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naa10 (21) 21
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1. Full Text The N-terminal acetyltransferase Naa10 is essential for zebrafish development
by Ree, Rasmus and Myklebust, Line M and Thiel, Puja and Foyn, Håvard and Fladmark, Kari E and Arnesen, Thomas
Bioscience Reports, ISSN 0144-8463, 10/2015, Volume 35, Issue 5, pp. e00249 - e00249
N-terminal acetylation, catalysed by N-terminal acetyltransferases (NATs), is among the most common protein modifications in eukaryotes and involves the... 
N-terminal acetyltransferase (NAT) | Nαacetyltransferase 10 (Naa10) | Abnormal development | N-terminal acetyltransferase A (NatA) | Danio rerio | N-terminal acetylation | abnormal development | COMPLEX | PROTEIN | NATA | ACTIN | ACETYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | N alpha-acetyltransferase 10 (Naa10) | CANCER | DROSOPHILA | CELL BIOLOGY | YEAST | PATHWAY | Amino Acid Sequence | Humans | N-Terminal Acetyltransferase A - chemistry | Zebrafish - abnormalities | N-Terminal Acetyltransferase A - genetics | Molecular Sequence Data | Substrate Specificity | Phylogeny | Zebrafish - embryology | Zebrafish - genetics | Gene Knockdown Techniques | N-Terminal Acetyltransferase E | Sequence Alignment | Animals | Acetylation | Nα-acetyltransferase 10 (Naa10)
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2. Full Text Prevalence and architecture of de novo mutations in developmental disorders
by McRae, Jeremy F and Clayton, Stephen and Fitzgerald, Tomas W and Kaplanis, Joanna and Prigmore, Elena and Rajan, Diana and Sifrim, Alejandro and Aitken, Stuart and Akawi, Nadia and Alvi, Mohsan and Ambridge, Kirsty and Barrett, Daniel M and Bayzetinova, Tanya and Jones, Philip and Jones, Wendy D and King, Daniel and Krishnappa, Netravathi and Mason, Laura E and Singh, Tarjinder and Tivey, Adrian R and Ahmed, Munaza and Anjum, Uruj and Archer, Hayley and Armstrong, Ruth and Awada, Jana and Balasubramanian, Meena and Banka, Siddharth and Baralle, Diana and Barnicoat, Angela and Batstone, Paul and Baty, David and Bennett, Chris and Berg, Jonathan and Bernhard, Birgitta and Bevan, A. Paul and Bitner-Glindzicz, Maria and Blair, Edward and Blyth, Moira and Bohanna, David and Bourdon, Louise and Bourn, David and Bradley, Lisa and Brady, Angela and Brent, Simon and Brewer, Carole and Brunstrom, Kate and Bunyan, David J and Burn, John and Canham, Natalie and Castle, Bruce and Chandler, Kate and Chatzimichali, Elena and Cilliers, Deirdre and Clarke, Angus and Clasper, Susan and Clayton-Smith, Jill and Clowes, Virginia and Coates, Andrea and Cole, Trevor and Colgiu, Irina and Collins, Amanda and Collinson, Morag N and Connell, Fiona and Cooper, Nicola and Cox, Helen and Cresswell, Lara and Cross, Gareth and Crow, Yanick and D'Alessandro, Mariella and Dabir, Tabib and Davidson, Rosemarie and Davies, Sally and De Vries, Dylan and Dean, John and Deshpande, Charu and Devlin, Gemma and Dixit, Abhijit and Dobbie, Angus and Donaldson, Alan and Donnai, Dian and Donnelly, Deirdre and Donnelly, Carina and Douglas, Angela and Douzgou, Sofia and Duncan, Alexis and Eason, Jacqueline and Ellard, Sian and Ellis, Ian and Elmslie, Frances and Evans, Karenza and Everest, Sarah and Fendick, Tina and Fisher, Richard and Flinter, Frances and Foulds, Nicola and Fry, Andrew and Fryer, Alan and Gardiner, Carol and Gaunt, Lorraine and Ghali, Neeti and ... and Deciphering Developmental Disorders Study
Nature, ISSN 0028-0836, 02/2017, Volume 542, Issue 7642, pp. 433 - 438
The genomes of individuals with severe, undiagnosed developmental disorders are enriched in damaging de novo mutations (DNMs) in developmentally important... 
