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Nature, ISSN 0028-0836, 07/2016, Volume 535, Issue 7610, pp. 111 - 116
Journal Article
Nature, ISSN 0028-0836, 09/2015, Volume 525, Issue 7568, pp. 265 - 268
Phytosulfokine (PSK) is a disulfated pentapeptide that has a ubiquitous role in plant growth and development(1,2). PSK is perceived by its receptor PSKR3,4, a... 
STRUCTURAL INSIGHT | CELLS | PERCEPTION | IMMUNITY | MULTIDISCIPLINARY SCIENCES | PROLIFERATION | GROWTH-FACTOR | ARABIDOPSIS | BAK1 | SOFTWARE | KINASES | Protein Kinases - metabolism | Peptide Hormones - pharmacology | Protein Kinases - chemistry | Substrate Specificity | Crystallography, X-Ray | Arabidopsis Proteins - metabolism | Peptide Hormones - metabolism | Plant Growth Regulators - chemistry | Plant Proteins - chemistry | Peptide Hormones - chemistry | Receptors, Cell Surface - chemistry | Plant Proteins - metabolism | Protein Stability | Protein-Serine-Threonine Kinases - metabolism | Allosteric Regulation - drug effects | Arabidopsis Proteins - agonists | Arabidopsis Proteins - genetics | Arabidopsis - chemistry | Plant Proteins - pharmacology | Receptors, Cell Surface - agonists | Models, Molecular | Receptors, Cell Surface - metabolism | Mutation - genetics | Arabidopsis Proteins - chemistry | Protein Structure, Secondary - drug effects | Protein Binding | Protein-Serine-Threonine Kinases - chemistry | Plant Growth Regulators - metabolism | Plant Growth Regulators - pharmacology | Protein Multimerization - drug effects | Protein Structure, Tertiary - drug effects | Receptors, Cell Surface - genetics | Chorionic gonadotropin | Cholecystokinin | Research | Plant physiology | Health aspects | Hydrogen bonds | Peptides | Plant growth | Ligands | Mutation | Flowers & plants | Kinases
Journal Article
Blood, ISSN 0006-4971, 03/2011, Volume 117, Issue 12, pp. 3286 - 3293
We examined in vivo FLT3 inhibition in acute myeloid leukemia patients treated with chemotherapy followed by the FLT3 inhibitor lestaurtinib, comparing newly... 
YOUNGER PATIENTS | CELLS | CONSOLIDATION | ACTIVATION | SERUM-LEVELS | TYROSINE KINASE INHIBITOR | ACUTE MYELOID-LEUKEMIA | MUTATIONS | CYTARABINE | HEMATOLOGY | CHEMOTHERAPY | Niacinamide - analogs & derivatives | fms-Like Tyrosine Kinase 3 - antagonists & inhibitors | Humans | Staurosporine - analogs & derivatives | Antineoplastic Agents - therapeutic use | Benzenesulfonates - therapeutic use | Membrane Proteins - pharmacology | Phenylurea Compounds | Benzenesulfonates - pharmacology | Multicenter Studies as Topic | Protein Kinase Inhibitors - antagonists & inhibitors | Membrane Proteins - physiology | Inhibitory Concentration 50 | Leukemia, Myeloid, Acute - drug therapy | Antineoplastic Agents - pharmacology | Membrane Proteins - metabolism | Membrane Proteins - blood | Pyridines - therapeutic use | Antineoplastic Agents - antagonists & inhibitors | Leukemia, Myeloid, Acute - pathology | Cells, Cultured | Treatment Outcome | Leukemia, Myeloid, Acute - blood | Piperazines - therapeutic use | Piperazines - pharmacology | Randomized Controlled Trials as Topic | Indazoles - pharmacology | Drug Antagonism | Protein Kinase Inhibitors - therapeutic use | Staurosporine - therapeutic use | Carbazoles - therapeutic use | Protein Kinase Inhibitors - pharmacology | Pyridines - pharmacology | Carbazoles - pharmacology | Indazoles - therapeutic use | Staurosporine - pharmacology | Clinical Trials and Observations
Journal Article
Nature, ISSN 0028-0836, 07/2016, Volume 535, Issue 7610, pp. 153 - 158
Inflammatory caspases (caspases 1, 4, 5 and 11) are activated in response to microbial infection and danger signals. When activated, they cleave mouse and... 
