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1. Full Text Regulation of the Stability of the Histone H2A–H2B Dimer by H2A Tyr57 Phosphorylation
by Sueoka, Takuma and Hayashi, Gosuke and Okamoto, Akimitsu
Biochemistry (Easton), ISSN 0006-2960, 09/2017, Volume 56, Issue 36, pp. 4767 - 4772
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | DNA - chemistry | Phosphorylation | Histones - chemistry | Models, Molecular | Protein Conformation | Protein Stability | Dimerization | Protein Folding | Index Medicus
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2. Full Text Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification
by Tessarz, Peter and Santos-Rosa, Helena and Robson, Sam C and Sylvestersen, Kathrine B and Nelson, Christopher J and Nielsen, Michael L and Kouzarides, Tony
Nature (London), ISSN 0028-0836, 2014, Volume 505, Issue 7484, pp. 564 - 568
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Molecular Chaperones - metabolism | Histones - chemistry | Saccharomyces cerevisiae - genetics | Humans | Methyltransferases - metabolism | Glutamine - metabolism | Molecular Sequence Data | Substrate Specificity | RNA Polymerase I - metabolism | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | Alanine - genetics | Cell Nucleolus - metabolism | Transcription, Genetic | Binding Sites | DNA, Ribosomal - genetics | RNA - metabolism | Amino Acid Sequence | Chromosomal Proteins, Non-Histone - metabolism | Nucleosomes - metabolism | Alanine - metabolism | Nuclear Proteins - metabolism | Amino Acid Motifs | Epistasis, Genetic | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Protein Processing, Post-Translational | Histones - metabolism | Methylation | Chromatin - genetics | Ribonucleoproteins, Small Nucleolar - metabolism | Physiological aspects | Covalent modifications | Research | Methyltransferases | Glutamine metabolism | Proteins | Enzymes | Cell culture | Peptides | Ribosomal DNA | DNA methylation | Genomes | Deoxyribonucleic acid--DNA | Index Medicus
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3. Full Text Structural basis of histone H2A-H2B recognition by the essential chaperone FACT
by Hondele, Maria and Stuwe, Tobias and Hassler, Markus and Halbach, Felix and Bowman, Andrew and Zhang, Elisa T and Nijmeijer, Bianca and Kotthoff, Christiane and Rybin, Vladimir and Amlacher, Stefan and Hurt, Ed and Ladurner, Andreas G
Nature (London), ISSN 0028-0836, 2013, Volume 499, Issue 7456, pp. 111 - 114
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Fungal Proteins - chemistry | Protein Structure, Tertiary | Chaetomium - chemistry | Molecular Chaperones - metabolism | Protein Structure, Secondary | Histones - chemistry | Nucleosomes - chemistry | Protein Multimerization | Models, Molecular | Nucleosomes - metabolism | Substrate Specificity | Crystallography, X-Ray | DNA Replication | DNA - metabolism | Molecular Chaperones - chemistry | Amino Acid Motifs | DNA - chemistry | Conserved Sequence | Hydrophobic and Hydrophilic Interactions | Protein Binding | Histones - metabolism | Fungal Proteins - metabolism | Histones | Genetic transcription | Research | Molecular chaperones | Structure | Proteins | Mutation | Binding sites | Deoxyribonucleic acid--DNA | Index Medicus
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4. Full Text RNF168 Ubiquitinates K13-15 on H2A/H2AX to Drive DNA Damage Signaling
by Mattiroli, Francesca and Vissers, Joseph H.A and van Dijk, Willem J and Ikpa, Pauline and Citterio, Elisabetta and Vermeulen, Wim and Marteijn, Jurgen A and Sixma, Titia K
Cell (Cambridge), ISSN 0092-8674, 09/2012, Volume 150, Issue 6, pp. 1182 - 1195
Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Protein Structure, Tertiary | Amino Acid Sequence | Histones - chemistry | Nucleosomes - chemistry | Humans | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Molecular Sequence Data | Nucleosomes - metabolism | Scattering, Small Angle | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | DNA-Binding Proteins - metabolism | X-Ray Diffraction | Lysine - metabolism | Histones - metabolism | Ubiquitin | Histones | DNA binding proteins | Ligases | DNA damage | DNA | Index Medicus
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5. Full Text The histone H2A isoform Hist2h2ac is a novel regulator of proliferation and epithelial–mesenchymal transition in mammary epithelial and in breast cancer cells
by Monteiro, Fátima Liliana and Vitorino, Rui and Wang, Jun and Cardoso, Hugo and Laranjeira, Hugo and Simões, Joana and Caldas, Margarida and Henrique, Rui and Amado, Francisco and Williams, Cecilia and Jerónimo, Carmen and Helguero, Luisa A
Cancer letters, ISSN 0304-3835, 2017, Volume 396, pp. 42 - 52
Hematology, Oncology and Palliative Medicine | Mammary epithelial cells | Histone H2A variants | Breast cancer | Epidermal growth factor | Epithelial mesenchymal transition | Hist2h2ac | Life Sciences & Biomedicine | Oncology | Science & Technology | Breast - cytology | Humans | RNA, Messenger - genetics | Cell Proliferation - physiology | Epithelial Cells - pathology | RNA, Messenger - metabolism | Breast Neoplasms - metabolism | Breast Neoplasms - genetics | Histones - genetics | Breast Neoplasms - pathology | Mass Spectrometry | Protein Isoforms | Epithelial-Mesenchymal Transition | Female | Histones - metabolism | Cell Differentiation - physiology | Chromatin | RNA | Cancer cells | Stem cells | Genetic research | Medical screening | Cell differentiation | Mass spectrometry | Index Medicus | Medicin och hälsovetenskap
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6. Full Text Structural evidence for Nap1‐dependent H2A–H2B deposition and nucleosome assembly
