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FEBS Letters, ISSN 0014-5793, 2005, Volume 579, Issue 22, pp. 5007 - 5012
Human Topors, which was originally identified as cellular binding partner of DNA topoisomerase I and of p53, has recently been shown to function as an... 
RING finger | E3 ligase | Topors | Small ubiquitin-like modifier | p53 | YFP | SUMO | UBC9 | HCMV | GST | green fluorescent protein | human cytomegalovirus | PIAS | GFP | small ubiquitin-like modifier | glutathione S-transferase | yellow fluorescent protein | ubiquitin conjugating enzyme 9 | protein inhibitors of activated STAT | LOCALIZATION | COACTIVATOR | UBIQUITIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-PROTEIN | TOPOISOMERASE-I | SUMOYLATION | CELL BIOLOGY | CONJUGATION | BIOPHYSICS | GENE-EXPRESSION | TUMOR-SUPPRESSOR | Humans | Neoplasm Proteins - metabolism | Recombinant Fusion Proteins - metabolism | Tumor Suppressor Protein p53 - genetics | DNA-Binding Proteins - metabolism | SUMO-1 Protein - genetics | Neoplasm Proteins - genetics | Nuclear Proteins - genetics | Zinc Fingers | DNA Topoisomerases, Type I - metabolism | DNA Topoisomerases, Type I - genetics | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | Nuclear Proteins - metabolism | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Transcription Factors - metabolism | Carrier Proteins - genetics | Carrier Proteins - metabolism | Protein Binding | Recombinant Fusion Proteins - genetics | SUMO-1 Protein - metabolism | HeLa Cells | In Vitro Techniques | Ubiquitin-Protein Ligases - genetics | Proteins | Sumo | Glutathione transferase | Ligases | DNA topoisomerase I | Fluorescence | Glutathione
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2018, Volume 115, Issue 45, pp. 11637 - 11642
The structurally conserved but sequence-unrelated MAX (Magnaporthe oryzae avirulence and ToxB-like) effectors AVR1-CO39 and AVR-PikD from the blast fungus M.... 
Magnaporthe oryzae | Immune receptor | Effector | Plant immunity | Rice | TRANSCRIPTION FACTORS | CRYSTALLIZATION | MULTIDISCIPLINARY SCIENCES | effector | rice | AVR1-CO39 | DECOY | MAGNAPORTHE-ORYZAE | AVR-PIA | TARGETS | immune receptor | PATHOGEN EFFECTORS | plant immunity | DISEASE RESISTANCE | Fungal Proteins - chemistry | Virulence Factors - genetics | Plant Diseases - immunology | Crystallography, X-Ray | Plant Diseases - microbiology | NLR Proteins - immunology | Host-Pathogen Interactions - immunology | Oryza - genetics | Plant Proteins - chemistry | Oryza - microbiology | Cloning, Molecular | Escherichia coli - metabolism | Magnaporthe - pathogenicity | Plant Diseases - genetics | Protein Interaction Domains and Motifs | Binding Sites | Magnaporthe - genetics | Oryza - immunology | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | Plant Immunity - genetics | NLR Proteins - genetics | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Plant Proteins - immunology | Recombinant Proteins - genetics | Virulence Factors - chemistry | Fungal Proteins - genetics | NLR Proteins - chemistry | Plant Proteins - genetics | Host-Pathogen Interactions - genetics | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Virulence Factors - metabolism | Fungal Proteins - metabolism | Ascomycota | Fungi | Physiological aspects | Observations | Binding sites (Biochemistry) | Life Sciences | Biomolecules | Vegetal Biology | Biochemistry, Molecular Biology | Biological Sciences
Journal Article
Biochemical Journal, ISSN 0264-6021, 01/2007, Volume 401, Issue 2, pp. 377 - 390
Small GTPases are involved in the control of diverse cellular behaviours, including cellular growth, differentiation and motility. In addition, recent studies... 
