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Nature, ISSN 0028-0836, 09/2012, Volume 489, Issue 7415, pp. 313 - 317
Cornelia de Lange syndrome (CdLS) is a dominantly inherited congenital malformation disorder, caused by mutations in the cohesin-loading protein NIPBL1,2 for... 
SISTER-CHROMATID COHESION | NIPPED-B | COMPLEX | NIPBL | HUMAN GENOME | RNA-SEQ | MULTIDISCIPLINARY SCIENCES | X-CHROMOSOME-INACTIVATION | S-PHASE | PROTEINS | BINDING | Chromatin - metabolism | Chondroitin Sulfate Proteoglycans - chemistry | Humans | Crystallography, X-Ray | Male | Phosphoproteins - metabolism | Cell Cycle Proteins - chemistry | Chromatin Immunoprecipitation | Repressor Proteins - deficiency | De Lange Syndrome - metabolism | Fibroblasts | Female | Transcription, Genetic | Acetylation | Binding Sites | Repressor Proteins - metabolism | De Lange Syndrome - genetics | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | Histone Deacetylases - genetics | Cell Cycle Proteins - metabolism | Chondroitin Sulfate Proteoglycans - metabolism | Histone Deacetylases - chemistry | Histone Deacetylases - deficiency | Mutant Proteins - genetics | Prophase | Models, Molecular | Repressor Proteins - genetics | Histone Deacetylases - metabolism | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | Mutation - genetics | Proteins - genetics | Mutant Proteins - chemistry | Protein Conformation | HeLa Cells | Adaptor Proteins, Signal Transducing - metabolism | Anaphase | Chromatin - genetics | Chromosomal Proteins, Non-Histone - chemistry | Genetics | De Lange syndrome | Genetic aspects | Research | Mutation (Biology) | Proteins | Cell culture | Genes | Cell cycle | Mutation | Females | Chromosomes | Crystal structure | Index Medicus | Chromatin | Repressor Proteins | Life Sciences | Phosphoproteins | Chromosomal Proteins, Non-Histone | Histone Deacetylases | De Lange Syndrome | Chondroitin Sulfate Proteoglycans | Nuclear Proteins | Mutant Proteins | Adaptor Proteins, Signal Transducing | Development Biology | Cell Cycle Proteins
Journal Article
Nature, ISSN 0028-0836, 11/2010, Volume 468, Issue 7322, pp. 400 - 405
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
Cell, ISSN 0092-8674, 03/2007, Volume 128, Issue 6, pp. 1063 - 1076
Methylation of histones has been regarded as a stable modification defining the epigenetic program of the cell, which regulates chromatin structure and... 
DOMAIN-CONTAINING PROTEINS | METHYLATION | CAENORHABDITIS-ELEGANS | METHYLTRANSFERASE | GENE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCAPES X-INACTIVATION | TRITHORAX | RETINOBLASTOMA-BINDING PROTEIN-2 | TRANSCRIPTIONAL REGULATION | CELL BIOLOGY | Caenorhabditis elegans Proteins - chemistry | Humans | Intracellular Signaling Peptides and Proteins - metabolism | Phylogeny | Gene Deletion | Tumor Suppressor Proteins - chemistry | Oxidoreductases, N-Demethylating - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Repressor Proteins - genetics | Caenorhabditis elegans - embryology | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Histone Demethylases | Lysine | Drosophila melanogaster - enzymology | Schizosaccharomyces - enzymology | Mice | Histones - metabolism | Caenorhabditis elegans Proteins - genetics | Caenorhabditis elegans - enzymology | Embryonic Stem Cells - metabolism | Oxidoreductases, N-Demethylating - genetics | Caenorhabditis elegans Proteins - metabolism | Molecular Sequence Data | DNA-Binding Proteins - metabolism | Tumor Suppressor Proteins - genetics | Carrier Proteins - chemistry | Nuclear Proteins - genetics | Genes, Homeobox | Protein Structure, Tertiary | Repressor Proteins - chemistry | Embryonic Stem Cells - enzymology | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | Oxidoreductases, N-Demethylating - chemistry | Proteins - genetics | Carrier Proteins - genetics | Sequence Alignment | Animals | Carrier Proteins - metabolism | Proteins - metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Retinoblastoma-Binding Protein 2 | Proteins - chemistry | Methylation | Jumonji Domain-Containing Histone Demethylases | Index Medicus
Journal Article
BBA - Biomembranes, ISSN 0005-2736, 11/2016, Volume 1858, Issue 11, pp. 2709 - 2716
Phosphatidic acid (PA) is a crucial membrane phospholipid involved in de novo lipid synthesis and numerous intracellular signaling cascades. The signaling... 
