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Journal Article
Science, ISSN 0036-8075, 5/2010, Volume 328, Issue 5981, pp. 1025 - 1029
SAGA is a transcriptional coactivator complex that is conserved across eukaryotes and performs multiple functions during transcriptional activation and... 
Proteins | Yeasts | Active sites | Ubiquitins | REPORTS | Histones | Atoms | Amino acids | Nucleosomes | Aldehydes | Zinc | COMPLEX | DOMAIN | UBP8 | CHROMATIN | NUCLEAR-PORE | UBIQUITIN | MULTIDISCIPLINARY SCIENCES | SUS1 | DEUBIQUITYLATION | MESSENGER-RNA EXPORT | ASSOCIATION | Transcription Factors - chemistry | Histone Acetyltransferases - chemistry | Nucleosomes - chemistry | Zinc - metabolism | Ubiquitin - metabolism | Crystallography, X-Ray | Ubiquitins - chemistry | Aldehydes - metabolism | Trans-Activators - chemistry | Zinc - chemistry | Endopeptidases - chemistry | Ubiquitination | Histone Acetyltransferases - metabolism | Ubiquitinated Proteins - metabolism | Ubiquitins - metabolism | Protein Structure, Tertiary | Endopeptidases - metabolism | Zinc Fingers | RNA-Binding Proteins - chemistry | Ubiquitin - chemistry | Models, Molecular | Nucleosomes - metabolism | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Transcription Factors - metabolism | Models, Biological | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Conformation | Trans-Activators - metabolism | Histones - metabolism | RNA-Binding Proteins - metabolism | Aldehydes - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Ubiquitin | Physiological aspects | Transcription factors | Research | Eukaryotes | Biochemistry | Cellular biology | Proteases | Crystal structure | Index Medicus | Modules | Mathematical models | Assembly | Elongation
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2009, Volume 36, Issue 1, pp. 39 - 50
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination.... 
PROTEINS | E3 LIGASE | OXIDATIVE STRESS | PROTEIN SPOP | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | BTB DOMAIN | F-BOX | TRANSCRIPTION FACTOR | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Crystallography, X-Ray | Drosophila Proteins - metabolism | Mutation - physiology | Protein Multimerization - physiology | Protein Structure, Quaternary - physiology | Ubiquitination - physiology | Peptide Fragments - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Cullin Proteins - chemistry | Peptide Fragments - chemistry | Phosphoprotein Phosphatases - genetics | Consensus Sequence - physiology | Recombinant Fusion Proteins - genetics | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Phosphoprotein Phosphatases - chemistry | Protein Binding - physiology | Adaptor Proteins, Signal Transducing - chemistry | Histones - chemistry | Protein Interaction Domains and Motifs - physiology | Phosphoprotein Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cullin Proteins - metabolism | Nuclear Proteins - genetics | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cullin Proteins - genetics | Transcription Factors - metabolism | Animals | Histones - genetics | Adaptor Proteins, Signal Transducing - genetics | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Chromatin | Phosphatases | Ligases | Index Medicus | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERIZATION | DIMERS | PHOSPHATASES
Journal Article
eLife, ISSN 2050-084X, 08/2014, Volume 3, Issue 2014, pp. 1 - 17
The Cdc45/Mcm2-7/GINS ( CMG) helicase separates DNA strands during replication in eukaryotes. How the CMG is assembled and engages DNA substrates remains... 
