نتائج البحث - "Histone Acetyltransferases"

1

Wilms’ tumor 1-associating protein complex regulates alternative splicing and polyadenylation at potential G-quadruplex-forming splice site sequences

المؤلفون: Takao Hamakubo, Takeshi Kawamura, Keiko Horiuchi

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: Polyadenylation, DEI, differentially expressed isoform, Ubiquitin-Protein Ligases, Cell Cycle Proteins, Biology, Biochemistry, Exon, alternative splicing, proteomics, RNA interference, FXR1, fragile X mental retardation syndrome-related protein 1, HUVEC, human umbilical vein endothelial cell, DEG, differentially expressed gene, Human Umbilical Vein Endothelial Cells, Humans, RNA-Seq, Molecular Biology, GO, gene ontology, Histone Acetyltransferases, KD, knockdown, G-quadruplex, PIR, percent intron retention, Alternative splicing, Intron, Cell Biology, FMR1, fragile X mental retardation 1, WTAP, Wilms’ tumor 1-associating protein, m6A, N6-methyladenosine, Exon skipping, Cell biology, WTAP, RIP, RNA coimmunoprecipitation, G-Quadruplexes, HEK293 Cells, SR, serine-rich, Multiprotein Complexes, RNA splicing, cell cycle, CpG Islands, AS, alternative splicing, RNA Splicing Factors, Minigene, Research Article

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a75a0e73b4f04a13642d9f9cd4d5690aTest
http://europepmc.org/articles/PMC8605363Test

2

Loss of O-GlcNAcase catalytic activity leads to defects in mouse embryogenesis

المؤلفون: Villő Muha, Lydia Teboul, Florence Authier, Sara Johnson, Zsombor Szoke-Kovacs, Daan M. F. van Aalten, Rory J. McCrimmon, Jennifer E. Gallagher, Alison D. McNeilly

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, Male, medicine.disease_cause, Biochemistry, Mice, O-GlcNAcylation, Pregnancy, Catalytic Domain, Aspartic acid, microCT, microcomputed tomography, Homeostasis, ID, intellectual disability, Histone Acetyltransferases, Alanine, chemistry.chemical_classification, Mutation, Mice, Inbred BALB C, biology, Chemistry, in vivo imaging, Embryo, Phenotype, beta-N-Acetylhexosaminidases, Cell biology, mESC, mouse embryonic stem cell, Female, AD, Alzheimer's disease, Research Article, embryo, Embryonic Development, perinatal lethality, CpOGA, clostridium perfringens O-GlcNAcase, N-Acetylglucosaminyltransferases, 03 medical and health sciences, glycobiology, medicine, Animals, Molecular Biology, development, microcomputed tomography, 030102 biochemistry & molecular biology, Cell Biology, Histone acetyltransferase, OGT, O-GlcNAc transferase, X-Ray Microtomography, O-GlcNAcase, CDG, congenital disorder of glycosylation, mouse genetics, Mice, Inbred C57BL, 030104 developmental biology, Enzyme, OGA, O-GlcNAcase, biology.protein, HAT, histone acetyltransferase, Protein Processing, Post-Translational

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9431406ba98edf1c449e766a30687087Test
http://europepmc.org/articles/PMC7988489Test

3

دورية أكاديمية

Tip60 acetyltransferase activity is controlled by phosphorylation.

المؤلفون: Lemercier, Claudie, Legube, Gaëlle, Caron, Cécile, Louwagie, Mathilde, Garin, Jérôme, Trouche, Didier, Khochbin, Saadi

المساهمون: Biologie moléculaire et cellulaire de la différenciation, Université Joseph Fourier - Grenoble 1 (UJF)-Institut Albert Bonniot-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de biologie moléculaire eucaryote (LBME), Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de chimie des protéines, Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)

المصدر: ISSN: 0021-9258.

مصطلحات موضوعية: MESH: Acetyltransferases, MESH: Amino Acid Sequence, MESH: Phosphorylation, MESH: Serine, MESH: Enzyme Activation, MESH: G2 Phase, MESH: Hela Cells, MESH: Histone Acetyltransferases, MESH: Histones, MESH: Humans, MESH: Molecular Sequence Data, MESH: Mutation, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology

العلاقة: info:eu-repo/semantics/altIdentifier/pmid/12468530; hal-00380484; https://hal.science/hal-00380484Test; https://hal.science/hal-00380484/documentTest; https://hal.science/hal-00380484/file/Lemercier_Tip60_JBC_2003.pdfTest; PUBMED: 12468530

الإتاحة: https://doi.org/10.1074/jbc.M211811200Test
https://hal.science/hal-00380484Test
https://hal.science/hal-00380484/documentTest
https://hal.science/hal-00380484/file/Lemercier_Tip60_JBC_2003.pdfTest

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4

دورية أكاديمية

Kinase activity and phosphorylation of the largest subunit of TFIIF transcription factor.

المؤلفون: Rossignol, M., Keriel, Anne, Staub, A, Egly, J

المساهمون: Institut National de la Santé et de la Recherche Médicale (INSERM)

المصدر: ISSN: 0021-9258.