INTELLECTUAL DISABILITY | METAANALYSIS | VARIANTS | GENETICS | HEART-DEFECTS | MULTIDISCIPLINARY SCIENCES | GENES | SEQUENCE | FRAMEWORK | DISCOVERY | GENOME | Prevalence | Humans | Middle Aged | Parents | Male | Mi-2 Nucleosome Remodeling and Deacetylase Complex - genetics | Developmental Disabilities - genetics | Casein Kinase II - genetics | Autoantigens - genetics | Young Adult | ras GTPase-Activating Proteins - genetics | Adult | Female | Child | CDC2 Protein Kinase - genetics | Histone-Lysine N-Methyltransferase - genetics | Repressor Proteins - genetics | Sex Characteristics | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Mutation - genetics | Nerve Tissue Proteins - genetics | Sequence Analysis, DNA | Homeodomain Proteins - genetics | DEAD-box RNA Helicases - genetics | Exome - genetics | Phenotype | Myeloid-Lymphoid Leukemia Protein - genetics | Adolescent | Heredity - genetics | Protein Phosphatase 2C - genetics | Cohort Studies | Child development deviations | Genetic aspects | Genetic disorders | Developmental disabilities | Distribution | Genes | Families & family life | Births | Genomes | Mutation | Causality | Estimates | Age | TRIO | MYT1L | EHMT1 | HNRNPU | SUV420H1 | COL4A3BP | SYNGAP1 | PPP2R1A | POGZ | EP300 | KCNH1 | SCN1A | MEF2C | CDKL5 | CSNK2A1 | DYRK1A | CASK | ALG13 | FOXP1 | KAT6B | TBL1XR1 | KAT6A | SCN8A | KCNQ2 | EEF1A2 | KCNQ3 | ADNP | PhenIcons | SET | KMT2A | ANKRD11 | STXBP1 | FOXG1 | ZC4H2 | ITPR1 | De novo mutation | Seizures | ZBTB18 | CREBBP | SMAD4 | PDHA1 | IQSEC2 | AUTS2 | BCL11A | BRAF | SMARCA2 | GRIN2B | MED13L | GNAO1 | CNOT3 | TCF4 | SCN2A | CDK13 | GABRB3 | SETD5 | KDM5B | Developmental Disease | DDX3X | CHD8 | PTEN | CHD4 | TCF20 | CTCF | CHD2 | WDR45 | SLC6A1 | MECP2 | CHAMP1 | KIF1A | Average Faces | MSL3 | PPP2R5D | SMC1A | ARID1B | DNM1 | CNKSR2 | PACS1 | WAC | ZMYND11 | AHDC1 | NFIX | SATB2 | HDAC8 | PPM1D | GNAI1 | PURA | PUF60 | NSD1 | Intellectual Disability | SLC35A2 | DYNC1H1 | NAA10 | USP9X | PTPN11 | GATAD2B | ASXL1 | KANSL1 | ASXL3 | CTNNB1 | QRICH1
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3. Full Text Clinical Manifestations Associated With the N-Terminal-Acetyltransferase NAA10 Gene Mutation in a Girl: Ogden Syndrome
by Sidhu, M and Brady, L and Tarnopolsky, M and Ronen, GM
PEDIATRIC NEUROLOGY, ISSN 0887-8994, 11/2017, Volume 76, pp. 82 - 85
BACKGROUND: Ogden syndrome is a rare X-linked disorder caused by pathogenic variants in the NAA10 gene. This syndrome, reported in just over 20 children, has... 
