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2005, ISBN 1588830276, xxv, 319
Book
IEEE reviews in biomedical engineering, ISSN 1941-1189, 2016, Volume 9, pp. 234 - 263
Journal Article
Journal Article
Current Opinion in Cell Biology, ISSN 0955-0674, 2016, Volume 40, pp. 32 - 40
Journal Article
Molecular cell, ISSN 1097-2765, 2017, Volume 66, Issue 5, pp. 684 - 697.e9
... α5 binding and nuclear translocation. In the nucleus, ACSS2 binds to transcription factor EB and translocates to lysosomal and autophagy gene promoter regions, where ACSS2 incorporates acetate generated from histone acetylation turnover... 
ACSS2 | lysosomal biogenesis | autophagy | TFEB | nucleus | AMPK | acetyl-CoA | tumor development | COENZYME-A-SYNTHETASE | ACTIVATION | ACETYL-COA | METABOLISM | PHOSPHORYLATION | PROTEIN-KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-GROWTH | BETA-CATENIN | ACETATE | HISTONE ACETYLATION | CELL BIOLOGY | alpha Karyopherins - metabolism | AMP-Activated Protein Kinases - metabolism | Glioblastoma - enzymology | Phosphorylation | Humans | Brain Neoplasms - pathology | Gene Expression Regulation, Neoplastic | Stress, Physiological | Male | Autophagy | Cell Nucleus - enzymology | Organelle Biogenesis | Lysosomes - metabolism | Transfection | Glioblastoma - genetics | RNA Interference | Acetate-CoA Ligase - genetics | Cell Nucleus - pathology | Transcription, Genetic | Acetylation | Active Transport, Cell Nucleus | Binding Sites | Promoter Regions, Genetic | Brain Neoplasms - enzymology | Cell Survival | Brain Neoplasms - genetics | Acetyl Coenzyme A - metabolism | Animals | Energy Metabolism | Acetate-CoA Ligase - metabolism | Mice, Nude | Glioblastoma - pathology | Basic Helix-Loop-Helix Leucine Zipper Transcription Factors - genetics | alpha Karyopherins - genetics | Cell Line, Tumor | Protein Binding | Basic Helix-Loop-Helix Leucine Zipper Transcription Factors - metabolism | Mice, Inbred BALB C | Protein Processing, Post-Translational | Histones - metabolism | Medical colleges | Thiols | Brain tumors | Genes | Genetic transcription | Glucose | Dextrose | Gliomas | Ligases | Stem cells | Medical genetics | Genetic aspects | Protein kinases | Resveratrol | Development and progression
Journal Article
Journal of cellular and molecular medicine, ISSN 1582-1838, 2017, Volume 21, Issue 7, pp. 1373 - 1387
...; however, the molecular mechanisms that drive IL‐1β production in the intervertebral disc, especially in nucleus pulposus (NP) cells, are unknown... 
intervertebral disc degeneration | IL‐1β | calcium | human nucleus pulposus cells | mitochondrial damage | NLRP3 inflammasome | advanced glycation end products | IL-1β | MEDICINE, RESEARCH & EXPERIMENTAL | PERMEABILITY TRANSITION PORE | IL-1 | NLRP3 INFLAMMASOME ACTIVATION | MITOCHONDRIA | LUMBAR INTERVERTEBRAL DISC | RECEPTOR | DEGENERATION | CELL BIOLOGY | TOLL-LIKE | PATTERN | ROLES | EXPRESSION | Inflammation - pathology | Inflammasomes - metabolism | Reactive Oxygen Species - metabolism | Scoliosis - genetics | Humans | Interleukin-1beta - genetics | Scoliosis - pathology | Intervertebral Disc Degeneration - metabolism | Intervertebral Disc Degeneration - pathology | NLR Family, Pyrin Domain-Containing 3 Protein - genetics | Interleukin-1beta - metabolism | Antigens, Neoplasm - metabolism | Low Back Pain - genetics | Low Back Pain - pathology | Glycation End Products, Advanced - genetics | Intervertebral Disc Degeneration - genetics | Antigens, Neoplasm - genetics | Nucleus Pulposus - metabolism | Oxidative Stress - genetics | Nucleus Pulposus - pathology | Mitochondria - metabolism | Mitochondria - pathology | Inflammasomes - genetics | Glycation End Products, Advanced - metabolism | Inflammation - genetics | Mitogen-Activated Protein Kinases - genetics | Mitogen-Activated Protein Kinases - metabolism | Oxidative stress | Back pain | Reactive oxygen species | Calcium | Mitochondrial permeability transition pore | Membrane permeability | Disorders | Inflammatory response | Activation | Nucleus pulposus | Intervertebral discs | Tissues | Calcium signalling | Pain | Scoliosis | Bioaccumulation | Interleukin 1 | Back | Aging | Degeneration | Damage | Assembly | Age | Activation analysis | Advanced glycosylation end products | Diabetes mellitus | Glycosylation | Permeability | Patients | Calcium permeability | Molecular modelling | Neurological complications | Nuclei (cytology) | MPTP | Immunofluorescence | In vitro methods and tests | Original
Journal Article
International journal of molecular sciences, ISSN 1422-0067, 2018, Volume 19, Issue 9, p. 2820
...-phosphotyrosine interaction, concentrated in the nucleus to regulate the expression of target genes [3]. The ubiquitously expressed STAT3 family member is canonically... 
Nucleus | Post-translational modifications | STAT3 | Mitochondrial associated membranes (MAMs) | Endoplasmic reticulum | Apoptosis | Cancer | mitochondrial associated membranes (MAMs) | OXIDATIVE STRESS | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | nucleus | apoptosis | SERINE PHOSPHORYLATION | CELL-SURVIVAL | CHEMISTRY, MULTIDISCIPLINARY | NEGATIVE REGULATOR | GENE-EXPRESSION | cancer | ENDOPLASMIC-RETICULUM | post-translational modifications | TRANSCRIPTION FACTOR | endoplasmic reticulum | SIGNAL TRANSDUCER | Neoplasms - metabolism | Endoplasmic Reticulum - genetics | Humans | Endoplasmic Reticulum - metabolism | STAT3 Transcription Factor - analysis | Mitochondria - metabolism | Mitochondria - pathology | Endoplasmic Reticulum - pathology | Animals | Cell Nucleus - metabolism | Cell Nucleus - genetics | Energy Metabolism | Mitochondria - genetics | Neoplasms - genetics | Cell Nucleus - pathology | Protein Processing, Post-Translational | Neoplasms - pathology | Oncogenes | STAT3 Transcription Factor - genetics | STAT3 Transcription Factor - metabolism | Tyrosine | Phosphorylation | Physiological effects | Transformation | Cytokines | Serine | Stat3 protein | Homeostasis | Energy balance | Mitochondria | Isoforms | Post-translation | Tumor suppressor genes | Physiology | Oxidation | Acetylation | Methylation | Growth factors | Calcium homeostasis | Tumors | Kinases | Phosphatase | Proteins | Cell growth | Epidermal growth factor | Rodents | Localization | Permeability | Stem cells | Regulation | Mutation | Binding sites | mitochondrial associated membranes (MAMs), nucleus
Journal Article