LISTERIA-MONOCYTOGENES | INTERLEUKIN-1-BETA | MULTIDISCIPLINARY SCIENCES | MIXED LINEAGE KINASE | PERFORIN | NLRP3 INFLAMMASOME | INTRACELLULAR BACTERIA | GRANZYMES | CASPASE-1 ACTIVATION | GRANULYSIN | CELL-DEATH | Conserved Sequence - genetics | Inflammasomes - metabolism | Phosphatidylinositol Phosphates - metabolism | Pyroptosis - drug effects | Escherichia coli - drug effects | Humans | Molecular Sequence Data | Neoplasm Proteins - pharmacology | Escherichia coli - cytology | Neoplasm Proteins - metabolism | Escherichia coli - metabolism | Protein Multimerization - genetics | Listeria monocytogenes - metabolism | Cell Membrane - metabolism | Membrane Proteins - metabolism | Listeria monocytogenes - cytology | Porosity - drug effects | Neoplasm Proteins - genetics | Cell Membrane - drug effects | Staphylococcus aureus - metabolism | Amino Acid Sequence | Cell Line | Microbial Viability - drug effects | Membrane Proteins - genetics | Mice, Inbred C57BL | Phosphatidylserines - metabolism | Neoplasm Proteins - chemistry | Cardiolipins - metabolism | Cell Membrane - ultrastructure | Protein Structure, Tertiary - genetics | Microscopy, Electron | Pyroptosis - genetics | Protein Transport | Liposomes - chemistry | Animals | Membrane Proteins - chemistry | Cell Membrane Permeability - drug effects | Staphylococcus aureus - cytology | Liposomes - metabolism | Mice | Mutation | Staphylococcus aureus - drug effects | Listeria monocytogenes - drug effects | Observations | Apoptosis | Proteins | Membranes | Bacterial infections | Immunology | Plasmids | Bacteria | Infections | Cells
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2010, Volume 107, Issue 30, pp. 13473 - 13478
Staphylococcus aureus α-hemolysin (Hla), a potent cytotoxin, plays an important role in the pathogenesis of staphylococcal diseases, including those caused by... 
Receptors | Epithelial cells | Cell lines | Erythrocytes | Small interfering RNA | Cytotoxicity | Toxins | Cell membranes | Focal adhesions | Staphylococcus aureus | Cellular receptor | Pore-forming cytotoxin | CELLS | INFECTIONS | TYROSINE PHOSPHORYLATION | PROTECTION | pore-forming cytotoxin | TOXIN | MULTIDISCIPLINARY SCIENCES | P130(CAS) | MURINE MODEL | ERYTHROCYTES | PORE | BINDING | cellular receptor | Amyloid Precursor Protein Secretases - genetics | Epithelial Cells - metabolism | Hemolysin Proteins - pharmacology | Staphylococcus aureus - physiology | Hemolysin Proteins - genetics | Humans | Focal Adhesions | Molecular Sequence Data | Immunoblotting | RNA Interference | Membrane Proteins - metabolism | Staphylococcus aureus - metabolism | Staphylococcus aureus - genetics | Amino Acid Sequence | Cell Line | Cell Survival - drug effects | Rabbits | Membrane Proteins - genetics | Electrophoresis, Polyacrylamide Gel | Bacterial Proteins - genetics | ADAM10 Protein | Epithelial Cells - pathology | Host-Pathogen Interactions | Integrin beta1 - metabolism | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Bacterial Proteins - pharmacology | Animals | Epithelial Cells - microbiology | Erythrocytes - metabolism | Cell Line, Tumor | Protein Binding | Bacterial Proteins - metabolism | Mutation | ADAM Proteins - genetics | Integrin beta1 - genetics | Hemolysin Proteins - metabolism | Biological Sciences
Journal Article
Journal Article
Journal Article
Nature, ISSN 0028-0836, 10/2015, Volume 526, Issue 7572, pp. 218 - 223
HIV-1 Nef and the unrelated mouse leukaemia virus glycosylated Gag (glycoGag) strongly enhance the infectivity of HIV-1 virions produced in certain cell types... 
