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1. 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, ISSN 1018-4813, 09/2018, Volume 26, Issue 9, pp. 1294 - 1305
The NAA10-NAA15 complex (NatA) is an N-terminal acetyltransferase that catalyzes N-terminal acetylation of similar to 40% of all human proteins. N-terminal... 
GTPASE ARL3P | MEMBRANE-PROTEIN SYS1P | NATA-COMPLEX | N-TERMINAL-ACETYLTRANSFERASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SUBSTRATE-SPECIFIC ACETYLATION | GENETICS & HEREDITY | OGDEN SYNDROME | LENZ MICROPHTHALMIA SYNDROME | ALPHA-ACETYLTRANSFERASE | MOLECULAR-BASIS | REVEALS | 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
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2. 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
The rise of antibiotic resistance as a public health concern has led to increased interest in studying the ways in which bacteria avoid the effects of... 
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
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3. Full Text Inactivating mutations of acetyltransferase genes in B-cell lymphoma
by Pasqualucci, Laura and Dominguez-Sola, David and Chiarenza, Annalisa and Fabbri, Giulia and Grunn, Adina and Trifonov, Vladimir and Kasper, Lawryn H and Lerach, Stephanie and Tang, Hongyan and Ma, Jing and Rossi, Davide and Chadburn, Amy and Murty, Vundavalli V and Mullighan, Charles G and Gaidano, Gianluca and Rabadan, Raul and Brindle, Paul K and Dalla-Favera, Riccardo
Nature, ISSN 0028-0836, 03/2011, Volume 471, Issue 7337, pp. 189 - 196
B-cell non-Hodgkin's lymphoma comprises biologically and clinically distinct diseases the pathogenesis of which is associated with genetic lesions affecting... 
CBP | RUBINSTEIN-TAYBI SYNDROME | HISTONE ACETYLTRANSFERASES | ACETYLATION | P300 | MULTIDISCIPLINARY SCIENCES | CREB-BINDING-PROTEIN | CYCLE ARREST | ACUTE MYELOID-LEUKEMIA | TRANSCRIPTIONAL COACTIVATOR | P53 | 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
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4. 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, p. 5176
Runt-related transcription factor 2 (Runx2) transactivates many genes required for osteoblast differentiation. The role of N-alpha-acetyltransferase 10 (NAA10,... 
N-TERMINAL ACETYLTRANSFERASE | ARD1 | OSTEOCALCIN GENE | ACETYLATION | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTION | GROWTH | RECEPTOR | MOLECULAR-BASIS | MORPHOGENETIC PROTEIN-2 | 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
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5. Lysine Methylation and Functional Modulation of Androgen Receptor by Set9 Methyltransferase
by Ko, Soyoung and Ahn, Jungmi and Song, Chung S and Kim, Soyoung and Knapczyk-Stwora, Katarzyna and Chatterjee, Bandana
Molecular Endocrinology, ISSN 0888-8809, 01/2011, Volume 25, Issue 3, pp. 433 - 444
Lysine methyltransferases modulate activities of transcription factors and transcription coregulators by methylating specific lysine residue(s). We report that... 
Acetyltransferase
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6. 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
Due to a combination of efforts from individual laboratories and structural genomics centers, there has been a surge in the number of members of the... 
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 | MYCOBACTERIUM-TUBERCULOSIS | AMINOGLYCOSIDE 6'-N-ACETYLTRANSFERASE | HIGH-THROUGHPUT | ACETYLATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COENZYME-A | POLYMYXIN-B | broad-substrate screen | IN-VITRO | PSEUDOMONAS-AERUGINOSA | SUPERFAMILY | 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 | Acetyltransferase | Methods and Applications
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7. Full Text N‐terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N‐terminal acetyltransferases and methionine aminopeptidases
by Damme, Petra and Hole, Kristine and Gevaert, Kris and Arnesen, Thomas
PROTEOMICS, ISSN 1615-9853, 07/2015, Volume 15, Issue 14, pp. 2436 - 2446
Cotranslational N‐terminal (Nt‐) acetylation of nascent polypeptides is mediated by N‐terminal acetyltransferases (NATs). The very N‐terminal amino acid... 