مصطلحات موضوعية: MESH: Amino Acid Sequence, MESH: Animals, MESH: Transcription Factors, TFII, MESH: Transcription, Genetic, MESH: Casein Kinase II, MESH: DNA Mutational Analysis, MESH: DNA-Binding Proteins, MESH: Histone Acetyltransferases, MESH: Humans, MESH: Molecular Sequence Data, MESH: Nuclear Proteins, MESH: Phosphorylation, MESH: Protein-Serine-Threonine Kinases, MESH: Recombinant Proteins, MESH: Spodoptera, MESH: Substrate Specificity, MESH: TATA-Binding Protein Associated Factors, MESH: Transcription Factor TFIID, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases

العلاقة: info:eu-repo/semantics/altIdentifier/pmid/10428810; hal-01994360; https://hal.umontpellier.fr/hal-01994360Test; https://hal.umontpellier.fr/hal-01994360/documentTest; https://hal.umontpellier.fr/hal-01994360/file/PIIS0021925818815538.pdfTest; PUBMED: 10428810

الإتاحة: https://doi.org/10.1074/jbc.274.32.22387Test
https://hal.umontpellier.fr/hal-01994360Test
https://hal.umontpellier.fr/hal-01994360/documentTest
https://hal.umontpellier.fr/hal-01994360/file/PIIS0021925818815538.pdfTest

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5

Histone acetyltransferase 7 (KAT7)-dependent intragenic histone acetylation regulates endothelial cell gene regulation

المؤلفون: Xiao-Yan Wen, Youdong Wang, J.J. David Ho, Philip A. Marsden, Paul J. Turgeon, Hon-Sum Jeffrey Man, Suzan El-Rass, Matthew S. Yan, Michelle K. Dubinsky

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00abab6328d5f55032e47ec7e1fedaedTest
https://europepmc.org/articles/PMC5868248Test/

6

The 19S proteasome is directly involved in the regulation of heterochromatin spreading in fission yeast

المؤلفون: Daeyoup Lee, Hogyu David Seo, Minhoo Kim, Takeshi Urano, Keunsoo Kang, Yoonjung Choi

مصطلحات موضوعية: 0301 basic medicine, Cytoplasm, Proteasome Endopeptidase Complex, Euchromatin, Heterochromatin, Biochemistry, chromatin regulation, epigenetics, heterochromatin, proteasome, RNA interference (RNAi), 19S RP, Epe1, RNAi, heterochromatin spreading, non-proteolytic function, 03 medical and health sciences, RNA interference, Schizosaccharomyces, Transcriptional regulation, Editors' Picks, Epigenetics, Molecular Biology, Histone Acetyltransferases, Genetics, biology, Nuclear Proteins, Cell Biology, Cell biology, 030104 developmental biology, Histone, Proteasome, Mutation, Proteolysis, biology.protein, Editors' Picks Highlights, Heterochromatin protein 1, RNA Polymerase II, Schizosaccharomyces pombe Proteins

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a65fb8a6eda726444d337f90dd6cf436Test
https://europepmc.org/articles/PMC5641893Test/

7

O-GlcNAcase Is an RNA Polymerase II Elongation Factor Coupled to Pausing Factors SPT5 and TIF1β*

المؤلفون: Brian A. Lewis, Brian J. Abraham, Melissa Resto, Bong Hyun Kim, Alfonso G. Fernandez, Keji Zhao

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb0f84d85297a8e8f2e4d3ff2016c0e2Test
https://europepmc.org/articles/PMC5077205Test/

8

Subunits of ADA-two-A-containing (ATAC) or Spt-Ada-Gcn5-acetyltrasferase (SAGA) Coactivator Complexes Enhance the Acetyltransferase Activity of GCN5*

المؤلفون: Anne Riss, Mathilde Joint, Simon Trowitzsch, Elisabeth Scheer, Imre Berger, Laszlo Tora

المساهمون: Tora, Laszlo, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), European Molecular Biology Laboratory Grenoble (EMBL - Outstation ), University of Bristol [Bristol]

المصدر: Riss, A, Scheer, E, Joint, M, Trowitzsch, S, Berger, I & Tora, L 2015, ' Subunits of ADA-two-A-containing (ATAC) or Spt-Ada-Gcn 5-acetyltrasferase (SAGA) coactivator complexes enhance the acetyltransferase activity of GCN 5 ', Journal of Biological Chemistry, vol. 290, pp. 28997-29009 . https://doi.org/10.1074/jbc.M115.668533Test
Journal of Biological Chemistry
Journal of Biological Chemistry, 2015, 290 (48), pp.28997-29009. ⟨10.1074/jbc.M115.668533⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (48), pp.28997-29009. ⟨10.1074/jbc.M115.668533⟩

مصطلحات موضوعية: histone acetylase, Protein subunit, [SDV]Life Sciences [q-bio], KAT2A, histone, Spodoptera, Biochemistry, environment and public health, 03 medical and health sciences, chromatin modification, 0302 clinical medicine, Transcription (biology), Coactivator, parasitic diseases, Sf9 Cells, Animals, Humans, mass spectrometry (MS), Gene Regulation, human, Molecular Biology, chromatin regulation, 030304 developmental biology, Adaptor Proteins, Signal Transducing, Histone Acetyltransferases, 0303 health sciences, biology, histone acetylation, Cell Biology, Molecular biology, Cell biology, Chromatin, [SDV] Life Sciences [q-bio], DNA-Binding Proteins, enzymes and coenzymes (carbohydrates), Histone, Acetylation, 030220 oncology & carcinogenesis, Acetyltransferase, Multiprotein Complexes, biology.protein, chromatin, complex, Transcription Factors