G-protein | Cell polarity | Directional sensing | Eukaryotic chemotaxis | Cellular motility | LIGHT-CHAIN KINASE | RHO-FAMILY GTPASES | II HEAVY-CHAIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHOSPHOINOSITIDE 3-KINASE ACTIVITY | MYOSIN-II | directional sensing | MEDIATES RAP1-INDUCED ADHESION | cellular motility | ADENYLYL-CYCLASE | PLECKSTRIN HOMOLOGY DOMAIN | NUCLEOTIDE EXCHANGE FACTOR | DICTYOSTELIUM-DISCOIDEUM | cell polarity | eukaryotic chemotaxis | GTP-Binding Proteins - physiology | Guanine Nucleotide Exchange Factors - physiology | GTP Phosphohydrolases - physiology | Actins - metabolism | Microtubules - physiology | PTEN Phosphohydrolase - metabolism | Phosphatidylinositol 3-Kinases - metabolism | Cell Movement - physiology | Animals | Chemotaxis - physiology | Microtubules - drug effects | Cell Polarity - physiology | Myosins - metabolism | Signal Transduction - physiology | ras Proteins - physiology | 3 complex, actin-related protein 2 | ROCK, p160-Rho-associated coil-containing protein kinase | PI3K, phosphoinositide 3-kinase | SCAR, suppressor of cAMP receptor | RBD, Ras-binding domain | cAR, cAMP receptor | IQGAP1, IQ-motif-containing GTPase-activating protein 1 | Review | Arp2 | Pia, Pianissimo | WAVE2, WASP family verprolin-homologous protein 2 | DGAP1, Dictyostelium GAP1 | Gbp, cGMP-binding protein | WASP, Wiskott–Aldrich syndrome protein | GPCR, G-protein-coupled receptor | APC, adenomatous polyposis coli | F-actin, filamentous actin | Hem-1, haemopoietic protein 1 | CLIP170, cytoplasmic linker protein-170 | MTOC, microtubule-organizing centre | GEF, guanine-nucleotide-exchange factor | MDia, formin protein mammalian homologue of Diaphanous | CRAC, cytosolic regulator of adenylate cyclase | RIP3, Ras-interacting protein 3 | PAK, p21-activated kinase | ERK2, extracellular-signal-regulated kinase 2 | MLC, myosin light chain | 3 complex | Epac1, exchange protein activated by cAMP-1 | MHC, myosin heavy chain | PH, pleckstrin homology | MHCK, MHC kinase | PTEN, phosphatase and tensin homologue deleted on chromosome ten | cdc42, cell-division cycle 42 | TORC2, target of rapamycin complex 2 | ACA, adenylate cyclase for aggregation | GAP, GTPase-activating protein | MLCK, MLC kinase | Gβγ, a subunit of heterotrimeric G-proteins | PDGF, platelet-derived growth factor
Journal Article
Genes and Development, ISSN 0890-9369, 12/2001, Volume 15, Issue 23, pp. 3088 - 3103
The Wnt-responsive transcription factor LEF1 can activate transcription in association with beta -catenin and repress transcription in association with... 
SUMO | Nuclear matrix | PIAS | PML bodies | LEF1/TCF | TRANSLOCATION | ACTIVATION | nuclear matrix | TRANSCRIPTIONAL REPRESSION | DEVELOPMENTAL BIOLOGY | RAR-ALPHA | PML | LEFI/TCF | INHIBITION | GENE | DNA | GENETICS & HEREDITY | PROTEINS | WNT | Nuclear Matrix - genetics | Humans | DNA-Binding Proteins - metabolism | Lymphoid Enhancer-Binding Factor 1 | Poly-ADP-Ribose Binding Proteins | Chromosomes - metabolism | Transcription, Genetic | Electrophoretic Mobility Shift Assay | Nuclear Matrix - metabolism | Cell Line | DNA-Binding Proteins - antagonists & inhibitors | Mutagenesis, Site-Directed | Signal Transduction | Small Ubiquitin-Related Modifier Proteins - metabolism | Gene Expression Regulation | Intracellular Signaling Peptides and Proteins | Ligases - metabolism | Transcription Factors - antagonists & inhibitors | DNA - metabolism | Protein Transport | Transcription Factors - metabolism | Ubiquitin-Protein Ligases | Microscopy, Confocal | Two-Hybrid System Techniques | Animals | Carrier Proteins - metabolism | Fluorescent Antibody Technique | Protein Binding | Mice | Organelles - metabolism | Protein Inhibitors of Activated STAT | Proteins | Ubiquitin | Ligases | Analysis | Genetic research | Physiological aspects | Genetic aspects | Genetic transcription | ubiquitin-protein ligase | LEF1 protein | PIASy protein | TCF | LEF1 | Research Paper
Journal Article
Biochemical Journal, ISSN 0264-6021, 11/2005, Volume 391, Issue 3, pp. 449 - 464
Steroid hormones are important endocrine signalling molecules controlling reproduction, development, metabolism, salt balance and specialized cellular... 
