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Nature, ISSN 0028-0836, 2014, Volume 508, Issue 7497, pp. 550 - 553
Journal Article
Nature, ISSN 0028-0836, 06/2017, Volume 546, Issue 7659, pp. 504 - 509
ABCG2 is a constitutively expressed ATP-binding cassette (ABC) transporter that protects many tissues against xenobiotic molecules. Its activity affects the... 
BINDING CASSETTE TRANSPORTER | SUBSTRATE | MULTIDISCIPLINARY SCIENCES | RESISTANCE-ASSOCIATED PROTEIN | MONOCLONAL-ANTIBODY | IDENTIFICATION | CANCER | EXPRESSION | RECONSTITUTION | P-GLYCOPROTEIN | ATPASE SUBUNIT | Immunoglobulin Fab Fragments - ultrastructure | Antibodies - chemistry | Humans | Neoplasm Proteins - antagonists & inhibitors | Neoplasm Proteins - metabolism | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - metabolism | Cholesterol - chemistry | Biological Transport | Antibodies - immunology | Protein Domains | Adenosine Triphosphatases - ultrastructure | Binding Sites | Amino Acid Sequence | Neoplasm Proteins - ultrastructure | Adenosine Triphosphatases - metabolism | Antibodies - ultrastructure | Models, Molecular | Neoplasm Proteins - chemistry | Cholesterol - metabolism | Cryoelectron Microscopy | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - antagonists & inhibitors | Immunoglobulin Fab Fragments - chemistry | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - chemistry | Polymorphism, Single Nucleotide - genetics | ATP Binding Cassette Transporter, Sub-Family G, Member 2 - ultrastructure | Adenosine Triphosphatases - chemistry | Adenosine Triphosphatases - genetics | Immunoglobulin Fab Fragments - immunology | Physiological aspects | Binding proteins | Observations | Drug interactions
Journal Article
Nature, ISSN 0028-0836, 02/2017, Volume 542, Issue 7641, pp. 377 - 380
The spliceosome excises introns from pre-mRNAs in two sequential transesterifications-branching and exon ligation(1)-catalysed at a single catalytic metal site... 
2ND STEP | ANGSTROM RESOLUTION | ELECTRON CRYOMICROSCOPY | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | FUNCTIONAL INTERACTIONS | CATALYTIC CENTER | CRYO-EM STRUCTURE | SPLICING FACTOR | SITE CHOICE | PRE-MESSENGER-RNA | RNA Helicases - metabolism | Spliceosomes - chemistry | Saccharomyces cerevisiae - genetics | Cell Cycle Proteins - ultrastructure | Ribonucleoprotein, U5 Small Nuclear - metabolism | RNA Splicing Factors - chemistry | Saccharomyces cerevisiae - ultrastructure | Ribonucleoprotein, U4-U6 Small Nuclear - metabolism | Ribonucleoprotein, U4-U6 Small Nuclear - ultrastructure | RNA Helicases - ultrastructure | RNA Splicing Factors - metabolism | DNA-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Spliceosomes - metabolism | RNA Splicing | Ribonucleoproteins, Small Nuclear - ultrastructure | RNA, Small Nuclear - genetics | Protein Domains | Ribonucleoprotein, U5 Small Nuclear - ultrastructure | Adenosine Triphosphatases - ultrastructure | DEAD-box RNA Helicases - metabolism | DEAD-box RNA Helicases - chemistry | Saccharomyces cerevisiae Proteins - ultrastructure | Catalytic Domain | Biocatalysis | RNA Splice Sites - genetics | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Exons - genetics | Spliceosomes - ultrastructure | Saccharomyces cerevisiae - chemistry | Cryoelectron Microscopy | DNA-Binding Proteins - ultrastructure | RNA-Binding Proteins - ultrastructure | RNA Splicing Factors - ultrastructure | Ribonuclease H - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Adenosine - metabolism | Protein Binding | DEAD-box RNA Helicases - ultrastructure | RNA-Binding Proteins - metabolism | Ribonucleoproteins, Small Nuclear - metabolism | Saccharomyces cerevisiae Proteins - chemistry | RNA sequencing | Methods | Mutation | Catalysis | Ribonucleic acid--RNA | Binding sites | Crystal structure
Journal Article
Journal Article
Cell, ISSN 0092-8674, 02/2018, Volume 172, Issue 4, pp. 771 - 783.e18
As in eukaryotes, bacterial genomes are not randomly folded. Bacterial genetic information is generally carried on a circular chromosome with a single origin... 
