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PLoS Biology, ISSN 1544-9173, 2014, Volume 12, Issue 9, pp. e1001954 - e1001954
Journal Article
Nature Communications, ISSN 2041-1723, 12/2019, Volume 10, Issue 1, pp. 1288 - 14
The TFIIH subunit XPB is involved in combined Xeroderma Pigmentosum and Cockayne syndrome (XP-B/CS). Our analyses reveal that XPB interacts functionally with... 
EXCISION-REPAIR | COMPLEX | XERODERMA-PIGMENTOSUM | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTION | COCKAYNE-SYNDROME | ABSENCE | DNA-REPAIR | INHIBITOR | SAGA | GENOME | Cockayne syndrome | Chromatin | Yeast | Xeroderma pigmentosum | Gene expression | Kinases | Histone acetyltransferase | DNA repair | Lymphocytes B | Acetylation | Mutation | Transcription initiation | Deoxyribonucleic acid--DNA | Cancer | Index Medicus
Journal Article
Journal Article
Advances in Protein Chemistry and Structural Biology, ISSN 1876-1623, 01/2019, Volume 115, pp. 21 - 67
Transcription factor IIH (TFIIH) is a multiprotein complex involved in both eukaryotic transcription and DNA repair, revealing a tight connection between these... 
Nucleotide excision repair | Structural proteomics | Transcription | TFIIH | Multi-subunit complex
Journal Article
PLOS NEGLECTED TROPICAL DISEASES, ISSN 1935-2735, 07/2019, Volume 13, Issue 7, pp. e0007591 - e0007591
Journal Article
Nature Structural & Molecular Biology, ISSN 1545-9993, 09/2008, Volume 15, Issue 9, pp. 980 - 984
Patients with the rare neurodevelopmental repair syndrome known as group A trichothiodystrophy (TTD-A) carry mutations in the gene encoding the p8 subunit of... 
COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | FACTOR TFIIH | P52 | NUCLEOTIDE EXCISION-REPAIR | CELL BIOLOGY | BIOPHYSICS | XERODERMA-PIGMENTOSUM | COMPONENT | DNA-REPAIR | FACTOR-IIH | SUBUNIT | Recombinant Proteins - metabolism | Trichothiodystrophy Syndromes - genetics | Saccharomyces cerevisiae - genetics | Humans | Models, Molecular | Recombinant Proteins - chemistry | Crystallography, X-Ray | Recombinant Proteins - genetics | Transcription Factor TFIIH - chemistry | Saccharomyces cerevisiae Proteins - genetics | Transcription Factor TFIIH - genetics | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - chemistry | DNA Repair | Saccharomyces cerevisiae Proteins - metabolism | Transcription Factor TFIIH - metabolism | Trichothiodystrophy Syndromes - metabolism | Transcription, Genetic | Protein Interaction Domains and Motifs | Mutation | Saccharomyces cerevisiae Proteins - chemistry | Trichothiodystrophy Syndromes - classification | Physiological aspects | Xeroderma pigmentosum | Causes of | Genetic aspects | DNA binding proteins | Research | Structure | Properties | Protein-protein interactions | Genetics | Molecular biology | DNA repair | Developmental disabilities | Crystal structure | Index Medicus | Life Sciences | Quantitative Methods | PATIENTS | DEFECTS | REPAIR | STABILIZATION | GENES | YEASTS | DNA REPAIR | CRYSTAL STRUCTURE | MATERIALS SCIENCE | MUTATIONS | POLYPEPTIDES
Journal Article
The Protein Journal, ISSN 1572-3887, 8/2017, Volume 36, Issue 4, pp. 240 - 248
Inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IP5 2-K) is an enzyme that catalyses the formation of phytic acid (IP6) from IP5 and ATP. In mammals, IP6 is... 
