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Chemical Research in Toxicology, ISSN 0893-228X, 11/2018, Volume 31, Issue 11, pp. 1185 - 1194
Di(2-ethylhexyl) phthalate (DEHP) can cause severe environmental pollution. Effects of DEHP on cardiac metabolism have been reported, but its mechanism(s) of... 
CHEMISTRY, MEDICINAL | UCP-3 | CHEMISTRY, MULTIDISCIPLINARY | HEART | SKELETAL-MUSCLE | TRANSPORT | FATTY-ACID OXIDATION | DEHP | MITOCHONDRIAL THIOESTERASE-1 | KEGG | TOXICOLOGY | PROTEINS | EXPRESSION
Journal Article
Molecular Genetics and Metabolism, ISSN 1096-7192, 02/2016, Volume 117, Issue 2, pp. 210 - 216
Infantile neuronal ceroid lipofuscinosis (INCL, Infantile Batten disease) is an invariably fatal neurodegenerative pediatric disorder caused by an inherited... 
Palmitoyl protein thioesterase-1 | Enzyme replacement therapy | Lysosomal storage disorder | Batten disease | Histochemistry
Journal Article
ELIFE, ISSN 2050-084X, 04/2019, Volume 8
Protein palmitoylation and depalmitoylation alter protein function. This post-translational modification is critical for synaptic transmission and plasticity.... 
NR2B SUBTYPE RECEPTOR | EXPERIENCE-DEPENDENT PLASTICITY | VISUAL-CORTEX | LONG-TERM-POTENTIATION | BIOLOGY | PALMITOYL-PROTEIN THIOESTERASE-1 | CRITICAL-PERIOD | SUBUNIT COMPOSITION | D-ASPARTATE RECEPTOR | SRC-FAMILY KINASES | SYNAPTIC PLASTICITY
Journal Article
The American Journal of Human Genetics, ISSN 0002-9297, 05/2011, Volume 88, Issue 5, pp. 566 - 573
Journal Article
Acta Neuropathologica, ISSN 0001-6322, 4/2016, Volume 131, Issue 4, pp. 621 - 637
Journal Article
HUMAN MOLECULAR GENETICS, ISSN 0964-6906, 05/2008, Volume 17, Issue 10, pp. 1406 - 1417
Infantile neuronal ceroid lipofuscinosis (INCL) is a severe neurodegenerative disease caused by deficiency of palmitoyl protein thioesterase 1 (PPT1). INCL... 
EXTRACELLULAR ATP | ATP SYNTHASE | HDL ENDOCYTOSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOTHELIAL-CELLS | GENETICS & HEREDITY | PHOSPHOLIPID TRANSFER PROTEIN | BLOOD-BRAIN-BARRIER | MOLECULAR-BASIS | PALMITOYL-PROTEIN-THIOESTERASE-1 PPT1 | NEURONAL CEROID-LIPOFUSCINOSIS | APOLIPOPROTEIN-A-I
Journal Article
Journal Article
Science Signaling, ISSN 1945-0877, 01/2018, Volume 11, Issue 511, p. eaam8705
Asymmetric cell division results in two distinctly fated daughter cells. A molecular hallmark of asymmetric division is the unequal partitioning of cell fate... 
ACYL-PROTEIN THIOESTERASE-1 | IN-VITRO | CANCER GENOMICS | MAMMARY STEM | DAUGHTER CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | EMBRYONIC STEM-CELLS | SELF-RENEWAL | BETA-CATENIN | T-LYMPHOCYTE DIVISION | NUMB PROTEIN | CELL BIOLOGY | Asymmetric Cell Division - genetics | Lipoylation | Membrane Proteins - genetics | Receptors, Notch - metabolism | Humans | Receptors, Notch - genetics | cdc42 GTP-Binding Protein - metabolism | Nerve Tissue Proteins - genetics | beta Catenin - metabolism | beta Catenin - genetics | Nerve Tissue Proteins - metabolism | Point Mutation | Animals | Triple Negative Breast Neoplasms - genetics | cdc42 GTP-Binding Protein - genetics | Cell Line, Tumor | Female | Cell Membrane - metabolism | Membrane Proteins - metabolism | Thiolester Hydrolases - genetics | Thiolester Hydrolases - metabolism | Triple Negative Breast Neoplasms - enzymology | Wnt Signaling Pathway | Cdc42 protein | Wnt protein | Transcription | Palmitoylation | Catalytic activity | Metastases | Proteins | Heterogeneity | β-catenin | Signal transduction | Partitioning | Cell fate | Polarity | Catalysis | Localization | Cell division | Breast cancer | Gene expression | Embryos | Signaling | Asymmetry | Stem cells | Breast | Determinants | NUMB protein | Mutation | Position (location) | Cancer | Guanosinetriphosphatase | Tumors | Index Medicus
Journal Article
BMC Evolutionary Biology, ISSN 1471-2148, 03/2017, Volume 17, Issue 1, pp. 83 - 83
Background: Protein post-translational modifications (PTMs) change protein properties. Each PTM type is associated with domain families that apply the... 
Post-translational modifications | Gene duplications | Gene losses | Correlated evolution | Phylogenetic reconstruction | Tree reconciliation | LOCALIZATION | RAS | PHYLOGENETIC ANALYSIS | PROTEIN THIOESTERASE-1 | SACCHAROMYCES-CEREVISIAE | EVOLUTIONARY BIOLOGY | TREES | GENOMES | GENETICS & HEREDITY | ACYLTRANSFERASES | LIFE | TOOL | Gene Duplication | Phosphorylation | Lipoylation | Eukaryota - classification | Humans | Phylogeny | Biological Evolution | Proteins - genetics | Animals | Eukaryota - genetics | Proteins - metabolism | Protein Processing, Post-Translational | Evolution, Molecular | Regulations | Trafficking | Escherichia coli | Attachment | Biochemistry | Cell interactions | Proteins | Fungi | Degradation | Case studies | Eukaryotes | Conserved sequence | Control surfaces | Phylogenetics | Clusters | Acetylation | Catalysis | Bioinformatics | Anchoring | Enzymes | Topology | Nucleic acids | Digestion | Acyltransferase | Metabolism | Organelles | Fatty acids | Substrates | Membrane proteins | Deacetylation | Granules | Deacylation | Markov process | Phosphates | Biotechnology | Residues | Surgical implants | Cysteine | Membranes | Calcium | Lysosomes | Lipids | Genomes | Agglomeration | Kinases | Allosteric properties | E coli | Nutrient status | Compartments | Evolution | Mathematical models | Neuronal ceroid lipofuscinosis | Biodegradation | Calcium channels | Neurons | Zinc | Anchors | Acids | Position (location) | Potassium | Index Medicus
Journal Article
Journal Article
Expert Opinion on Orphan Drugs, ISSN 2167-8707, 06/2017, Volume 5, Issue 6, pp. 487 - 501
Introduction: Adult-onset neuronal ceroid lipofuscinoses (ANCL) are a group of rare inherited neurodegenerative diseases of early adulthood, named after the... 
ANCL diagnosis | treatment | NCL | Adult-onset neuronal ceroid lipofuscinosis | neuropathology | Parry disease | therapeutic strategies | STORAGE | DOMINANT INHERITANCE | MOUSE MODELS | CLN5 MUTATIONS | PALMITOYL PROTEIN THIOESTERASE-1 | EXTRACEREBRAL BIOPSIES | PHARMACOLOGY & PHARMACY | BATTEN-DISEASE | CATHEPSIN-F | TRANSMEMBRANE PROTEIN
Journal Article