NAT | Naa50 | N‐terminomics | Methionine aminopeptidase | Acetylation | Nt‐acetylome | N‐terminal acetyltransferase | N-terminomics | N-terminal acetyltransferase | Nt-acetylome | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | ALPHA-ACETYLTRANSFERASE | IDENTIFICATION | NASCENT POLYPEPTIDE-CHAINS | YEAST | PEPTIDES | IN-VIVO | PROTEINS | PROTEOMICS | Saccharomyces cerevisiae - genetics | Humans | Glycoproteins - metabolism | Molecular Sequence Data | Substrate Specificity | Saccharomyces cerevisiae - metabolism | N-Terminal Acetyltransferase D - genetics | Gene Deletion | Aminopeptidases - chemistry | Glycoproteins - chemistry | Aminopeptidases - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Gene Expression | Methionine - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - chemistry | N-Terminal Acetyltransferase D - metabolism | N-Terminal Acetyltransferase E - chemistry | N-Terminal Acetyltransferase D - chemistry | Saccharomyces cerevisiae Proteins - metabolism | N-Terminal Acetyltransferase E - genetics | Kinetics | N-Terminal Acetyltransferase E - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Amino acids | Aminopeptidases | Analysis | Competition | Yeast | Polypeptides | Substrate specificity | Deduction | Methionine | Amino acid sequence | Catalysis | Substrates
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8. Full Text Molecular basis for N-terminal acetylation by the heterodimeric NatA complex
by Liszczak, Glen and Goldberg, Jacob M and Foyn, Håvard and Petersson, E. James and Arnesen, Thomas and Marmorstein, Ronen
Nature Structural and Molecular Biology, ISSN 1545-9993, 09/2013, Volume 20, Issue 9, pp. 1098 - 1105
N-terminal acetylation is ubiquitous among eukaryotic proteins and controls a myriad of biological processes. Of the N-terminal acetyltransferases (NATs) that... 
ARD1 | APOPTOSIS | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALPHA-ACETYLTRANSFERASE | HISTONE ACETYLTRANSFERASE | IDENTIFICATION | CELL BIOLOGY | YEAST | BIOPHYSICS | CATALYTIC MECHANISM | KNOCKDOWN | EXPRESSION | Protein Subunits | Schizosaccharomyces pombe Proteins - chemistry | Acetyltransferases - metabolism | Allosteric Regulation | Humans | N-Terminal Acetyltransferase A - chemistry | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Holoenzymes - chemistry | Acetyltransferases - genetics | Schizosaccharomyces - genetics | Holoenzymes - metabolism | Protein Structure, Quaternary | Schizosaccharomyces pombe Proteins - metabolism | Amino Acid Sequence | Catalytic Domain | Mutagenesis, Site-Directed | Schizosaccharomyces pombe Proteins - genetics | N-Terminal Acetyltransferase A - genetics | Models, Molecular | Acetyltransferases - chemistry | Sequence Homology, Amino Acid | Animals | N-Terminal Acetyltransferase A - metabolism | Schizosaccharomyces - enzymology | Holoenzymes - genetics | Kinetics | Physiological aspects | Cellular proteins | Acetylation | Research | Structure | Proteins | Molecular biology | Binding sites | Crystal structure
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9. Nucleotide Exchange and Excision Technology DNA Shuffling and Directed Evolution
by Speck, J and Stebel, SC and Arndt, KM and Miiller, KM
Methods in Molecular Biology, ISSN 1064-3745, 01/2011, Volume 687, pp. 333 - 341
Remarkable success in optimizing complex properties within DNA and proteins has been achieved by directed evolution. In contrast to various random mutagenesis... 