ACETYLATION | hypersomnolence | CLINICAL NEUROLOGY | INTELLECTUAL DISABILITY | NAA10 gene | movement disorder | X-linked condition | Ogden syndrome | levodopa | PEDIATRICS | evolving neurological condition | genetic syndrome | MALES | acetyltransferase
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4. Full Text Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway
by Oh, Jang-Hyun and Hyun, Ju-Yeon and Varshavsky, Alexander
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 05/2017, Volume 114, Issue 22, pp. E4370 - E4379
We found that the heat shock protein 90 (Hsp90) chaperone system of the yeast Saccharomyces cerevisiae is greatly impaired in naa10 Delta cells, which lack the... 
Ufd4 | Protein degradation | Chk1 | Ubr1 | Naa10 | MOLECULAR CHAPERONES | DEGRADATION SIGNAL | MULTIDISCIPLINARY SCIENCES | UBIQUITIN LIGASES | STRUCTURAL BASIS | PROTEIN-QUALITY CONTROL | GLUCONEOGENIC ENZYMES | SPLIT-UBIQUITIN | ARGINYLATION | CELLULAR-PROTEINS | protein degradation | Ubiquitin | Biodegradation | Hsp90 protein | Yeast | Glycerol-3-phosphate dehydrogenase | CHK1 protein | Heat shock proteins | Homeostasis | Saccharomyces | Kinases | Clients | Ablation | Cells | Substrates | Proteins | Acetylation | Saccharomyces cerevisiae | Heat shock | Biological Sciences | PNAS Plus
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5. Full Text NAT6 acetylates the N‐terminus of different forms of actin
by Wiame, Elsa and Tahay, Gaëlle and Tyteca, Donatienne and Vertommen, Didier and Stroobant, Vincent and Bommer, Guido T and Van Schaftingen, Emile
The FEBS Journal, ISSN 1742-464X, 09/2018, Volume 285, Issue 17, pp. 3299 - 3316
All forms of mammalian actin comprise at their N‐terminus a negatively charged region consisting of an N‐acetylated aspartate or glutamate followed by two or... 
acetylation | NAT6 | actin | NAA10 | acetyltransferase | N-acetyltransferase | RAT-LIVER | ACYLPEPTIDE HYDROLASE | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | PHOSPHATE | METABOLISM | CLONING | FRUCTOSELYSINE | EXPRESSION | ACETYLTRANSFERASE | Muscles | Enzymes | Aspartate | Muscle proteins | Actin | Cells | Residues | Sequences | Peptides | Incubation | Low concentrations | Mammals | Substrates | Skeletal muscle | Proteins | Cell lines | Acetylation | Recombinant
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6. Full Text NAA10 polyadenylation signal variants cause syndromic microphthalmia
by Johnston, Jennifer J and Williamson, Kathleen A and Chou, Christopher M and Sapp, Julie C and Ansari, Morad and Chapman, Heather M and Cooper, David N and Dabir, Tabib and Dudley, Jeffrey N and Holt, Richard J and Ragge, Nicola K and Schäffer, Alejandro A and Sen, Shurjo K and Slavotinek, Anne M and Fitzpatrick, David R and Glaser, Thomas M and Stewart, Fiona and Black, Graeme C.M and Biesecker, Leslie G
Journal of Medical Genetics, ISSN 0022-2593, 2019, Volume 56, Issue 7, pp. 444 - 452
A single variant in (c.471+2T>A), the gene encoding N-acetyltransferase 10, has been associated with Lenz microphthalmia syndrome. In this study, we aimed to... 
Naa10 | polyadenylation signal | METHYLATION | IDENTIFY | PROTEIN | ANOPHTHALMIA | PHENOTYPE | FAMILY | NEURODEVELOPMENTAL DISORDERS | GENE | GENETICS & HEREDITY | SITES | MUTATIONS | Haplotypes | Genomics | N-Acetyltransferase | mRNA | Genomes | Gene expression | Males | Data bases | Genetic screening | Genetic analysis | Polyadenylation | Genetics | Acetyltransferase | Mutation | Anophthalmia | Deoxyribonucleic acid--DNA | Microphthalmia | Linkage analysis
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7. Full Text Co-translational, Post-translational, and Non-catalytic Roles of N-Terminal Acetyltransferases
by Aksnes, Henriette and Ree, Rasmus and Arnesen, Thomas
Molecular Cell, ISSN 1097-2765, 03/2019, Volume 73, Issue 6, pp. 1097 - 1114
Recent studies of N-terminal acetylation have identified new N-terminal acetyltransferases (NATs) and expanded the known functions of these enzymes beyond... 