replication fork | DNA replication | helicase | motor proteins | AAA+ ATPase | Mcm2-7 | MCM2-7 HELICASE | HEXAMERIC HELICASE | MINICHROMOSOME MAINTENANCE PROTEIN | ARCHAEAL MCM | BUDDING YEAST | STRUCTURAL BASIS | BIOLOGY | REPLICATIVE HELICASE | ELECTRON-MICROSCOPY | 26S PROTEASOME | CRYO-EM STRUCTURE | Minichromosome Maintenance Proteins - metabolism | Protein Multimerization | Eukaryotic Cells - metabolism | Drosophila Proteins - metabolism | Minichromosome Maintenance Proteins - chemistry | Protein Subunits - metabolism | Cell Cycle Proteins - chemistry | DNA-Binding Proteins - metabolism | Drosophila melanogaster - metabolism | Multiprotein Complexes - metabolism | Adenosine Triphosphate - metabolism | Protein Structure, Quaternary | Repressor Proteins - metabolism | Protein Structure, Tertiary | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | DNA, Single-Stranded - metabolism | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | RNA Splicing Factors | Adenosine Triphosphatases - metabolism | Models, Molecular | DNA Replication | DNA - metabolism | Drosophila Proteins - chemistry | Microscopy, Electron | DNA-Binding Proteins - chemistry | Adenosine Triphosphate - analogs & derivatives | DNA, Single-Stranded - chemistry | Multiprotein Complexes - ultrastructure | DNA - chemistry | Multiprotein Complexes - chemistry | Animals | Protein Binding | Adenosine Triphosphatases - chemistry | Protein Subunits - chemistry | Adenosine Triphosphate - chemistry | Chromosomal Proteins, Non-Histone - chemistry | RNA-Binding Proteins - metabolism | Medical research | Single-stranded DNA | Hexamers | Electron microscopy | DNA biosynthesis | DNA helicase | Handedness | Microscopy | Insects | Cdc45 protein | Cell cycle | Polarity | Dimerization | Deoxyribonucleic acid--DNA | Adenosine triphosphatase | Index Medicus
Journal Article
Structure, ISSN 0969-2126, 10/2015, Volume 23, Issue 10, pp. 1801 - 1814
Bromodomains are epigenetic readers that are recruited to acetyllysine residues in histone tails. Recent studies have identified non-acetyl acyllysine... 
WIDESPREAD | EPIGENETIC READERS | SUCCINYLATION | ACETYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | CELL BIOLOGY | BIOPHYSICS | SMALL-MOLECULE INHIBITORS | LYSINE PROPIONYLATION | PROTEINS | ACETYLOME | POSTTRANSLATIONAL MODIFICATION | TATA-Binding Protein Associated Factors - metabolism | Transcription Factor TFIID - chemistry | Butyrates - metabolism | Transcription Factors - chemistry | Crotonates - metabolism | Histone Acetyltransferases - chemistry | Histones - chemistry | Epigenesis, Genetic | Humans | Histone Acetyltransferases - genetics | Crystallography, X-Ray | Transcription Factor TFIID - metabolism | Transcription Factor TFIID - genetics | Histone Acetyltransferases - metabolism | Escherichia coli - metabolism | Water - chemistry | Lysine - metabolism | Binding Sites | Acylation | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Crotonates - chemistry | Gene Expression | Protein Structure, Secondary | Water - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | TATA-Binding Protein Associated Factors - chemistry | Transcription Factors - genetics | TATA-Binding Protein Associated Factors - genetics | Transcription Factors - metabolism | Histones - genetics | Escherichia coli - genetics | Butyrates - chemistry | Protein Array Analysis | Protein Binding | Protein Processing, Post-Translational | Histones - metabolism | Kinetics | Lysine - chemistry | Peptides | Epigenetic inheritance | Index Medicus
Journal Article
Nature Structural & Molecular Biology, ISSN 1545-9993, 10/2010, Volume 17, Issue 10, pp. 1247 - 1254
Inherited mutations in human PALB2 are associated with a predisposition to breast and pancreatic cancers. PALB2's tumor-suppressing effect is thought to be... 
