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Journal Article
Journal of Neuroscience, ISSN 0270-6474, 03/2010, Volume 30, Issue 9, pp. 3184 - 3198
Increasing evidence suggests that phosphorylation may play an important role in the oligomerization, fibrillogenesis, Lewy body (LB) formation, and... 
BACKBONE DYNAMICS | MULTIPLE SYSTEM ATROPHY | INCLUSION FORMATION | BETA-SHEET | ALZHEIMERS-DISEASE | SERINE 129 | TAU-PHOSPHORYLATION | NEUROSCIENCES | LEWY BODIES | RAT MODEL | PARKINSONS-DISEASE | Phosphorylation | Rats, Wistar | Humans | Male | Brain - metabolism | Lewy Bodies - genetics | Lewy Body Disease - genetics | Protein Isoforms - metabolism | Multiple System Atrophy - metabolism | Cell Membrane - metabolism | Neurons - metabolism | Parkinson Disease - metabolism | Lewy Bodies - metabolism | Lewy Bodies - pathology | Disease Models, Animal | Alzheimer Disease - physiopathology | Rats | Mice, Transgenic | Neurodegenerative Diseases - genetics | Amino Acid Sequence - physiology | Multiple System Atrophy - genetics | Neurodegenerative Diseases - metabolism | Parkinson Disease - genetics | Parkinson Disease - physiopathology | Serine - metabolism | alpha-Synuclein - chemistry | Creatine Kinase - genetics | Lewy Body Disease - metabolism | Animals | Neurodegenerative Diseases - physiopathology | Alzheimer Disease - metabolism | Brain - pathology | Creatine Kinase - metabolism | Mice | Multiple System Atrophy - physiopathology | Alzheimer Disease - genetics | alpha-Synuclein - metabolism | Polymers - metabolism | Lewy Body Disease - physiopathology | Protein Isoforms - genetics | Index Medicus | serine 87 | phosphorylation | synucleinopathies | phosphomimics | Parkinson’s disease | α-synuclein
Journal Article
Journal Article
Journal Article
Cancer Letters, ISSN 0304-3835, 2016, Volume 383, Issue 2, pp. 261 - 271
Abstract Inactivation of p53 occurs frequently in various cancers. RITA is a promising anticancer small molecule that dissociates p53-MDM2 interaction,... 
Hematology, Oncology and Palliative Medicine | RITA | NF-κB RelA/p65 | ABCC6 | Chemoresistance | CANCER-CELLS | TRANSCRIPTION | DRUG-RESISTANCE | P53 FUNCTION | NEUROBLASTOMA-CELLS | NECK-CANCER | ONCOLOGY | SIGNALING PATHWAY | IN-VIVO | MULTIDRUG-RESISTANCE | NF-kappa B RelA/p65 | SMALL-MOLECULE RITA | Colonic Neoplasms - genetics | Phosphorylation | Apoptosis - drug effects | Drug Resistance, Multiple | Colonic Neoplasms - drug therapy | Furans - pharmacology | Humans | Serine | Drug Resistance, Neoplasm | Transcription Factor RelA - genetics | Colonic Neoplasms - metabolism | Breast Neoplasms - metabolism | Dose-Response Relationship, Drug | Transfection | MCF-7 Cells | RNA Interference | Time Factors | HEK293 Cells | Female | Multidrug Resistance-Associated Proteins - genetics | Antineoplastic Agents - pharmacology | HCT116 Cells | Breast Neoplasms - drug therapy | Xenograft Model Antitumor Assays | Animals | Breast Neoplasms - genetics | Signal Transduction - drug effects | Transcription Factor RelA - metabolism | Tumor Burden - drug effects | Breast Neoplasms - pathology | Mice, Nude | Colonic Neoplasms - pathology | Mutation | Multidrug Resistance-Associated Proteins - metabolism | p53 Protein | Xenotransplantation | Kinases | Drug resistance | Inactivation | Cancer therapies | Blockage | Anticancer properties | Proteins | Cell cycle | Xenografts | Conflicts of interest | Deoxyribonucleic acid--DNA | NF-κB protein | MDM2 protein | Deactivation | Gene expression | Sensitivity | Chemotherapy | Antitumor activity | RelA protein | Transporter | Cancer | Apoptosis | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 9, pp. 4374 - 4385
Although trace levels of phosphorylated alpha-synuclein (alpha-syn) are detectable in normal brains, nearly all alpha-syn accumulated within Lewy bodies in... 
MULTIPLE SYSTEM ATROPHY | INCLUSION FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISEASE-LINKED MUTATIONS | LEWY BODY DISEASE | MEDIATED PHOSPHORYLATION | SER-129 PHOSPHORYLATION | PARKINSONS-DISEASE | TRANSGENIC MICE | CELL-DEATH | OLIGODENDROGLIAL CELLS | Phosphorylation | Mesencephalon - cytology | Dopaminergic Neurons - pathology | Mesencephalon - metabolism | Humans | Synaptosomes - metabolism | Recombinant Fusion Proteins - metabolism | Dopaminergic Neurons - cytology | Endocytosis | Synaptosomes - pathology | Protein Aggregation, Pathological - pathology | Dopaminergic Neurons - metabolism | Parkinson Disease - metabolism | alpha-Synuclein - genetics | Protein Aggregation, Pathological - genetics | Protein-Serine-Threonine Kinases - metabolism | Mesencephalon - pathology | Animals, Newborn | Recombinant Proteins - metabolism | Cell Line | Parkinson Disease - pathology | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Parkinson Disease - genetics | Serine - metabolism | Protein Folding | alpha-Synuclein - chemistry | Animals | Recombinant Fusion Proteins - genetics | Mice | Protein Processing, Post-Translational | Mutation | alpha-Synuclein - metabolism | Protein Aggregation, Pathological - metabolism | Amino Acid Substitution | Index Medicus | post-translational modification (PTM) | Molecular Bases of Disease | fibril | protein misfolding | Parkinson disease | endocytosis | protein self-assembly | protein kinase | vesicles
Journal Article
Journal of Neurochemistry, ISSN 0022-3042, 09/2014, Volume 130, Issue 6, pp. 805 - 15
Journal Article
Journal Article
Journal Article