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Nature Cell Biology, ISSN 1465-7392, 05/2008, Volume 10, Issue 5, pp. 538 - 546
Journal Article
Nature Genetics, ISSN 1061-4036, 12/2012, Volume 44, Issue 12, pp. 1310 - 1315
Journal Article
Nature Structural and Molecular Biology, ISSN 1545-9993, 07/2016, Volume 23, Issue 7, pp. 647 - 655
The opposing activities of 53BP1 and BRCA1 influence pathway choice in DNA double-strand-break repair. How BRCA1 counteracts the inhibitory effect of 53BP1 on... 
STRAND BREAK REPAIR | RING-RING COMPLEX | TUMOR SUPPRESSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | REPAIR PATHWAY CHOICE | BRCA1 | REMODELING ENZYME | CELL BIOLOGY | E3 LIGASE | BIOPHYSICS | END RESECTION | HOMOLOGOUS RECOMBINATION | FUN30 | Chromatin - metabolism | DNA, Neoplasm - metabolism | Humans | Gene Expression Regulation, Neoplastic | Ubiquitin - metabolism | DNA Breaks, Double-Stranded | Ubiquitination - drug effects | BRCA1 Protein - metabolism | Tumor Suppressor Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Binding Sites | Chromatin - drug effects | DNA Helicases - genetics | Chromatin - chemistry | Tumor Suppressor p53-Binding Protein 1 - metabolism | Recombinant Proteins - metabolism | Gene Expression | Recombinational DNA Repair | Tumor Suppressor Proteins - metabolism | Tumor Suppressor p53-Binding Protein 1 - genetics | Signal Transduction | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Recombinant Proteins - genetics | Ubiquitin - genetics | Piperazines - pharmacology | DNA Cleavage - drug effects | BRCA1 Protein - genetics | DNA Helicases - metabolism | Phthalazines - pharmacology | Histones - genetics | Escherichia coli - genetics | Protein Binding | DNA, Neoplasm - genetics | HeLa Cells | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Camptothecin - pharmacology | Breast cancer | BRCA mutations | DNA repair | Analysis | Risk factors | Enzymes | Protein expression | Chromatin | DNA damage | Index Medicus
Journal Article
Journal Article
Plant Physiology, ISSN 0032-0889, 10/2012, Volume 160, Issue 2, pp. 1011 - 1022
MdMYB1 is a crucial regulator of light-induced anthocyanin biosynthesis and fruit coloration in apple (Malus domestica). In this study, it was found that... 
Callus | Colors | SYSTEMS BIOLOGY, MOLECULAR BIOLOGY, AND GENE REGULATION | Genes | Monoclonal antibodies | Antibodies | Gene expression regulation | Biosynthesis | Plants | Transgenic plants | Plant cells | UV-B | PLANT | PERCEPTION | COP1-MEDIATED DEGRADATION | COP1 | MYB TRANSCRIPTION FACTOR | ARABIDOPSIS | ACCUMULATION | AGROBACTERIUM-MEDIATED TRANSFORMATION | DEPENDENT GENE-EXPRESSION | PLANT SCIENCES | Darkness | Arabidopsis - enzymology | Immunoprecipitation | Genes, Plant | DNA, Complementary - genetics | Anthocyanins - biosynthesis | Fruit - enzymology | Malus - radiation effects | Ubiquitination | Proteolysis | Cloning, Molecular - methods | Gene Expression Regulation, Plant | Protein Stability | Plants, Genetically Modified - genetics | Color | Plants, Genetically Modified - enzymology | Ubiquitin-Protein Ligases - metabolism | Genetic Vectors - metabolism | Malus - enzymology | Enzyme Assays | Transcription Factors - genetics | Pigmentation | Genetic Vectors - genetics | Malus - genetics | Protein Interaction Mapping | Arabidopsis - genetics | Proteasome Endopeptidase Complex - genetics | Transcription Factors - metabolism | Two-Hybrid System Techniques | Enzyme Activation | Proteasome Endopeptidase Complex - metabolism | Ubiquitin-Protein Ligases - genetics | DNA, Complementary - metabolism | Ubiquitin | Anthocyanin | Apple | Ligases | Phytochemistry | Physiological aspects | Research | Health aspects | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 2012, Volume 488, Issue 7413, pp. 665 - 669
LGR5+ stem cells reside at crypt bottoms, intermingled with Paneth cells that provide Wnt, Notch and epidermal growth factor signals. Here we find that the... 
IN-VITRO | INHIBITION | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTION | UBIQUITYLATION | SMALL-INTESTINE | COLON | BETA-CATENIN | LGR5 | CANCER | NEGATIVE REGULATOR | Oncogene Proteins - genetics | Receptors, Wnt - antagonists & inhibitors | Cell Proliferation | Receptors, G-Protein-Coupled - metabolism | Humans | Ubiquitin - metabolism | Paneth Cells - pathology | Stem Cells - cytology | Receptors, Wnt - metabolism | Stem Cells - metabolism | DNA-Binding Proteins - deficiency | Adenoma - metabolism | DNA-Binding Proteins - metabolism | Endocytosis | Ubiquitination | Lysosomes - metabolism | Stem Cells - enzymology | Tumor Suppressor Proteins - deficiency | Organoids - metabolism | Tumor Suppressor Proteins - genetics | HEK293 Cells | Colorectal Neoplasms - metabolism | Paneth Cells - metabolism | Tumor Suppressor Proteins - metabolism | Organoids - pathology | Oncogene Proteins - metabolism | Organoids - cytology | Ubiquitin-Protein Ligases - metabolism | Frizzled Receptors - metabolism | DNA-Binding Proteins - genetics | beta Catenin - metabolism | Animals | Wnt Signaling Pathway - drug effects | Adenoma - pathology | Ubiquitin-Protein Ligases - deficiency | Oncogene Proteins - deficiency | Mice | Receptors, G-Protein-Coupled - genetics | Colorectal Neoplasms - pathology | Ubiquitin-Protein Ligases - genetics | Ubiquitin | Colorectal cancer | Physiological aspects | Development and progression | Research | Gene expression | Risk factors | Proteins | Epidermal growth factor | Mutation | Kinases | Rodents | Stem cells | Index Medicus
Journal Article
Journal Article
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