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Nature, ISSN 0028-0836, 03/2011, Volume 471, Issue 7337, pp. 189 - 195
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 | Index Medicus
Journal Article
Nature Communications, ISSN 2041-1723, 2014, Volume 5, Issue 1, pp. 5176 - 5176
Journal Article
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
Journal Article
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 | Protein Structure, Tertiary | Acetyltransferases - metabolism | Multigene Family | Drug Resistance, Bacterial | Enterococcus faecium - enzymology | Models, Molecular | Aminoglycosides | Crystallography, X-Ray | Acetyl Coenzyme A - metabolism | Acetyltransferases - chemistry | Enterococcus faecium - metabolism | Protein Binding | Anti-Bacterial Agents - pharmacology | Binding Sites | Evolution, Molecular | Index Medicus
Journal Article
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 | 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
Journal Article
The EMBO Journal, ISSN 0261-4189, 07/2011, Volume 30, Issue 14, pp. 2829 - 2842
The SAGA (Spt–Ada–Gcn5 acetyltransferase) complex is an important chromatin modifying complex that can both acetylate and deubiquitinate histones. Sgf29 is a... 
Tudor | Sgf29 | H3K4 methylation | SAGA | MOLECULAR REPLACEMENT | CODING REGIONS | PROTEIN IDENTIFICATION TECHNOLOGY | COACTIVATOR COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | SACCHAROMYCES-CEREVISIAE | MASS-SPECTROMETRY | CELL BIOLOGY | SWIRM DOMAIN | STRUCTURAL BASIS | TUDOR DOMAIN | ACETYLTRANSFERASE COMPLEXES | Acetyltransferases - metabolism | Peptide Fragments | Histone Acetyltransferases - chemistry | Saccharomyces cerevisiae - genetics | Humans | Histone Acetyltransferases - genetics | Molecular Sequence Data | Acetyltransferases - genetics | Saccharomyces cerevisiae - metabolism | Chromatin Immunoprecipitation | Histone Acetyltransferases - metabolism | Trans-Activators - genetics | Acetylation | Protein Structure, Tertiary | Amino Acid Sequence | RNA, Messenger - genetics | Gene Expression Regulation | Saccharomyces cerevisiae Proteins - genetics | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Acetyltransferases - chemistry | Sequence Homology, Amino Acid | Saccharomyces cerevisiae Proteins - metabolism | Trans-Activators - metabolism | Protein Processing, Post-Translational | Histones - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Binding sites | Crystal structure | Index Medicus | HUMAN POPULATIONS | CHROMATIN | BASIC BIOLOGICAL SCIENCES | ACETYLATION | COMPLEXES | LENGTH | SACCHAROMYCES CEREVISIAE | CRYSTAL STRUCTURE | IN VIVO | 60 APPLIED LIFE SCIENCES | HISTONES | PEPTIDES | ALANINES | IN VITRO | TARGETS | GENE REGULATION | RESIDUES | FUNCTIONALS
Journal Article
Nature Structural and Molecular Biology, ISSN 1545-9993, 09/2013, Volume 20, Issue 9, pp. 1098 - 1105
Journal Article
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 | SUBUNITS | 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 | Eukaryotes | Microorganisms | Mutagenesis | Biochemistry | Enzyme kinetics | Index Medicus | Biological Sciences
Journal Article
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
Journal Article
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 | Index Medicus
Journal Article