CYTOPLASMIC DOMAIN | CELL-SURFACE CD4 | GLYCOSYLATED-GAG | VIRION FUSION | REPLICATION | PRIMARY T-LYMPHOCYTES | MULTIDISCIPLINARY SCIENCES | IMMUNODEFICIENCY-VIRUS TYPE-1 | CD4 DOWN-REGULATION | MURINE LEUKEMIA-VIRUS | OPTIMAL VIRAL INFECTIVITY | Humans | Neoplasm Proteins - antagonists & inhibitors | Neoplasm Proteins - pharmacology | Virion - chemistry | Host-Pathogen Interactions - drug effects | Membrane Proteins - pharmacology | Neoplasm Proteins - metabolism | Receptors, Cell Surface - antagonists & inhibitors | Membrane Proteins - deficiency | HIV-1 - growth & development | HIV-1 - physiology | HIV-1 - chemistry | Gene Deletion | nef Gene Products, Human Immunodeficiency Virus - metabolism | Membrane Proteins - metabolism | Cell Line | Virus Replication - drug effects | nef Gene Products, Human Immunodeficiency Virus - deficiency | HIV-1 - drug effects | Down-Regulation | HIV Infections - virology | Virion - physiology | CD4-Positive T-Lymphocytes - metabolism | Receptors, Cell Surface - metabolism | Gene Products, gag - metabolism | Protein Transport | Virion - drug effects | Membrane Proteins - antagonists & inhibitors | Receptors, Cell Surface - deficiency | HIV Infections - drug therapy | Neoplasm Proteins - deficiency | Virion - growth & development | Leukemia Virus, Murine - chemistry | Development and progression | Genetic aspects | Virulence (Microbiology) | Viral proteins | Properties | HIV infection | Proteins | Genomes | Immunology | Mutation | Human immunodeficiency virus--HIV | Cells
Journal Article
Nature Neuroscience, ISSN 1097-6256, 10/2009, Volume 12, Issue 10, pp. 1248 - 1256
Neural stem cells (NSCs) are controlled by diffusible factors. The transcription factor Sox2 is expressed by NSCs and Sox2 mutations in humans cause defects in... 
SOX2 | ADULT-MOUSE BRAIN | IN-VIVO | SELF-RENEWAL | MICE | PLURIPOTENCY | SUBVENTRICULAR ZONE | MUTATIONS | EXPRESSION | NEUROSCIENCES | SONIC-HEDGEHOG | Nestin | Age Factors | Embryo, Mammalian | SOXB1 Transcription Factors - deficiency | Gene Expression Regulation, Developmental - genetics | Culture Media, Conditioned - pharmacology | Green Fluorescent Proteins - genetics | Hedgehog Proteins - physiology | RNA, Messenger - metabolism | Wnt Proteins - metabolism | Glial Fibrillary Acidic Protein | Neurogenesis - genetics | Wnt Proteins - genetics | Intermediate Filament Proteins - genetics | Neurons - physiology | Chromatin Immunoprecipitation - methods | Female | SOXB1 Transcription Factors - physiology | Bromodeoxyuridine - metabolism | Cell Differentiation - physiology | Hippocampus - growth & development | Gene Expression Regulation, Developmental - physiology | Animals, Newborn | Hippocampus - embryology | Cell Survival | Mice, Inbred C57BL | Cells, Cultured | Enzyme Inhibitors - pharmacology | Mice, Transgenic | In Situ Nick-End Labeling - methods | Signal Transduction - genetics | Hedgehog Proteins - antagonists & inhibitors | Hippocampus - cytology | Mutation - genetics | Nerve Tissue Proteins - genetics | Embryonic Stem Cells - physiology | Nerve Tissue Proteins - metabolism | Electrophoretic Mobility Shift Assay - methods | Animals | Signal Transduction - drug effects | Cell Differentiation - drug effects | Intercellular Signaling Peptides and Proteins - pharmacology | Wnt3 Protein | Mice | Wnt3A Protein | DNA Nucleotidyltransferases - genetics | Transcription factors | Gene mutations | Stem cells | Physiological aspects | Genetic aspects | Hippocampus (Brain) | Research | Health aspects
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 9/2005, Volume 170, Issue 7, pp. 1067 - 1078
Mutations in GDAP1 lead to severe forms of the peripheral motor and sensory neuropathy, Charcot-Marie-Tooth disease (CMT), which is characterized by... 