Af1 transactivation domain | Post-translational modification | Steroid receptor | Allosteric regulation | Protein-protein interaction | Protein-nucleic acid interaction | Secondary structure | protein-nucleic acid interaction | RNA-POLYMERASE-II | HUMAN ESTROGEN-RECEPTOR | HUMAN MINERALOCORTICOID RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACTIVATION FUNCTION 1 | AF1 transactivation domain | allosteric regulation | post-translational modification | TRANSCRIPTION FACTOR-TFIIF | steroid receptor | secondary structure | AMINO-TERMINAL DOMAIN | HUMAN ANDROGEN RECEPTOR | HUMAN GLUCOCORTICOID-RECEPTOR | protein-protein interaction | LIGAND-BINDING DOMAIN | HUMAN PROGESTERONE-RECEPTORS | Protein Structure, Tertiary | Animals | Receptors, Steroid - metabolism | Humans | Transcriptional Activation | Models, Molecular | Protein Binding | Protein Processing, Post-Translational | Receptors, Steroid - chemistry | SMRT, silencing mediator of retinoid and thyroid hormone receptor | protein–protein interaction | PSA, prostate-specific antigen | PIC, pre-initiation complex | SRC-1, steroid receptor co-activator 1 | Review | PR, progesterone receptor | HCA, hydrophobic cluster analysis | IF, inhibitory function | protein–nucleic acid interaction | PKB, protein kinase B | FLASH, Fas-associated huge protein | AF, activation function | SC, synergy control | SHR, steroid hormone receptor | TIF2, transcription intermediary factor 2 | GTF, general transcription factor | β, oestrogen receptor α and β respectively | TFE, trifluoroethanol | DBD, DNA-binding domain | ERα | GRIP1, glucocorticoid receptor-interacting protein 1 | TBP, TATA-binding protein | LBD, ligand-binding domain | PIAS, protein inhibitor of activated STAT | TMAO, trimethylamine-N-oxide | NCoR, nuclear receptor co-repressor | MR, mineralocorticoid receptor | NTD, N-terminal domain | GR, glucocorticoid receptor | ERE, oestrogen-response element | FTIR spectroscopy, Fourier-transform infrared spectroscopy | AR, androgen receptor | CBP, CREB (cAMP-response-element-binding protein)-binding protein | MAPK, mitogen-activated protein kinase
Journal Article
PLoS ONE, ISSN 1932-6203, 11/2012, Volume 7, Issue 11, p. e49283
GTF2IRD1 is one of the genes implicated in Williams-Beuren syndrome, a disease caused by haploinsufficiency of certain dosage-sensitive genes within a... 
PIAS PROTEINS | ZINC FINGERS | BROAD-SPECTRUM IDENTIFICATION | MENTAL-RETARDATION | SUMO CONJUGATION | MULTIDISCIPLINARY SCIENCES | WILLIAMS-BEUREN-SYNDROME | GENE FAMILY | FAMILY PROTEINS | HISTONE DEACETYLASE-3 | TFII-I | Humans | Ubiquitin - metabolism | Molecular Sequence Data | Protein Inhibitors of Activated STAT - metabolism | Trans-Activators - chemistry | Trans-Activators - physiology | Sequence Analysis, Protein | Proteolysis | HEK293 Cells | Muscle Proteins - metabolism | Lysine - metabolism | Binding Sites | Muscle Proteins - physiology | Gene Expression Regulation | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Ubiquitin - physiology | Amino Acid Motifs | Two-Hybrid System Techniques | Sequence Alignment | Ubiquitin-Conjugating Enzymes - metabolism | Sumoylation | Trans-Activators - metabolism | Muscle Proteins - chemistry | Nuclear Proteins - physiology | Lysine - chemistry | Protein Inhibitors of Activated STAT - physiology | Ubiquitin | Ligases | Protein binding | Histone deacetylase | Transcription factors | Yeast | Transcription | Genes | Genomics | Degradation | Proteins | SUMO protein | Signal transduction | Ubiquitination | Post-translation | Trends | Localization | Deoxyribonucleic acid--DNA | Enzymes | Cloning | Chromosome 7 | Gene expression | Haploinsufficiency | Medicine | Respiratory distress syndrome | Lysine | Plasmids | Proteasomes | Control stability | Binding sites | Deoxyribonucleic acid | DNA
Journal Article
Journal Article