by Aguilar‐Gurrieri, Carmen and Larabi, Amédé and Vinayachandran, Vinesh and Patel, Nisha A and Yen, Kuangyu and Reja, Rohit and Ebong, Ima‐O and Schoehn, Guy and Robinson, Carol V and Pugh, B Franklin and Panne, Daniel
The EMBO journal, ISSN 0261-4189, 07/2016, Volume 35, Issue 13, pp. 1465 - 1482
H2A–H2B | Nap1 | nucleosome assembly | chromatin | histone chaperone | Histone chaperone | Chromatin | Nucleosome assembly | H2A-H2B | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Nucleosome Assembly Protein 1 - genetics | Nucleosome Assembly Protein 1 - metabolism | Histones - chemistry | Protein Multimerization | Models, Molecular | Nucleosomes - metabolism | Crystallography, X-Ray | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - chemistry | Saccharomyces cerevisiae - metabolism | Nucleosome Assembly Protein 1 - chemistry | Chromatin Immunoprecipitation | DNA Mutational Analysis | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Conformation | Histones - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Eukaryotes | Molecular biology | Crystal structure | Index Medicus | Life Sciences | Biomolecules | Biochemistry, Molecular Biology | Chromatin, Epigenetics, Genomics & Functional Genomics | Structural Biology
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7. Full Text Constitutive expression exposes functional redundancy between the Arabidopsis histone H2A gene HTA1 and other H2A gene family members
by Yi, HoChul and Sardesai, Nagesh and Fujinuma, Toshinori and Chan, Chien-Wei and Veena, Veena and Gelvin, Stanton B
The Plant cell, ISSN 1040-4651, 07/2006, Volume 18, Issue 7, pp. 1575 - 1589
Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Plant Sciences | Science & Technology | Cell Biology | Transformation, Genetic | Amino Acid Sequence | Promoter Regions, Genetic | Arabidopsis Proteins - genetics | Multigene Family | Histones - classification | Caulimovirus - genetics | Agrobacterium tumefaciens - genetics | Molecular Sequence Data | Plant Roots - cytology | Phylogeny | Plant Roots - microbiology | Recombinant Fusion Proteins - metabolism | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Plant Roots - physiology | Sequence Alignment | Histones - genetics | Agrobacterium tumefaciens - metabolism | Gene Expression Regulation, Plant | Recombinant Fusion Proteins - genetics | Histones - metabolism | Arabidopsis Proteins - classification | Plant proteins | Genetic aspects | Research | Gene expression | Arabidopsis | Index Medicus
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8. Full Text Phosphorylation of Histone H2A at Serine 95
: A Plant-Specific Mark Involved in Flowering Time Regulation and H2A.Z Deposition
by Yanhua Su and Shiliang Wang and Fei Zhang and Han Zheng and Yanan Liu and Tongtong Huang and Yong Ding
The Plant cell, ISSN 1040-4651, 9/2017, Volume 29, Issue 9, pp. 2197 - 2213
RESEARCH ARTICLES | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Plant Sciences | Science & Technology | Cell Biology | Amino Acid Sequence | Phosphorylation | Histones - chemistry | Photoperiod | Mutation - genetics | Phosphoserine - metabolism | Genetic Complementation Test | Promoter Regions, Genetic - genetics | Subcellular Fractions - metabolism | Protein Subunits - metabolism | Arabidopsis - metabolism | Arabidopsis - genetics | Time Factors | Gene Expression Regulation, Plant | Protein Binding | Flowers - physiology | Acetylation | Histones - metabolism | Arabidopsis thaliana | Plants, Flowering of | Analysis | Serine | Histones | Physiological aspects | Genetic aspects | Gene expression | Circadian rhythms | Chromatin | Phenotypes | Histone H2A | Transcription | Kinases | Histone H4 | Flowering | Mutation | Deposition | Adenosine triphosphatase | Histone H3 | Index Medicus
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9. Full Text Histone h2a monoubiquitination promotes histone h3 methylation in polycomb repression
by Kalb, R and Latwiel, S and Baymaz, H.I and Jansen, P. W and Muller, C.W and Vermeulen, M and Muller, J
Nature structural & molecular biology, ISSN 1545-9993, 2014, Volume 21, Issue 6, pp. 569 - 571
Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Ubiquitination | Animals | Epigenetic Repression | Polycomb-Group Proteins - genetics | Histones - metabolism | Methylation | Drosophila - genetics | Histones | Genetic research | Genetic aspects | Research | Properties | Ubiquitin-proteasome system | Gene expression | Proteins | DNA methylation | Binding sites | Index Medicus
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10. Full Text Transcriptional repression by PRC1 in the absence of H2A monoubiquitylation
by Pengelly, Ana Raquel and Kalb, Reinhard and Finkl, Katja and Müller, Jürg
Genes & development, ISSN 0890-9369, 07/2015, Volume 29, Issue 14, pp. 1487 - 1492
H2A and H2Av monoubiquitylation | Polycomb | PRC1 | Drosophila | Transcriptional repression | Genetics & Heredity | Life Sciences & Biomedicine | Developmental Biology | Science & Technology | Cell Biology | Polycomb Repressive Complex 1 - metabolism | Ubiquitin-Protein Ligases - metabolism | Gene Expression Regulation, Developmental - genetics | Drosophila Proteins - metabolism | Polycomb Repressive Complex 1 - genetics | Ubiquitination | Animals | Histones - genetics | Metamorphosis, Biological - genetics | Drosophila - embryology | Drosophila Proteins - genetics | Histones - metabolism | Mutation | Drosophila - genetics | Histones | Genetic transcription | Research | Ubiquitin-proteasome system | Mutation (Biology) | Index Medicus | Research Communication | transcriptional repression
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