COS cells | Mitochondria | Transfection | Neurons | Charcot Marie Tooth disease | Schwann cells | HeLa cells | Genetic mutation | Peripheral nervous system diseases | Cells | OUTER-MEMBRANE | FUSION | NEUROPATHY | SCHWANN-CELLS | FISSION | GDAP1 GENE | MAMMALIAN-CELLS | DYNAMIN-RELATED PROTEIN | ETHACRYNIC-ACID | AUTOSOMAL RECESSIVE CMT | CELL BIOLOGY | Humans | Nerve Tissue Proteins - analysis | Microtubule-Associated Proteins - pharmacology | Neurons - cytology | Schwann Cells - cytology | Charcot-Marie-Tooth Disease - genetics | Mitochondrial Membrane Transport Proteins - genetics | Mitochondrial Membrane Transport Proteins - physiology | Mitochondrial Proteins - metabolism | Membrane Transport Proteins - metabolism | Membrane Proteins - metabolism | Neurons - metabolism | Mitochondria - chemistry | Charcot-Marie-Tooth Disease - metabolism | Nerve Tissue Proteins - physiology | Cells, Cultured | Gene Expression Regulation | Rats | Schwann Cells - metabolism | Mitochondria - pathology | Intracellular Membranes - chemistry | Nerve Tissue Proteins - genetics | Mitochondrial Proteins - pharmacology | Animals | Charcot-Marie-Tooth Disease - etiology | GTP Phosphohydrolases - metabolism | Models, Biological | Mice | Mutation | Mitochondria - physiology | GTP Phosphohydrolases - pharmacology | Proteins | Care and treatment | Research | Gangliosides | Charcot-Marie-Tooth disease
Journal Article
Brain Research, ISSN 0006-8993, 05/2006, Volume 1089, Issue 1, pp. 67 - 78
Small heat shock proteins Hsp20 and HspB2/B3 co-localize with Aβ deposition in senile plaques and cerebral amyloid angiopathy in Alzheimer's disease brains,... 
Cerebrovascular amyloid | Amyloid-β protein | Small heat shock protein | Alzheimer's disease | Fibrillization | HSPB8 | ALPHA-B-CRYSTALLIN | ALZHEIMERS-DISEASE BRAINS | CHAPERONE | NEUROSCIENCES | VESSEL WALL | HUMAN BRAIN PERICYTES | fibrillization | IN-VITRO | small heat shock protein | A-BETA | amyloid-beta protein | SMOOTH-MUSCLE-CELLS | cerebrovascular amyloid | EXPRESSION | Protein Binding - genetics | Humans | Neoplasm Proteins - pharmacology | Cerebral Amyloid Angiopathy - metabolism | Neoplasm Proteins - metabolism | alpha-Crystallins - metabolism | HSP20 Heat-Shock Proteins - metabolism | Neuroprotective Agents - metabolism | HSP20 Heat-Shock Proteins - pharmacology | Neuroprotective Agents - pharmacology | Amyloid beta-Peptides - genetics | Amyloid beta-Peptides - metabolism | Peptide Fragments - genetics | Alzheimer Disease - physiopathology | Peptide Fragments - metabolism | Plaque, Amyloid - pathology | Cerebral Amyloid Angiopathy - physiopathology | Heat-Shock Proteins - metabolism | Cells, Cultured | Cerebral Arteries - physiopathology | Heat-Shock Proteins - pharmacology | Mutation - genetics | Amyloid beta-Peptides - antagonists & inhibitors | alpha-Crystallins - pharmacology | Cerebral Arteries - metabolism | Peptide Fragments - antagonists & inhibitors | Alzheimer Disease - metabolism | Plaque, Amyloid - metabolism | Amyloid beta-Peptides - chemistry | HSP27 Heat-Shock Proteins
Journal Article