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1. Full Text Long-term memory deficits in Huntington's disease are associated with reduced CBP histone acetylase activity
by Giralt, A and Puigdellívol, M and Carretón, O and Paoletti, P and Valero, J and Parra-damas, A and Saura, C.A and Alberch, J and Ginés, S
Human Molecular Genetics, ISSN 0964-6906, 03/2012, Volume 21, Issue 6, pp. 1203 - 1216
Huntingtons disease (HD) is an autosomal dominant progressive neurodegenerative disorder caused by an expanded CAG/polyglutamine repeat in the coding region of... 
RUBINSTEIN-TAYBI-SYNDROME | C-FOS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOUSE MODEL | TRANSCRIPTION | GENETICS & HEREDITY | CREB-BINDING-PROTEIN | MICE | SYNAPTIC PLASTICITY | EXPRESSION | PRESYMPTOMATIC CARRIERS | COGNITIVE DEFICIT | Histone Acetyltransferases - deficiency | Immunoprecipitation | Humans | Huntington Disease - pathology | Male | Immunoenzyme Techniques | Behavior, Animal | Cognition Disorders - etiology | Genes, fos | Female | Acetylation | Huntington Disease - enzymology | Real-Time Polymerase Chain Reaction | Disease Models, Animal | Memory, Long-Term | Mice, Inbred C57BL | RNA, Messenger - genetics | Cognition Disorders - pathology | Hippocampus - pathology | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | CREB-Binding Protein - physiology | Hippocampus - metabolism | Animals | Maze Learning | Mice | Histone deacetylase | Animal models | Polyglutamine | Huntingtin | Neurodegenerative diseases | Transcription | Cognitive ability | Trinucleotide repeats | Cyclic AMP response element-binding protein | Huntington's disease | Hereditary diseases | CREB-binding protein | Coding | Long term memory | Trichostatin A | c-Fos protein | Hippocampus | Histone H3 | Movement disorders
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2. Full Text HBO1 Histone Acetylase Activity Is Essential for DNA Replication Licensing and Inhibited by Geminin
by Miotto, Benoit and Struhl, Kevin
Molecular Cell, ISSN 1097-2765, 2010, Volume 37, Issue 1, pp. 57 - 66
HBO1, an H4-specific histone acetylase, is a coactivator of the DNA replication licensing factor Cdt1. HBO1 acetylase activity is required for licensing,... 
PROTEINS | CELLCYCLE | DNA | ORIGIN ACTIVITY | COMPLEX | DROSOPHILA FOLLICLE CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | EUKARYOTIC CELLS | GENE-REGULATION | FACTOR CDT1 | S-PHASE | BINDING | PREVENTS REREPLICATION | ACETYLTRANSFERASE HBO1 | CELL BIOLOGY | Cell Cycle | Histone Acetyltransferases - antagonists & inhibitors | Histone Acetyltransferases - metabolism | Humans | Cell Cycle Proteins - metabolism | DNA Replication | Acetylation | Histones - metabolism | Geminin | Histone Acetyltransferases - physiology | Cell Cycle Proteins - physiology | Histones | DNA replication | DNA binding proteins | Life Sciences | origin licensing | Cdt1 | geminin | HBO1 | histone acetylation
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3. Full Text The histone acetylase PCAF is a nuclear receptor coactivator
by Blanco, Jorge C.G and Minucci, Saverio and Lu, Jianming and Yang, Xiang-Jiao and Walker, Kristen K and Chen, Hongwu and Evans, Ronald M and Nakatani, Yoshihiro and Ozato, Keiko
Genes and Development, ISSN 0890-9369, 06/1998, Volume 12, Issue 11, pp. 1638 - 1651
Whereas the histone acetylase PCAF has been suggested to be part of a coactivator complex mediating transcriptional activation by the nuclear hormone... 