Acetyltransferase
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10. Full Text Biochemical characterization of Hpa2 and Hpa3, two small closely related acetyltransferases from saccharomyces cerevisiae
by Sampath, Vinaya and Liu, Bingsheng and Tafrov, Stefan and Srinivasan, Madhusudhan and Rieger, Robert and Chen, Emily I and Sternglanz, Rolf and Brookhaven National Laboratory (BNL)
Journal of Biological Chemistry, ISSN 0021-9258, 07/2013, Volume 288, Issue 30, pp. 21506 - 21513
Based on their sequences, the Saccharomyces cerevisiae Hpa2 and Hpa3 proteins are annotated as two closely related members of the Gcn5 acetyltransferase... 
D-AMINO ACIDS | Translation | PROTEIN | ACETYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | Mass Spectrometry (MS) | ACID-N-ACETYLTRANSFERASE | HISTONE ACETYLTRANSFERASE | Polyamines | HAT COMPLEX | YEAST | Histone Modification | METABOLISM | GENES | Acetyltransferase | Histone Acetylase | EXPRESSION | Acetyltransferases - metabolism | Codon, Initiator - genetics | Histone Acetyltransferases - chemistry | Saccharomyces cerevisiae - genetics | Protein Multimerization | Spermidine - metabolism | Histone Acetyltransferases - genetics | Molecular Sequence Data | Substrate Specificity | Amino-Acid N-Acetyltransferase - metabolism | Acetyltransferases - genetics | Amino Acids - metabolism | Isoenzymes - metabolism | Histone Acetyltransferases - metabolism | Lysine - metabolism | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Acetylation | Amino Acid Sequence | High Mobility Group Proteins - metabolism | Isoenzymes - genetics | Electrophoresis, Polyacrylamide Gel | Amino-Acid N-Acetyltransferase - genetics | Saccharomyces cerevisiae Proteins - genetics | Amino-Acid N-Acetyltransferase - chemistry | Acetyltransferases - chemistry | Sequence Homology, Amino Acid | Spermine - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Histones - metabolism | Mutation | Methionine - genetics | Putrescine - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Index Medicus | BASIC BIOLOGICAL SCIENCES | Enzymology
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11. Full Text Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog
by Glen Liszczak and Ronen Marmorstein
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2013, Volume 110, Issue 36, pp. 14652 - 14657
Amino-terminal acetylation is a ubiquitous modification in eukaryotes that is involved in a growing number of biological processes.There are six known... 
Proteins | Enzymes | Active sites | Substrate specificity | Archaea | Evolution | Acetylation | Catalysis | Enzyme substrates | Cartoons | X-ray crystallography | Evolutionary biology | Enzymology | Structural biology | YEAST | COMPLEX | evolutionary biology | ACETYLATION | MULTIDISCIPLINARY SCIENCES | structural biology | N-ACETYLTRANSFERASE | enzymology | PROTEOMICS | N-Terminal Acetyltransferase A - chemistry | Protein Multimerization | Archaeal Proteins - chemistry | Molecular Sequence Data | Crystallography, X-Ray | N-Terminal Acetyltransferases - chemistry | N-Terminal Acetyltransferases - metabolism | N-Terminal Acetyltransferases - genetics | Archaeal Proteins - genetics | Acetyl Coenzyme A - chemistry | Archaeal Proteins - metabolism | Eukaryotic Cells - enzymology | Protein Structure, Tertiary | Amino Acid Sequence | Catalytic Domain - genetics | N-Terminal Acetyltransferase A - genetics | Models, Molecular | Sulfolobus solfataricus - enzymology | Acetyl Coenzyme A - metabolism | Sequence Homology, Amino Acid | N-Terminal Acetyltransferase E - chemistry | N-Terminal Acetyltransferase A - metabolism | N-Terminal Acetyltransferase E - genetics | Protein Binding | Kinetics | Mutation | N-Terminal Acetyltransferase E - metabolism | Evolution, Molecular | Microbial genetics | Transferases | Bacteria, Thermophilic | Crystals | Physiological aspects | Evolutionary genetics | Genetic aspects | Research | Structure | Index Medicus | Biological Sciences
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12. Full Text Circadian Regulator CLOCK Is a Histone Acetyltransferase
by Doi, Masao and Hirayama, Jun and Sassone-Corsi, Paolo
Cell, ISSN 0092-8674, 05/2006, Volume 125, Issue 3, pp. 497 - 508
The molecular machinery that governs circadian rhythmicity comprises proteins whose interplay generates time-specific transcription of clock genes. The role of... 
