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1. Full Text X‐ray structure of the AAC(6′)‐Ii antibiotic resistance enzyme at 1.8 Å resolution; examination of oligomeric arrangements in GNAT superfamily members
by Burk, David L and Ghuman, Navleen and Wybenga‐Groot, Leanne E and Berghuis, Albert M
Protein science, ISSN 0961-8368, 03/2003, Volume 12, Issue 3, pp. 426 - 437
AAC‐Ia, aminoglycoside 3‐acetyltransferase type Ia | Aminoglycoside acetyltransferase | N‐acetyltransferase | AAC, aminoglycoside acetyltransferase | tGCN5, Tetramymena thermophila | dimerization | RMSD, root‐mean‐square deviation | yGCN5, yeast GCN5 transcriptional activator | CoA, coenzyme A | GNAT, GCN5‐related N‐acetyltransferase | GNA1, Saccharomyces cerevisiae GCN5‐related N‐acetyltransferase | yHPA2, yeast histone acetyltransferase HPA2 | AcCoA, acetyl coenzyme A | cNMT, Candida albicans N‐myristoyl transferase | GCN5, histone acetyltransferase domain | antibiotic resistance | X‐ray crystallography | AAC(6′)‐Ii, aminoglycoside 6′‐acetyltransferase type Ii | hPCAF, human histone acetyltransferase domain of P300/CBP associating factor | AAC(2′)‐Ic, aminoglycoside 2′‐acetyltransferase type Ic | AANAT, serotonin N‐acetyltransferase (arylalkylamine N‐acetyltransferase) | yNMT, yeast N‐myristoyl transferase | yHAT1, yeast histone acetyltransferase HAT1 | X-ray crystallography | Dimerization | N-acetyltransferase | Antibiotic resistance | Index Medicus
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2. Full Text NAA10 controls osteoblast differentiation and bone formation as a feedback regulator of Runx2
by Yoon, Haejin and Kim, Hye-Lim and Chun, Yang-Sook and Shin, Dong Hoon and Lee, Kyoung-Hwa and Shin, Chan Soo and Lee, Dong Yeon and Kim, Hong-Hee and Lee, Zang Hee and Ryoo, Hyun-Mo and Lee, Mi-Ni and Oh, Goo Taeg and Park, Jong-Wan
Nature communications, ISSN 2041-1723, 2014, Volume 5, Issue 1, pp. 5176 - 5176
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | N-Terminal Acetyltransferase A - physiology | Bone Regeneration - physiology | Osteogenesis - physiology | N-Terminal Acetyltransferase E - physiology | N-Terminal Acetyltransferases - deficiency | Molecular Sequence Data | Male | Skull - physiology | N-Terminal Acetyltransferases - genetics | Skull - injuries | Female | Osteoblasts - cytology | Cell Differentiation - physiology | Amino Acid Sequence | N-Terminal Acetyltransferase A - deficiency | Osteoblasts - physiology | Cells, Cultured | Core Binding Factor Alpha 1 Subunit - physiology | N-Terminal Acetyltransferase A - genetics | Rats | Mice, Transgenic | Rats, Sprague-Dawley | Mice, Knockout | Animals | N-Terminal Acetyltransferase E - deficiency | N-Terminal Acetyltransferase E - genetics | Signal Transduction - physiology | Mice | Wound Healing - physiology | Feedback, Physiological - physiology | N-Terminal Acetyltransferases - physiology | Index Medicus
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3. Full Text Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK
by Deng, Sunbin and McTiernan, Nina and Wei, Xuepeng and Arnesen, Thomas and Marmorstein, Ronen
Nature communications, ISSN 2041-1723, 02/2020, Volume 11, Issue 1, pp. 818 - 818
Humans | N-Terminal Acetyltransferase A - chemistry | N-Terminal Acetyltransferase A - antagonists & inhibitors | Structure-Activity Relationship | Cryoelectron Microscopy | N-Terminal Acetyltransferase E - chemistry | N-Terminal Acetyltransferase E - antagonists & inhibitors | Carrier Proteins - metabolism | N-Terminal Acetyltransferase A - metabolism | Protein Domains | Protein Processing, Post-Translational | Acetylation | Binding Sites | N-Terminal Acetyltransferase E - metabolism | Proteins | N-Terminus | Tethering | N-terminal acetyltransferase | Acetyltransferase | Inhibition | Localization | Binding sites | Substrates | Biological activity | Index Medicus