Histone acetylation | Retinoids | PCAF | RXR | ILAR | Steroid receptors | GLUCOCORTICOID RECEPTOR | RAR | TRANSCRIPTIONAL ACTIVATION | DEPENDENT TRANSCRIPTION | RETINOID-X RECEPTOR | DEVELOPMENTAL BIOLOGY | steroid receptors | RESPONSE PATHWAYS | HORMONE RECEPTORS | ACID RECEPTORS | TATA-BINDING PROTEIN | GENETICS & HEREDITY | CO-REPRESSOR | CONSERVED REGION | histone acetylation | retinoids | Histones | Receptors | Genetic aspects | Research | Steroid hormones
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4. Full Text Altered Memory Capacities and Response to Stress in p300 CBP-Associated Factor (PCAF) Histone Acetylase Knockout Mice
by Maurice, Tangui and Duclot, Florian and Meunier, Johann and Naert, Gaëlle and Givalois, Laurent and Meffre, Julie and Célérier, Aurélie and Jacquet, Chantal and Copois, Virginie and Mechti, Nadir and Ozato, Keiko and Gongora, Céline
Neuropsychopharmacology, ISSN 0893-133X, 06/2008, Volume 33, Issue 7, pp. 1584 - 1602
Chromatin remodeling by posttranslational modification of histones plays an important role in brain plasticity, including memory, response to stress and... 
Age | Stress | Short-term memory | Histone acetylase PCAF | Spatial memory | stress | ACTIVATION | RUBINSTEIN-TAYBI-SYNDROME | PROTEIN | PSYCHIATRY | spatial memory | RETENTION | TRANSCRIPTIONAL COACTIVATORS P300 | MECHANISMS | short-term memory | NEUROSCIENCES | CBP | histone acetylase PCAF | PHARMACOLOGY & PHARMACY | RAT HIPPOCAMPUS | EXPRESSION | age | ACETYLTRANSFERASES | Memory Disorders - physiopathology | Age Factors | Memory Disorders - genetics | Male | Pattern Recognition, Visual - physiology | Behavior, Animal | Exploratory Behavior - physiology | Female | Corticosterone - blood | Disease Models, Animal | Emotions - physiology | Maze Learning - physiology | Conditioning (Psychology) - physiology | p300-CBP Transcription Factors - deficiency | Hippocampus - pathology | Avoidance Learning - physiology | Mice, Knockout | Stress, Psychological - pathology | Fear | Stress, Psychological - genetics | Animals | Analysis of Variance | Sex Factors | Mice | Memory - physiology | Stress, Psychological - physiopathology | Life Sciences | Neurons and Cognition | behavioral phenotyping
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5. Full Text Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration
by Rouaux, Caroline and Loeffler, Jean-Philippe and Boutillier, Anne-Laurence and Boutillier, Stephanie and Jokic, Natasa and Mbebi, Corinne
The EMBO Journal, ISSN 0261-4189, 12/2003, Volume 22, Issue 24, pp. 6537 - 6549
By altering chromatin structure, histone acetyltransferases (HATs) act as transcriptional regulators. We observed in a model of primary neurons that histone... 