POLY(ADP-RIBOSE) POLYMERASE | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | DOUBLE-STRAND BREAKS | HISTONE H2AX | FANCONI-ANEMIA | CELL BIOLOGY | RAD51 | BIOPHYSICS | IN-VIVO | SUSCEPTIBILITY GENE | D-LOOP FORMATION | DNA-REPAIR | Recombination, Genetic - physiology | DNA, Neoplasm - metabolism | Humans | Neoplasm Proteins - physiology | DNA Repair - physiology | Molecular Sequence Data | Structure-Activity Relationship | DNA Breaks, Double-Stranded | BRCA2 Protein - physiology | Breast Neoplasms - metabolism | Base Sequence | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Female | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Nucleic Acid Conformation | Fanconi Anemia Complementation Group N Protein | Peptide Fragments - metabolism | Neoplasm Proteins - chemistry | Nuclear Proteins - chemistry | Poly(ADP-ribose) Polymerase Inhibitors | Protein Interaction Mapping | Tumor Suppressor Proteins - physiology | Peptide Fragments - chemistry | Apoptosis Regulatory Proteins | Models, Biological | Rad51 Recombinase - chemistry | Rad51 Recombinase - physiology | BRCA2 Protein - chemistry | Nuclear Proteins - physiology | Poly (ADP-Ribose) Polymerase-1 | Breast cancer | Genetic aspects | Research | BRCA mutations | Ovarian cancer | Proteins | Mutation | Molecular biology | Prostate cancer | Index Medicus | homologous recombination | BRCA2 | PALB2
Journal Article
Nature, ISSN 0028-0836, 2013, Volume 499, Issue 7456, pp. 50 - 54
53BP1 (also called TP53BP1) is a chromatin-associated factor that promotes immunoglobulin class switching and DNA double-strand-break (DSB) repair by... 
CRB2 | RECRUITMENT | FISSION YEAST | METHYLATION | CHROMATIN | DEPENDENT RESPONSE | RESECTION | MULTIDISCIPLINARY SCIENCES | SITES | DOUBLE-STRAND BREAKS | CLASS-SWITCH RECOMBINATION | Schizosaccharomyces pombe Proteins - chemistry | Histones - chemistry | Nucleosomes - chemistry | Humans | Ubiquitin - metabolism | Molecular Sequence Data | Male | Intracellular Signaling Peptides and Proteins - metabolism | DNA Breaks, Double-Stranded | DNA-Binding Proteins - deficiency | Cell Cycle Proteins - chemistry | Intracellular Signaling Peptides and Proteins - deficiency | Ubiquitination | Schizosaccharomyces pombe Proteins - metabolism | Female | Lysine - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Schizosaccharomyces | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Signal Transduction | Cell Cycle Proteins - metabolism | Nucleosomes - metabolism | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Chromosomal Proteins, Non-Histone - deficiency | Amino Acid Motifs | Chromosomal Proteins, Non-Histone - genetics | Animals | Intracellular Signaling Peptides and Proteins - chemistry | Mutant Proteins - chemistry | Protein Binding | Mice | DNA Damage | Histones - metabolism | Tumor Suppressor p53-Binding Protein 1 | Chromosomal Proteins, Non-Histone - chemistry | Ubiquitin | Research | Properties | DNA repair | DNA damage | Proteins | DNA methylation | Mutation | Experiments | Recruitment | Index Medicus
Journal Article
Nature Chemical Biology, ISSN 1552-4450, 08/2014, Volume 10, Issue 10, pp. 810 - 812
Approximately 25% of cytoplasmic tRNAs in eukaryotic organisms have the wobble uridine (U34) modified at C5 through a process that, according to genetic... 
DOMAIN | PROTEIN | POLYMERASE-II HOLOENZYME | BIOCHEMISTRY & MOLECULAR BIOLOGY | HISTONE ACETYLTRANSFERASE | SACCHAROMYCES-CEREVISIAE | ELONGATOR COMPLEX | EXPRESSION | SAM | Histone Acetyltransferases - chemistry | Archaeal Proteins - chemistry | Histone Acetyltransferases - genetics | Molecular Sequence Data | S-Adenosylmethionine - chemistry | Protein Subunits - metabolism | Nerve Tissue Proteins - chemistry | Histone Acetyltransferases - metabolism | Escherichia coli - metabolism | Conserved Sequence | Free Radicals - metabolism | Archaeal Proteins - genetics | RNA, Transfer - chemistry | Methanocaldococcus - chemistry | Uridine - chemistry | Protein Subunits - genetics | Archaeal Proteins - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Gene Expression | Biocatalysis | Free Radicals - chemistry | RNA, Transfer - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Escherichia coli - genetics | Methanocaldococcus - enzymology | Saccharomyces cerevisiae Proteins - metabolism | Uridine - metabolism | Protein Subunits - chemistry | Structural Homology, Protein | S-Adenosylmethionine - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Eukaryotes | Biocatalysts | Cytoplasm | Transfer RNA | Index Medicus
Journal Article