X-ray crystallography | Biochemistry, general | IP 5 2-K | Inositol kinase | Chemistry | Mammal IPK | Animal Anatomy / Morphology / Histology | Bioorganic Chemistry | Inositol hexakisphosphate | Organic Chemistry | IP 6 | 2-K | MOLECULAR REPLACEMENT | PROTEIN CRYSTALS | HEXAKISPHOSPHATE | RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | POLYPHOSPHATES | IP6 | SUBSTRATE-BINDING | PATHWAY | ROLES | IP5 2-K | EXPRESSION | PYROPHOSPHATES | Recombinant Fusion Proteins - isolation & purification | Baculoviridae - metabolism | Baculoviridae - genetics | Crystallography, X-Ray | Recombinant Fusion Proteins - metabolism | Spodoptera | Lectins - metabolism | Sf9 Cells | Glutathione Transferase - genetics | X-Ray Diffraction | Cloning, Molecular | Escherichia coli - metabolism | Gene Expression | Phosphotransferases (Alcohol Group Acceptor) - isolation & purification | Crystallization | Glutathione Transferase - metabolism | Phosphotransferases (Alcohol Group Acceptor) - genetics | Phosphotransferases (Alcohol Group Acceptor) - metabolism | Animals | Escherichia coli - genetics | Recombinant Fusion Proteins - genetics | Lectins - genetics | Mice | Chromatography, Gel | Agaricales - chemistry | Enzymes | Inositol | Diffraction | RNA | Analysis | Escherichia coli | X-rays | Information management | Recombinant proteins | Goods and services tax | GTP-binding protein | Protein purification | X-ray diffraction | Catalytic activity | mRNA | Kinases | Crystallography | Phytic acid | DNA repair | Proteins | E coli | Catalysis | Pyrophosphates | Inositol 1,4,5-trisphosphate | Deoxyribonucleic acid--DNA | Inositol 1,4,5-trisphosphate receptors | Recombinant | Data analysis | Filtration | rRNA | Crystals | Data processing | Mammals | Asymmetry | Insects | Insect cells | Gel filtration | Apoptosis | Index Medicus
Journal Article
PLoS Biology, ISSN 1544-9173, 09/2014, Volume 12, Issue 9
  The eukaryotic XPD helicase is an essential subunit of TFIIH involved in both transcription and nucleotide excision repair (NER). Mutations in human XPD are... 
Proteins | Enzymes | Transcription factors | Spectrum analysis | Mutation | DNA repair | Deoxyribonucleic acid--DNA | Cancer
Journal Article
Annals of Medicine, ISSN 0785-3890, 03/2019, Volume 51, Issue sup1, pp. 38 - 38
Introduction: Gla-rich protein (GRP) is a vitamin K-dependent protein (VKDP) acting as a calcification inhibitor and anti-inflammatory agent in cardiovascular... 
Calcification | therapeutics | extracellular vesicles (EVs) | inflammation
Journal Article
CELL, ISSN 0092-8674, 09/2000, Volume 102, Issue 5, pp. 599 - 607
TFIIH is a multiprotein complex required for both transcription and DNA repair. Single particles of human TFIIH were revealed by electron microscopy and image... 
RNA-POLYMERASE-II | RING FINGER PROTEIN | CDK-ACTIVATING KINASE | XERODERMA-PIGMENTOSUM | BIOCHEMISTRY & MOLECULAR BIOLOGY | CTD KINASE | COCKAYNE-SYNDROME | TRANSCRIPTION FACTOR TFIIH | DNA-REPAIR | SACCHAROMYCES-CEREVISIAE | NUCLEOTIDE EXCISION-REPAIR | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Multiprotein Complexes | Protein-Serine-Threonine Kinases - ultrastructure | DNA Helicases - ultrastructure | Xeroderma Pigmentosum Group D Protein | Transcription Factor TFIIH | Microscopy, Immunoelectron | DNA-Binding Proteins - metabolism | RNA, Messenger - biosynthesis | Cyclins - metabolism | Protein Structure, Quaternary | Transcription, Genetic | Cyclin-Dependent Kinases | Transcription Factors, TFII | Protein-Serine-Threonine Kinases - metabolism | Proteins - ultrastructure | Cyclin H | Recombinant Proteins - metabolism | DNA Helicases - chemistry | Recombinant Proteins - ultrastructure | Cyclins - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Antibodies, Monoclonal | Transcription Factors - ultrastructure | DNA-Binding Proteins - chemistry | Macromolecular Substances | DNA-Binding Proteins - ultrastructure | Transcription Factors - metabolism | DNA Helicases - metabolism | Proteins - metabolism | Image Processing, Computer-Assisted | Protein-Serine-Threonine Kinases - chemistry | Cyclins - ultrastructure | HeLa Cells | Proteins - chemistry | Proteins | Analysis | Regulation | Genetic transcription | Structure | Recombinant molecules | Structure-activity relationships (Biochemistry) | transcription initiation factor TFIIH | Index Medicus
Journal Article