CBP | neurodegeneration | apoptosis | caspase‐6 | HAT | Caspase-6 | Neurodegeneration | Apoptosis | caspase-6 | NEURONAL APOPTOSIS | RUBINSTEIN-TAYBI-SYNDROME | EMBRYONIC-DEVELOPMENT | CAM KINASE-IV | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMYOTROPHIC-LATERAL-SCLEROSIS | CELL APOPTOSIS | MICE LACKING | CELL BIOLOGY | CREB-BINDING PROTEIN | SIGNALING PATHWAY | SUPEROXIDE-DISMUTASE | p300-CBP Transcription Factors | Histone Acetyltransferases | Neurons - cytology | Cerebellum - enzymology | Acetyltransferases - genetics | Caspases - metabolism | Acetyltransferases - deficiency | Neurons - physiology | Cell Cycle Proteins - genetics | Caspase 6 | Recombinant Proteins - metabolism | Nerve Degeneration - enzymology | Caspases - genetics | Cell Survival | Cells, Cultured | Mice, Inbred Strains | Reverse Transcriptase Polymerase Chain Reaction | Nerve Degeneration - pathology | Hydrolysis | Histones - isolation & purification | Animals | Neurons - enzymology | Cerebellum - cytology | Cyclic AMP Response Element-Binding Protein - metabolism | Mice | Transcription Factors | Apoptosis - physiology | Histones - metabolism | Kinetics
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6. Full Text Efficient AuPd@GO-based electrochemical nanoprobe for sensitive detection of histone acetylase activity and its inhibitor
by Liu, Qiong and Yang, Linfei and She, Yuqi and Hu, Yufang
Analytical and Bioanalytical Chemistry, ISSN 1618-2642, 11/2019, Volume 411, Issue 27, pp. 7327 - 7336
Histone acetylase (HAT p300), which has aroused great concern in fundamental research and clinical applications, serves as one class of significant tumor... 
Biochemistry, general | Chemistry | Analytical Chemistry | Food Science | Monitoring/Environmental Analysis | Amperometric i-t curve | Graphene-assisted supported AuPd nanomaterial | Characterization and Evaluation of Materials | Electrochemical immunoassay | Inhibitor | Laboratory Medicine | Histone acetylase | Antigens | Immunoassay | Tumor markers | Intermetallic compounds | Therapeutic applications | Antibodies | Nanomaterials | Event-related potentials | Immunosensors | Sandwich structures | Electrical measurement | Corrosion inhibitors | Graphene | Electrochemistry | Histones | Acetylation | Biosensors | Commercialization
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7. Full Text HBO1 histone acetylase is a coactivator of the replication licensing factor Cdt1
by Miotto, Benoit and Struhl, Kevin
Genes and Development, ISSN 0890-9369, 10/2008, Volume 22, Issue 19, pp. 2633 - 2638
HBO1 histone acetylase is important for DNA replication licensing. In human cells, HBO1 associates with replication origins specifically during the G1 phase of... 
Dna replication | Cdt1 | Histone acetylation | Geminin | Origin licensing | HBO1 | REREPLICATION | DNA replication | TRANSCRIPTION | EUKARYOTIC CELLS | MECHANISMS | DEVELOPMENTAL BIOLOGY | DNA-REPLICATION | ACETYLTRANSFERASE HBO1 | CELL BIOLOGY | origin licensing | ORIGIN ACTIVITY | DROSOPHILA FOLLICLE CELLS | GENETICS & HEREDITY | BINDING | histone acetylation | Cell Line | Humans | RNA, Messenger - genetics | Cell Cycle Proteins - metabolism | Enzyme Stability | Histone Acetyltransferases - genetics | DNA Replication | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | RNA, Messenger - metabolism | DNA-Binding Proteins - metabolism | G1 Phase | Animals | Replication Origin | Histone Acetyltransferases - metabolism | Cell Cycle Proteins - genetics | Mice | HeLa Cells | Binding Sites | Histones | Chemical properties | Genetic transcription | Genetic regulation | Analysis | Life Sciences | Research Communication
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8. Full Text The role dietary of bioactive compounds on the regulation of histone acetylases and deacetylases: A review
by Vahid, F and Zand, H and Nosrat–Mirshekarlou, E and Najafi, R and Hekmatdoost, A
Gene, ISSN 0378-1119, 05/2015, Volume 562, Issue 1, pp. 8 - 15
Nutrigenomics is an area of epigenomics that explores and defines the rapidly evolving field of diet-genome interactions. Lifestyle and diet can significantly... 