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4. Full Text A novel NAA10 p.(R83H) variant with impaired acetyltransferase activity identified in two boys with ID and microcephaly
by Ree, Rasmus and Geithus, Anni Sofie and Tørring, Pernille Mathiesen and Sørensen, Kristina Pilekær and Damkjær, Mads and Lynch, Sally Ann and Arnesen, Thomas and DDD Study and DDD study
BMC medical genetics, ISSN 1471-2350, 06/2019, Volume 20, Issue 1, pp. 101 - 101
Intellectual disability | NAA10 | NatA | XLID | X-linked | Acetylation | Microcephaly | N-alpha-acetyltransferase | Life Sciences & Biomedicine | Genetics & Heredity | Science & Technology | Amino Acid Sequence | Acetyltransferases - metabolism | Microcephaly - genetics | Humans | N-Terminal Acetyltransferase A - chemistry | N-Terminal Acetyltransferase A - genetics | Child, Preschool | Models, Molecular | Infant | Male | Mutation, Missense | Acetyltransferases - genetics | Intellectual Disability - genetics | Whole Exome Sequencing | Sequence Homology, Amino Acid | N-Terminal Acetyltransferase E - chemistry | Phenotype | N-Terminal Acetyltransferase A - metabolism | N-Terminal Acetyltransferase E - genetics | Protein Domains | N-Terminal Acetyltransferase E - metabolism | Ethylenediaminetetraacetic acid | Care and treatment | Transferases | Research | Cells | Risk factors | Heart | Phenotypes | Automation | Intellectual disabilities | Pipelines | Attention deficit hyperactivity disorder | Proteins | Microencephaly | Enzymatic activity | Boys | Coenzyme A | Acetyltransferase | Mutation | Females | Bioinformatics | Index Medicus
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5. Full Text Inactivating mutations of acetyltransferase genes in B-cell lymphoma
by Trifonov, Vladimir and Rossi, Davide and Dominguez-Sola, David and Grunn, Adina and Chadburn, Amy and Kasper, Lawryn H and Lerach, Stephanie and Murty, Vundavalli V and Ma, Jing and Brindle, Paul K and Rabadan, Raul and Chiarenza, Annalisa and Tang, Hongyan and Pasqualucci, Laura and Dalla-Favera, Riccardo and Mullighan, Charles G and Gaidano, Gianluca and Fabbri, Giulia
Nature (London), ISSN 0028-0836, 03/2011, Volume 471, Issue 7337, pp. 189 - 195
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Hematologic and hematopoietic diseases | Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis | Biological and medical sciences | Medical sciences | Histone Acetyltransferases - deficiency | Recurrence | Acetyltransferases - metabolism | Histone Acetyltransferases - chemistry | Humans | E1A-Associated p300 Protein - genetics | Gene Expression Regulation, Neoplastic | Histone Acetyltransferases - genetics | CREB-Binding Protein - chemistry | E1A-Associated p300 Protein - metabolism | Lymphoma, B-Cell - genetics | Acetyltransferases - genetics | Mutation, Missense - genetics | CREB-Binding Protein - genetics | DNA-Binding Proteins - metabolism | CREB-Binding Protein - metabolism | Lymphoma, Follicular - genetics | Acetyltransferases - deficiency | Base Sequence | Histone Acetyltransferases - metabolism | Lymphoma, B-Cell - enzymology | HEK293 Cells | Acetylation | CREB-Binding Protein - deficiency | Lymphoma, Large B-Cell, Diffuse - pathology | Lymphoma, Follicular - pathology | Cells, Cultured | E1A-Associated p300 Protein - chemistry | Lymphoma, Large B-Cell, Diffuse - enzymology | Tumor Suppressor Protein p53 - metabolism | Protein Structure, Tertiary - genetics | Mutation - genetics | Acetyl Coenzyme A - metabolism | Acetyltransferases - chemistry | Animals | Lymphoma, B-Cell - pathology | Polymorphism, Single Nucleotide - genetics | Protein Binding | Lymphoma, Follicular - enzymology | Mice | E1A-Associated p300 Protein - deficiency | Lymphoma, Large B-Cell, Diffuse - genetics | Proto-Oncogene Proteins c-bcl-6 | Sequence Deletion - genetics | Lymphomas | Genetic aspects | B cells | Gene mutations | Health aspects | Abnormalities | Proteins | Congenital diseases | Pathogenesis | Genes | Cell cycle | Genomes | Genetic engineering | Mutation | Binding sites | Index Medicus
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6. Full Text Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex
by Deng, Sunbin and Magin, Robert S and Wei, Xuepeng and Pan, Buyan and Petersson, E. James and Marmorstein, Ronen and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Structure (London), ISSN 0969-2126, 07/2019, Volume 27, Issue 7, pp. 1057 - 1070.e4
X-ray crystallography | NatE | Naa50 | NatA | protein complex | N-terminal acetylation | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Acetyltransferases - metabolism | Saccharomyces cerevisiae - genetics | Humans | N-Terminal Acetyltransferase A - chemistry | Multienzyme Complexes - metabolism | Substrate Specificity | Crystallography, X-Ray | Isoenzymes - chemistry | Acetyltransferases - genetics | Spodoptera | Sf9 Cells | Isoenzymes - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | Acetylation | Acetyl Coenzyme A - chemistry | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Isoenzymes - genetics | N-Terminal Acetyltransferase A - genetics | Models, Molecular | Recombinant Proteins - chemistry | Multienzyme Complexes - genetics | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Acetyl Coenzyme A - metabolism | Acetyltransferases - chemistry | Multienzyme Complexes - chemistry | N-Terminal Acetyltransferase E - chemistry | Animals | N-Terminal Acetyltransferase A - metabolism | Protein Conformation, beta-Strand | Escherichia coli - genetics | Saccharomyces cerevisiae Proteins - metabolism | N-Terminal Acetyltransferase E - genetics | Protein Binding | Saccharomyces cerevisiae - enzymology | Protein Processing, Post-Translational | Kinetics | N-Terminal Acetyltransferase E - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Enzymes | Medical colleges | Structure | Acetates | Crystals | Index Medicus | x-ray crystallography | INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
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7. Full Text A novel NAA10 variant with impaired acetyltransferase activity causes developmental delay, intellectual disability, and hypertrophic cardiomyopathy
by Støve, Svein Isungset and Blenski, Marina and Stray-Pedersen, Asbjørg and Wierenga, Klaas J and Jhangiani, Shalini N and Akdemir, Zeynep Coban and Crawford, David and McTiernan, Nina and Myklebust, Line M and Purcarin, Gabriela and McNall-Knapp, Rene and Wadley, Alexandrea and Belmont, John W and Kim, Jeffrey J and Lupski, James R and Arnesen, Thomas
European journal of human genetics : EJHG, ISSN 1018-4813, 09/2018, Volume 26, Issue 9, pp. 1294 - 1305