ACTIVATION | CHROMATIN | MECHANISM | ACETYLATION | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | MOUSE | PERIPHERAL CLOCK | GENE-EXPRESSION | PROTEIN SIR2 | 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 | 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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13. Full Text De novo missense mutations in the NAA10 gene cause severe non-syndromic developmental delay in males and females
by Popp, Bernt and Støve, Svein I and Endele, Sabine and Myklebust, Line M and Hoyer, Juliane and Sticht, Heinrich and Azzarello-Burri, Silvia and Rauch, Anita and Arnesen, Thomas and Reis, André
European Journal of Human Genetics, ISSN 1018-4813, 05/2015, Volume 23, Issue 5, pp. 602 - 609
Recent studies revealed the power of whole-exome sequencing to identify mutations in sporadic cases with non-syndromic intellectual disability. We now... 
N-TERMINAL ACETYLTRANSFERASE | INTELLECTUAL DISABILITY | ARD1 | COMPLEX | HUMAN GENOME | COFFIN-LOWRY-SYNDROME | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENETICS & HEREDITY | LENZ MICROPHTHALMIA SYNDROME | ALPHA-ACETYLTRANSFERASE | AUTISM SPECTRUM DISORDERS | SEQUENCING DATA | Phenotypes | Intellectual disabilities | Genes | Licenses | Genomes | Males | Proteins | Genotype & phenotype | Missense mutation | Cell cycle | Genetics | N-terminal acetyltransferase | Acetyltransferase | Mutation | Acetylation
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14. Full Text Cellular localization and kinetics of the rice melatonin biosynthetic enzymes SNAT and ASMT
by Byeon, Yeong and Lee, Hyoung Yool and Lee, Kyungjin and Park, Sangkyu and Back, Kyoungwhan
Journal of Pineal Research, ISSN 0742-3098, 01/2014, Volume 56, Issue 1, pp. 107 - 114
Serotonin N‐acetyltransferase (SNAT) and N‐acetylserotonin methyltransferase (ASMT) are the final two enzymes in the melatonin synthesis pathway in plants.... 
localization | chlorophyll | serotonin N‐acetyltransferase | O‐methyltransferase | chloroplast | O-methyltransferase | serotonin N-acetyltransferase | N-ACETYLSEROTONIN METHYLTRANSFERASE | PHYSIOLOGY | CATHARANTHUS-ROSEUS | SUBCELLULAR-LOCALIZATION | PINEAL-GLAND | SWEET CHERRY | NEUROSCIENCES | GROWTH-STIMULATING COMPOUND | TRANSGENIC RICE | ENDOCRINOLOGY & METABOLISM | SEROTONIN | EXOGENOUS MELATONIN | TRYPTOPHAN DECARBOXYLASE | Acetylserotonin O-Methyltransferase - metabolism | Oryza - metabolism | Arylalkylamine N-Acetyltransferase - genetics | Acetylserotonin O-Methyltransferase - analysis | Oryza - enzymology | Intracellular Space - chemistry | Acetylserotonin O-Methyltransferase - genetics | Analysis of Variance | Arylalkylamine N-Acetyltransferase - metabolism | Oryza - genetics | Acetylserotonin O-Methyltransferase - chemistry | Arylalkylamine N-Acetyltransferase - chemistry | Intracellular Space - metabolism | Arylalkylamine N-Acetyltransferase - analysis | Melatonin - metabolism | Melatonin - biosynthesis | Kinetics | Oryza - cytology | Chlorophyll | Enzymes | Melatonin | Aralkylamine N-acetyltransferase
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