Epigenetics | Histones acetyltransferase | Histone deacetylase | Dietary bioactive compounds | MATERNAL DIET | HIGH-FAT-DIET | CURCUMIN | TUMOR VIRUS PROMOTER | CELL-CYCLE ARREST | CANCER | PROINFLAMMATORY CYTOKINE | INHIBITION | C-MYC GENE | SODIUM-BUTYRATE | GENETICS & HEREDITY | Chromatin - metabolism | Histone Deacetylases - genetics | Signal Transduction | Epigenesis, Genetic | Humans | Histone Acetyltransferases - genetics | Histone Deacetylases - metabolism | Stilbenes - pharmacology | DNA Methylation | Histones - genetics | Diet | Protein Processing, Post-Translational - drug effects | Histone Acetyltransferases - metabolism | Genomic Instability - drug effects | Indoles - pharmacology | Flavonoids - pharmacology | Histones - metabolism | Genome, Human | Chromatin - drug effects | Chromatin - genetics | Epigenetic inheritance | RNA | Transferases | Genomics | Resveratrol | Histones | Cellular signal transduction
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9. Full Text Mutations truncating the EP300 acetylase in human cancers
by Daigo, Yataro and Kouzarides, Tony and Batley, Sarah J and Bannister, Andy and Russell, Paul and Sowter, Heidi M and Gayther, Simon A and Delhanty, Joy D.A and Chin, Suet-Feung and Thorpe, Karen and Caldas, Carlos and Wilson, Annie and Linger, Lori and Ponder, Bruce A.J
Nature Genetics, ISSN 1061-4036, 03/2000, Volume 24, Issue 3, pp. 300 - 303
The EP300 protein is a histone acetyltransferase that regulates transcription via chromatin remodelling and is important in the processes of cell proliferation... 
E1A-ASSOCIATED PROTEIN P300 | CBP | GENE | GENETICS & HEREDITY | COACTIVATORS P300 | BINDING | P53 | FAMILY | Sequence Deletion | Histone Acetyltransferases | Colorectal Neoplasms - genetics | Genes | Humans | Ovarian Neoplasms - pathology | Male | Acetyltransferases - genetics | Ovarian Neoplasms - genetics | Neoplasms - genetics | DNA Mutational Analysis | Female | Codon - genetics | Tumor Cells, Cultured | Carcinoma - pathology | Neoplasm Proteins - genetics | Genes, Tumor Suppressor | Neoplasms - enzymology | Terminator Regions, Genetic | Point Mutation | Breast Neoplasms - genetics | Breast Neoplasms - pathology | Saccharomyces cerevisiae Proteins | Carcinoma - genetics | DNA, Neoplasm - genetics | Mutation | Colorectal Neoplasms - pathology | Physiological aspects | Genetic aspects | Research | Gene mutations | DNA damage | Cancer | EP300 gene | TP53 protein | EP300 protein
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10. Full Text Exendin-4 increases histone acetylase activity and reverses epigenetic modifications that silence Pdx1 in the intrauterine growth retarded rat
by Pinney, S E and Jaeckle Santos, L J and Han, Y and Stoffers, D A and Simmons, R A
Diabetologia, ISSN 0012-186X, 10/2011, Volume 54, Issue 10, pp. 2606 - 2614
The abnormal intrauterine milieu of intrauterine growth retardation (IUGR) permanently alters gene expression and function of pancreatic beta cells leading to... 