PA target proteins | Epsin-like clathrin adaptor (ECA) | Membrane curvature stress | Type I and type II lipids | PA-binding | Phosphatidic acid | Liposome binding assays | TARGET | DIACYLGLYCEROL | PHOSPHOLIPASE-D | LIPID POLYMORPHISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | BIOPHYSICS | LYSOPHOSPHATIDIC ACID | ARABIDOPSIS | IONIZATION | HYDROGEN BOND SWITCH | MODULATION | Qb-SNARE Proteins - chemistry | 3-Phosphoinositide-Dependent Protein Kinases - chemistry | Humans | Qb-SNARE Proteins - metabolism | Adaptor Proteins, Vesicular Transport - metabolism | Recombinant Fusion Proteins - metabolism | Arabidopsis Proteins - metabolism | Cell Membrane - chemistry | Qc-SNARE Proteins - metabolism | Proto-Oncogene Proteins c-raf - chemistry | Biological Assay | Carrier Proteins - chemistry | Adaptor Proteins, Vesicular Transport - chemistry | Cell Membrane - metabolism | Cell Membrane - drug effects | Repressor Proteins - metabolism | Lysophosphatidylcholines - pharmacology | Repressor Proteins - chemistry | Arabidopsis - chemistry | 3-Phosphoinositide-Dependent Protein Kinases - metabolism | Recombinant Fusion Proteins - chemistry | Proto-Oncogene Proteins c-raf - metabolism | Saccharomyces cerevisiae - chemistry | Liposomes - chemistry | Carrier Proteins - metabolism | Arabidopsis Proteins - chemistry | Phosphatidic Acids - chemistry | Qc-SNARE Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Liposomes - metabolism | Phosphatidic Acids - metabolism | Phosphatidylethanolamines - metabolism | Phosphatidylethanolamines - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Arabidopsis thaliana | Chemical properties | Binding proteins | Membrane proteins | Protein binding | Plant physiology | Analysis | Phospholipids
Journal Article
Nature, ISSN 0028-0836, 12/2010, Volume 468, Issue 7325, pp. 790 - 795
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
Science, ISSN 0036-8075, 9/2011, Volume 333, Issue 6048, pp. 1445 - 1449
Bacterial chromosomes are confined in submicrometer-sized nucleoids. Chromosome organization is facilitated by nucleoid-associated proteins (NAPs), but the... 
Proteins | Molecules | DNA | Genes | Imaging | REPORTS | Cell lines | Genetic loci | Gene expression regulation | Genomes | Chromosomes | CELLS | STRUCTURING PROTEIN | CAULOBACTER-CRESCENTUS | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | GENE-EXPRESSION | OPTICAL RECONSTRUCTION MICROSCOPY | H-NS PROTEIN | BINDING | GENOME | Molecular Chaperones - metabolism | DNA, Bacterial - metabolism | Factor For Inversion Stimulation Protein - metabolism | Fimbriae Proteins - metabolism | Protein Multimerization | DNA, Bacterial - chemistry | Genetic Loci | Recombinant Fusion Proteins - metabolism | Escherichia coli K12 - ultrastructure | DNA-Binding Proteins - metabolism | Integration Host Factors - metabolism | Chromosomes, Bacterial - metabolism | Escherichia coli K12 - metabolism | Cell Division | Nucleic Acid Conformation | Binding Sites | Repressor Proteins - metabolism | Protein Structure, Tertiary | Genome, Bacterial | Repressor Proteins - chemistry | Operon | Repressor Proteins - genetics | Escherichia coli Proteins - metabolism | Chromosomes, Bacterial - ultrastructure | Fimbriae Proteins - genetics | Escherichia coli Proteins - genetics | Fimbriae Proteins - chemistry | Escherichia coli K12 - genetics | Escherichia coli Proteins - chemistry | Gene Expression Regulation, Bacterial | Cellular proteins | Research | Properties | Bacterial genetics | E coli | Microbiology | Bacterial proteins | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2007, Volume 104, Issue 52, pp. 20749 - 20752
Journal Article