SMC | bacteria | MatP | chromatin | Hi-C | genome organization | ORGANIZATION | BACTERIAL CHROMOSOME | DNA-BINDING | 3D GENOME | BACILLUS-SUBTILIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | GENE-EXPRESSION | H-NS | TOPOISOMERASE-IV | MOLECULAR-BASIS | CELL BIOLOGY | Chromosomes, Bacterial - genetics | Chromosomal Proteins, Non-Histone - metabolism | Adenosine Triphosphatases - metabolism | Repressor Proteins - genetics | Escherichia coli Proteins - metabolism | Multiprotein Complexes - genetics | DNA-Binding Proteins - genetics | Escherichia coli K12 - ultrastructure | Chromosomal Proteins, Non-Histone - genetics | DNA-Binding Proteins - metabolism | DNA-Binding Proteins - ultrastructure | Multiprotein Complexes - metabolism | Multiprotein Complexes - ultrastructure | Chromosomes, Bacterial - metabolism | Escherichia coli K12 - metabolism | Chromosomes, Bacterial - ultrastructure | Protein Structure, Quaternary | Escherichia coli Proteins - genetics | Adenosine Triphosphatases - genetics | Adenosine Triphosphatases - ultrastructure | Escherichia coli K12 - genetics | Repressor Proteins - metabolism | Bacteria | Chromatin | Escherichia coli | Genomics | Escherichia coli K12 | Life Sciences | Escherichia coli Proteins | Adenosine Triphosphatases | Multiprotein Complexes | Repressor Proteins | Chromosomal Proteins, Non-Histone | Chromosomes, Bacterial | DNA-Binding Proteins
Journal Article
Nature, ISSN 0028-0836, 11/2017, Volume 551, Issue 7682, pp. 653 - 657
Eukaryotic transcription-coupled repair (TCR) is an important and well-conserved sub-pathway of nucleotide excision repair that preferentially removes DNA... 
RNA-POLYMERASE-II | DEFOCUS | DAMAGE RECOGNITION | ELONGATION COMPLEX | MULTIDISCIPLINARY SCIENCES | RESOLUTION | VALIDATION | FACTOR CSB/ERCC6 | GROUP-B PROTEIN | MICROSCOPY | INSIGHTS | Saccharomyces cerevisiae Proteins - ultrastructure | Transcription Factors - chemistry | RNA Polymerase II - ultrastructure | Adenosine Triphosphatases - metabolism | DNA - ultrastructure | Saccharomyces cerevisiae - ultrastructure | DNA - metabolism | RNA Polymerase II - metabolism | Saccharomyces cerevisiae - chemistry | Transcription Elongation, Genetic | Cryoelectron Microscopy | DNA - genetics | Saccharomyces cerevisiae - metabolism | Transcription Factors - metabolism | DNA - chemistry | DNA Repair | Saccharomyces cerevisiae Proteins - metabolism | Protein Domains | Adenosine Triphosphatases - chemistry | Transcription, Genetic | Adenosine Triphosphatases - ultrastructure | RNA Polymerase II - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Genetic research | Research | Genetic transcription | DNA repair | Cockayne syndrome | Yeast | Transcription elongation | Saccharomyces | DNA-directed RNA polymerase | Transcription-coupled repair | Proteins | T-cell receptor | Eukaryotes | Lesions | Elongation | Deoxyribonucleic acid--DNA | Translocation | Photosensitivity | Pol II | Nucleotide excision repair | RNA polymerase | Electron microscopy | Hereditary diseases | Polymerase | Ribonucleic acids | Microscopy | Mutation | Transcription initiation | Saccharomyces cerevisiae | Adenosine triphosphatase | RNA polymerase II | Structure-function relationships
Journal Article
Journal Article