acetylation | NAT | actin | protein modifications | NAA10 | N-terminal acetylation | N-terminal acetyltransferase | lysine acetyltransferase | KAT | NAA80 | GTPASE ARL3P | SIGNALING PATHWAY | HUMAN-CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELLULAR-PROTEINS | ALPHA-ACETYLTRANSFERASE | PROTEIN ACETYLATION | IDENTIFICATION | MOLECULAR-BASIS | SIR3 STABILIZES | CALORIE RESTRICTION | CELL BIOLOGY
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8. Full Text Structural basis of HypK regulating N-Terminal acetylation by the NatA complex
by Weyer, Felix Alexander and Gumiero, Andrea and Lapouge, Karine and Bange, Gert and Kopp, Jürgen and Sinning, Irmgard
Nature Communications, ISSN 2041-1723, 06/2017, Volume 8, Issue 1, p. 15726
In eukaryotes, N-terminal acetylation is one of the most common protein modifications involved in a wide range of biological processes. Most... 
YEAST | PROTEIN HYPK | NAA10 | INTERACTS | MULTIDISCIPLINARY SCIENCES | CHAPERONE | HUNTINGTIN | MOLECULAR-BASIS | ACETYLTRANSFERASES | RIBOSOME | REVEALS | Catalytic Domain | Protein Biosynthesis | Selenomethionine - chemistry | Peptides - chemistry | Protein Structure, Secondary | Humans | N-Terminal Acetyltransferase A - chemistry | Protein Multimerization | Models, Molecular | Crystallography, X-Ray | Acetyltransferases - genetics | Chaetomium | Light | Protein Denaturation | Protein Binding | Protein Domains | Carrier Proteins - chemistry | Protein Processing, Post-Translational | Scattering, Radiation | Acetylation
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9. Full Text Expanding the Phenotype Associated with NAA10-Related N-Terminal Acetylation Deficiency
by Saunier, Chloé and Støve, Svein Isungset and Popp, Bernt and Gérard, Bénédicte and Blenski, Marina and Ahmew, Nicholas and de Bie, Charlotte and Goldenberg, Paula and Isidor, Bertrand and Keren, Boris and Leheup, Bruno and Lampert, Laetitia and Mignot, A and Tezcan, Kamer and Mancini, Grazia and Nava, Caroline and Wasserstein, Melissa and Bruel, Ange-Line and Thevenon, Julien and Masurel, Alice and Duffourd, Yannis and Kuentz, Paul and Huet, Frédéric and Riviere, J.-B and Slegtenhorst, Marjon and Faivre, Laurence and Piton, Amélie and Reis, Ané and Arnesen, Thomas and Thauvin-Robinet, Christel and Zweier, Christiane
Human Mutation, ISSN 1059-7794, 01/2016, Volume 37, Issue 8, pp. 755 - 764
textabstractN-terminal acetylation is a common protein modification in eukaryotes associated with numerous cellular processes. Inherited mutations in NAA10,... 