Intrauterine growth retardation | Medicine & Public Health | Human Physiology | Metabolic Diseases | Beta cell | Epigenetics | Pdx1 | Internal Medicine | Histone | Exendin-4 | PANCREAS DEVELOPMENT | BETA-CELLS | CELL-PROLIFERATION | DNA-BINDING ACTIVITY | GLUCAGON-LIKE PEPTIDE-1 | INSULIN-RESISTANCE | LYSINE METHYLATION | ENDOCRINOLOGY & METABOLISM | H3 ACETYLATION | TRANSCRIPTION FACTOR | EXPRESSION | Animals, Newborn | Upstream Stimulatory Factors - genetics | Homeodomain Proteins - metabolism | Histone Acetyltransferases - genetics | Rats | DNA Methylation - genetics | Fetal Growth Retardation - metabolism | Promoter Regions, Genetic - genetics | Homeodomain Proteins - genetics | Animals | Chromatin Immunoprecipitation | Epigenesis, Genetic - genetics | Upstream Stimulatory Factors - metabolism | Histone Acetyltransferases - metabolism | Trans-Activators - genetics | Venoms - therapeutic use | CpG Islands - genetics | Trans-Activators - metabolism | Epigenesis, Genetic - drug effects | DNA Methylation - drug effects | Peptides - therapeutic use | Medical colleges | Chromatin | Pancreatic beta cells | Promoters (Genetics) | Peptides | Methyltransferases | Growth | DNA | Physiological aspects | Diabetes | Methylation | Gene expression | Transferases | Resveratrol | Genetic transcription
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11. Full Text Involvement of the TIP60 Histone Acetylase Complex in DNA Repair and Apoptosis
by Ikura, Tsuyoshi and Ogryzko, Vasily V and Grigoriev, Mikhail and Groisman, Regina and Wang, Jin and Horikoshi, Masami and Scully, Ralph and Qin, Jun and Nakatani, Yoshihiro
Cell, ISSN 0092-8674, 2000, Volume 102, Issue 4, pp. 463 - 473
It is well known that histone acetylases are important chromatin modifiers and that they play a central role in chromatin transcription. Here, we present... 
COACTIVATOR | STRAND BREAK REPAIR | CHROMATIN | GCN5-RELATED N-ACETYLTRANSFERASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SWI/SNF | COMPONENTS | SUPERFAMILY | RUVB-LIKE PROTEIN | COENZYME-A | CELL BIOLOGY | Proteins - physiology | Acetyltransferases - metabolism | Histone Acetyltransferases | Molecular Weight | Apoptosis - radiation effects | Electrophoresis, Polyacrylamide Gel | Humans | Bacterial Proteins - chemistry | Adenosine Triphosphatases - metabolism | DNA - metabolism | Macromolecular Substances | DNA Helicases - metabolism | DNA Repair | Saccharomyces cerevisiae Proteins | Actins - chemistry | Adenosine Triphosphatases - chemistry | Apoptosis - physiology | HeLa Cells | Proteins - chemistry | Lysine Acetyltransferase 5 | Enzymes | Chromatin | Cell death | Structure-activity relationship | Histones | Physiological aspects | DNA repair
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12. Full Text Histone Acetylase Inhibitor Curcumin Impairs Mouse Spermiogenesis-An In Vitro Study
by Xia, Xiaoyu and Cai, Heng and Qin, Shixiao and Xu, Chen
PLoS ONE, ISSN 1932-6203, 11/2012, Volume 7, Issue 11, p. e48673
In the previous study, we unraveled the unique "erasure strategy'' during the mouse spermiogenesis. Chromatin associated proteins sequentially disassociated... 
NANOPARTICLES | SPERM | MULTIDISCIPLINARY SCIENCES | EMBRYONIC STEM-CELLS | SPERMATOGENIC CELLS | MICE | TRANSCRIPTION PROGRAM | PROTEINS | TRICHOSTATIN-A | RAT TESTIS | ACETYLTRANSFERASE | Cell Line | Spermatids - metabolism | Spermatogenesis - drug effects | Apoptosis - drug effects | Curcumin - pharmacology | Male | Down-Regulation - drug effects | RNA, Messenger - metabolism | Spermatids - pathology | Acetylation - drug effects | Animals | Histone Acetyltransferases - antagonists & inhibitors | Spermatids - drug effects | Mice | Histones - metabolism | Chromatin | Reproductive health | Spermiogenesis | Laboratories | Toxicity | Sperm | Spermatids | Histology | Kinases | Gene expression | Proteins | Medicine | Transcription termination | Embryology | Inhibitors | Rodents | Morphology | Epigenetics | Curcumin | Acetylation | Drug dosages | Elongation | Apoptosis
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