Biochemistry & Molecular Biology | Genetics & Heredity | Life Sciences & Biomedicine | Science & Technology | Cardiomyopathy, Hypertrophic - genetics | Humans | N-Terminal Acetyltransferase A - chemistry | Enzyme Stability | Intellectual Disability - pathology | N-Terminal Acetyltransferase A - genetics | Child, Preschool | Infant | Male | Developmental Disabilities - genetics | Syndrome | Intellectual Disability - genetics | N-Terminal Acetyltransferase E - chemistry | Developmental Disabilities - pathology | Phenotype | N-Terminal Acetyltransferase A - metabolism | N-Terminal Acetyltransferase E - genetics | Protein Binding | HeLa Cells | Mutation | N-Terminal Acetyltransferase E - metabolism | Cardiomyopathy, Hypertrophic - pathology | Proteins | Phenotypes | Intellectual disabilities | Cardiomyopathy | N-terminal acetyltransferase | Acetyltransferase | Acetylation | Localization | Protein interaction | Genotypes | Index Medicus
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8. Full Text Broad‐substrate screen as a tool to identify substrates for bacterial Gcn5‐related N‐acetyltransferases with unknown substrate specificity
by Kuhn, Misty L and Majorek, Karolina A and Minor, Wladek and Anderson, Wayne F
Protein science, ISSN 0961-8368, 02/2013, Volume 22, Issue 2, pp. 222 - 230
acetylation of antibiotics | Ellman's reagent | Gcn5‐related acetyltransferase | GNAT | N‐acetyltransferase | broad‐substrate screen | Broadsubstrate screen | N-acetyltransferase | Acetylation of antibiotics | Gcn5-related acetyltransferase | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Acetyltransferases - metabolism | Staphylococcus aureus - enzymology | Vibrio cholerae - enzymology | Pseudomonas aeruginosa - enzymology | Clostridium difficile - enzymology | Substrate Specificity | Agrobacterium tumefaciens - enzymology | Acetyltransferases - genetics | Acetyltransferases - chemistry | Enzymes | Peptides | Metabolites | Genomics | Physiological aspects | Catecholamines | Polyamines | Index Medicus | Acetyltransferase | broad-substrate screen | Methods and Applications
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9. Full Text Circadian Regulator CLOCK Is a Histone Acetyltransferase
by Doi, Masao and Hirayama, Jun and Sassone-Corsi, Paolo
Cell (Cambridge), ISSN 0092-8674, 05/2006, Volume 125, Issue 3, pp. 497 - 508
Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Oncogene Proteins - genetics | Trans-Activators - classification | Acetyltransferases - metabolism | Humans | Histone Acetyltransferases - genetics | Chromatin Assembly and Disassembly - genetics | Oncogene Proteins - classification | Acetyltransferases - genetics | Basic Helix-Loop-Helix Transcription Factors - metabolism | Mice, Mutant Strains | Histone Acetyltransferases - metabolism | Acetyltransferases - classification | Binding Sites - physiology | Trans-Activators - genetics | Acetylation | ARNTL Transcription Factors | Cell Line | Basic Helix-Loop-Helix Transcription Factors - genetics | Circadian Rhythm - genetics | Oncogene Proteins - metabolism | Mice, Transgenic | Transcription Factors - genetics | Transcription Factors - classification | Sequence Homology, Amino Acid | Transcription Factors - metabolism | Amino Acid Motifs - physiology | Animals | CLOCK Proteins | Cell Line, Tumor | Nuclear Receptor Coactivator 1 | Trans-Activators - metabolism | Mice | Nuclear Receptor Coactivator 3 | Histones - metabolism | Histones | Chromatin | Pacemaker, Artificial (Heart) | Research | Enzymes | DNA binding proteins | Index Medicus | Histone Acetyltransferases | Trans-Activators | Biochemistry, Molecular Biology | Oncogene Proteins | Chromatin Assembly and Disassembly | Circadian Rhythm | Amino Acid Motifs | Life Sciences | Transcription Factors | Molecular biology | Binding Sites | Acetyltransferases | Basic Helix-Loop-Helix Transcription Factors
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