | Cell Cycle Proteins - ultrastructure | Models, Molecular | Crystallography, X-Ray | GTP-Binding Proteins - ultrastructure | Nucleotides - metabolism | Cell Cycle Proteins - chemistry | Multiprotein Complexes - metabolism | Multiprotein Complexes - ultrastructure | Multiprotein Complexes - chemistry | Protein Structure, Quaternary | Phosphoric Monoester Hydrolases - metabolism | Binding Sites | Dimerization | GTP-Binding Proteins - metabolism | Phosphoric Monoester Hydrolases - chemistry | Chemical properties | Research | Binding proteins | Structure | Protein-protein interactions | Proteins | Biochemistry | Cellular biology | Mammals | Polymers | Binding sites | Human | Oligomers | Asymmetry | Filaments | Coiling | X-rays | Blocking | Polarity | Index Medicus
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8. Full Text Tks5 and SHIP2 Regulate Invadopodium Maturation, but Not Initiation, in Breast Carcinoma Cells
by Sharma, Ved P and Eddy, Robert and Entenberg, David and Kai, Masayuki and Gertler, Frank B and Condeelis, John
Current Biology, ISSN 0960-9822, 11/2013, Volume 23, Issue 21, pp. 2079 - 2089
Tks5 regulates invadopodium formation, but the precise timing during invadopodium lifetime (initiation, stabilization, maturation) when Tks5 plays a role is... 
CANCER-CELLS | I-ALPHA | INVASION | MATRIX DEGRADATION | INOSITOL 5-PHOSPHATASE SHIP2 | CORTACTIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | N-WASP-ARP2/3 COMPLEX | N-WASP | ADAPTER PROTEIN | PODOSOME FORMATION | CELL BIOLOGY | Phosphoric Monoester Hydrolases - genetics | Cell Surface Extensions - metabolism | Humans | Adaptor Proteins, Vesicular Transport - genetics | Inositol Polyphosphate 5-Phosphatases | Adaptor Proteins, Vesicular Transport - metabolism | Breast Neoplasms - metabolism | Breast Neoplasms - pathology | Neoplasm Metastasis - pathology | Biosensing Techniques | Female | Adaptor Proteins, Vesicular Transport - chemistry | Microfilament Proteins - metabolism | Phosphoric Monoester Hydrolases - metabolism | Cell Movement | Phosphoric Monoester Hydrolases - chemistry | Breast cancer | Index Medicus
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9. Full Text Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
by Murata, Yoshimichi and Iwasaki, Hirohide and Okamura, Yasushi and Inaba, Kazuo and Sasaki, Mari
Nature, ISSN 0028-0836, 06/2005, Volume 435, Issue 7046, pp. 1239 - 1243
Changes in membrane potential affect ion channels and transporters, which then alter intracellular chemical conditions. Other signalling pathways coupled to... 
ACTIVATION | PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE | PERSPECTIVE | POTASSIUM CHANNELS | MULTIDISCIPLINARY SCIENCES | ASCIDIAN CIONA-INTESTINALIS | PTEN | RECTIFYING K+ CHANNELS | TUMOR-SUPPRESSOR | ION CHANNELS | IDENTIFICATION | Immunohistochemistry | Protein Structure, Tertiary | Xenopus | Amino Acid Sequence | Phosphoric Monoester Hydrolases - genetics | Oocytes - metabolism | Electrophysiology | Molecular Sequence Data | Male | Membrane Potentials - physiology | Ciona intestinalis - genetics | Ciona intestinalis - enzymology | Potassium Channels - metabolism | Animals | Sperm Tail - enzymology | Phosphatidylinositols - metabolism | Phosphoric Monoester Hydrolases - metabolism | Phosphoric Monoester Hydrolases - chemistry | Proteins | Cellular biology | Genomics | Genes | Deoxyribonucleic acid--DNA | Index Medicus
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10. Full Text A family of metal-dependent phosphatases implicated in metabolite damage-control
by Huang, Lili and Khusnutdinova, Anna and Nocek, Boguslaw and Brown, Greg and Xu, Xiaohui and Cui, Hong and Petit, Pierre and Flick, Robert and Zallot, Rémi and Balmant, Kelly and Ziemak, Michael J and Shanklin, John and De Crécy-Lagard, Valérie and Fiehn, Oliver and Gregory, Jesse F and Joachimiak, Andrzej and Savchenko, Alexei and Yakunin, Alexander F and Hanson, Andrew D and Argonne National Lab. (ANL), Argonne, IL (United States)
Nature Chemical Biology, ISSN 1552-4450, 08/2016, Volume 12, Issue 8, pp. 621 - 627
DUF89 family proteins occur widely in both prokaryotes and eukaryotes, but their functions are unknown. Here we define three DUF89 subfamilies (I, II, and... 
ACYL CARRIER PROTEIN | PANTOTHENATE KINASE | SUBSTRATE-SPECIFICITY | ENZYME | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DIRECTED-OVERFLOW | DNA-DAMAGE | COENZYME-A | PYROCOCCUS-FURIOSUS | Catalytic Domain | Phosphoric Monoester Hydrolases - genetics | Phosphoric Triester Hydrolases - genetics | Saccharomyces cerevisiae - genetics | Models, Molecular | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - metabolism | Metals - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Phosphoric Triester Hydrolases - metabolism | Phosphoric Triester Hydrolases - chemistry | Phosphoric Monoester Hydrolases - metabolism | Phosphoric Monoester Hydrolases - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Index Medicus | BASIC BIOLOGICAL SCIENCES
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