X‐linked | N‐terminal acetylation | NAA10 | intellectual disability | X-linked | Intellectual disability | N-terminal acetylation | GTPASE ARL3P | COMPLEX | FEMALES | IDENTIFICATION | MISSENSE MUTATIONS | MEMBRANE-PROTEIN SYS1P | GENETICS & HEREDITY | REQUIRES | X-CHROMOSOME INACTIVATION | ACETYLTRANSFERASE | Genetic Predisposition to Disease | Genetic Association Studies | N-Terminal Acetyltransferase A - deficiency | Humans | N-Terminal Acetyltransferase A - chemistry | N-Terminal Acetyltransferase A - genetics | Models, Molecular | Male | Mutation, Missense | Intellectual Disability - genetics | N-Terminal Acetyltransferase E - chemistry | Genes, X-Linked | Pedigree | N-Terminal Acetyltransferase E - deficiency | Germ-Line Mutation | N-Terminal Acetyltransferase E - genetics | Female | Mosaicism | Acetylation | Enzymes | Acetates | Genetic aspects | Proteins | Genotype & phenotype | Genetic disorders | Mutation | Life Sciences | Genetics
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10. Full Text microRNA-342-5p and miR-608 inhibit colon cancer tumorigenesis by targeting NAA10
by Yang, Hongju and Li, Qian and Niu, Jie and Li, Bai and Jiang, Dejun and Wan, Zhihua and Yang, Qingmei and Jiang, Fei and Wei, Ping and Bai, Song
Oncotarget, ISSN 1949-2553, 2016, Volume 7, Issue 3, pp. 2709 - 2720
miRNAs have been shown to play pivotal roles in the establishment and progression of colon cancer, but their underlying mechanisms are not fully understood.... 
MiR-342-5p | MiR-608 | Colon cancer | NAA10 | Cell Proliferation - genetics | Colonic Neoplasms - genetics | Humans | Gene Expression Regulation, Neoplastic | N-Terminal Acetyltransferase A - genetics | Apoptosis - genetics | Mice, SCID | Xenograft Model Antitumor Assays | Animals | N-Terminal Acetyltransferase A - metabolism | Cell Transformation, Neoplastic - genetics | Colonic Neoplasms - pathology | Cell Line, Tumor | N-Terminal Acetyltransferase E - genetics | Mice | MicroRNAs - genetics | N-Terminal Acetyltransferase E - metabolism
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11. 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
BMC Medical Genetics, ISSN 1471-2350, 06/2019, Volume 20, Issue 1, pp. 101 - 8
N-terminal acetylation is a common protein modification in human cells and is catalysed by N-terminal acetyltransferases (NATs), mostly cotranslationally. The... 
Intellectual disability | NAA10 | NatA | XLID | X-linked | Acetylation | Microcephaly | N-alpha-acetyltransferase | 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
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12. Full Text The biological functions of Naa10 — From amino-terminal acetylation to human disease
by Dörfel, Max J and Lyon, Gholson J
Gene, ISSN 0378-1119, 08/2015, Volume 567, Issue 2, pp. 103 - 131
N-terminal acetylation (NTA) is one of the most abundant protein modifications known, and the N-terminal acetyltransferase (NAT) machinery is conserved... 
Proteins | NAA50 | ard1 | NAA10 | Ogden syndrome | Amino-terminal acetylation | Proteomics | NAA15 | Enzymology | Acetyltransferases | Ard1 | INDUCIBLE FACTOR 1-ALPHA | ALTERNATIVE TRANSLATION INITIATION | N-ALPHA-ACETYLTRANSFERASE | LARGE-SCALE IDENTIFICATION | ARF-LIKE GTPASE | SUBSTRATE-SPECIFIC ACETYLATION | GENETICS & HEREDITY | SIGNAL RECOGNITION PARTICLE | END RULE PATHWAY | RIBOSOMAL-PROTEIN MODIFICATION | INTEGRAL MEMBRANE-PROTEIN | N-Terminal Acetyltransferase A - physiology | Protein Structure, Tertiary | Amino Acid Sequence | N-Terminal Acetyltransferase E - physiology | Humans | N-Terminal Acetyltransferase A - chemistry | Gene Expression Regulation | Genetic Diseases, Inborn - genetics | Molecular Sequence Data | Neoplasms - enzymology | Cell Hypoxia | N-Terminal Acetyltransferase E - chemistry | Animals | Genetic Diseases, Inborn - metabolism | Protein Processing, Post-Translational | Acetylation | DNA Damage | Analysis | Protein-protein interactions | Medicine, Experimental | Medical research | Lysine
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