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Journal Article
Nature Biotechnology, ISSN 1087-0156, 06/2002, Volume 20, Issue 6, pp. 619 - 622
Journal Article
2008, RSC biomolecular sciences, ISBN 9780854042722, Volume 11, xvii, 397
Written by a team of experts, this book bridges the gap between the DNA- and RNA- views of protein-nucleic acid recognition which are often treated as separate... 
RNA-protein interactions | DNA-protein interactions | General | Chemistry | SCIENCE | Biochemistry
Book
Nature Neuroscience, ISSN 1097-6256, 11/2012, Volume 15, Issue 11, pp. 1488 - 1497
FUS/TLS (fused in sarcoma/translocated in liposarcoma) and TDP-43 are integrally involved in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia.... 
NEURODEGENERATIVE DISEASE | GENE | AMYOTROPHIC-LATERAL-SCLEROSIS | FAMILY PROTEINS | FUS PATHOLOGY | MUTATIONS | FRONTOTEMPORAL LOBAR DEGENERATION | BINDING | NEUROSCIENCES | BRAIN | NASCENT TRANSCRIPTION | RNA, Small Interfering - genetics | Protein Binding - genetics | Oligonucleotide Array Sequence Analysis | Humans | tau Proteins - metabolism | Gene Expression Profiling | RNA, Messenger - metabolism | Kv Channel-Interacting Proteins - metabolism | Brain - metabolism | Frontotemporal Dementia - metabolism | RNA Splicing - genetics | Frontotemporal Dementia - genetics | RNA-Binding Protein FUS - deficiency | Amyotrophic Lateral Sclerosis - genetics | Cell Cycle Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | RNA-Binding Protein FUS - genetics | Mice, Knockout | Motor Neurons - metabolism | Amyotrophic Lateral Sclerosis - pathology | Shal Potassium Channels - metabolism | Brain - pathology | Mice | Neurofilament Proteins - metabolism | RNA, Small Interfering - metabolism | Immunoprecipitation | Spinal Cord - metabolism | DNA-Binding Proteins - deficiency | DNA-Binding Proteins - metabolism | tau Proteins - genetics | Cell Cycle Proteins - genetics | Female | RNA Precursors - metabolism | Excitatory Amino Acid Transporter 2 - genetics | Membrane Proteins - metabolism | Frontotemporal Dementia - pathology | Gene Expression Regulation - genetics | Mice, Inbred C57BL | RNA, Messenger - genetics | RNA Precursors - genetics | Protein Structure, Tertiary - genetics | RNA-Binding Protein FUS - metabolism | DNA-Binding Proteins - genetics | Excitatory Amino Acid Transporter 2 - metabolism | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Histone-Lysine N-Methyltransferase - metabolism | Amyotrophic Lateral Sclerosis - metabolism | Neural Cell Adhesion Molecules - metabolism | Neural Stem Cells - metabolism | Cell Line, Transformed | Amyotrophic lateral sclerosis | Development and progression | Genetic aspects | Messenger RNA | Health aspects
Journal Article
Nature, ISSN 0028-0836, 2013, Volume 499, Issue 7456, pp. 50 - 54
53BP1 (also called TP53BP1) is a chromatin-associated factor that promotes immunoglobulin class switching and DNA double-strand-break (DSB) repair by... 
CRB2 | RECRUITMENT | FISSION YEAST | METHYLATION | CHROMATIN | DEPENDENT RESPONSE | RESECTION | MULTIDISCIPLINARY SCIENCES | SITES | DOUBLE-STRAND BREAKS | CLASS-SWITCH RECOMBINATION | Schizosaccharomyces pombe Proteins - chemistry | Histones - chemistry | Nucleosomes - chemistry | Humans | Ubiquitin - metabolism | Molecular Sequence Data | Male | Intracellular Signaling Peptides and Proteins - metabolism | DNA Breaks, Double-Stranded | DNA-Binding Proteins - deficiency | Cell Cycle Proteins - chemistry | Intracellular Signaling Peptides and Proteins - deficiency | Ubiquitination | Schizosaccharomyces pombe Proteins - metabolism | Female | Lysine - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Schizosaccharomyces | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Signal Transduction | Cell Cycle Proteins - metabolism | Nucleosomes - metabolism | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Chromosomal Proteins, Non-Histone - deficiency | Amino Acid Motifs | Chromosomal Proteins, Non-Histone - genetics | Animals | Intracellular Signaling Peptides and Proteins - chemistry | Mutant Proteins - chemistry | Protein Binding | Mice | DNA Damage | Histones - metabolism | Tumor Suppressor p53-Binding Protein 1 | Chromosomal Proteins, Non-Histone - chemistry | Ubiquitin | Research | Properties | DNA repair | DNA damage | Proteins | DNA methylation | Mutation | Experiments | Recruitment
Journal Article
Biochemical Journal, ISSN 0264-6021, 04/2017, Volume 474, Issue 8, pp. 1417 - 1438
Approximately 70 human RNA-binding proteins (RBPs) contain a prion-like domain (PrLD). PrLDs are low-complexity domains that possess a similar amino acid... 
EUKARYOTIC STRESS GRANULES | MUTANT FUS PROTEINS | MULTISYSTEM PROTEINOPATHY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHASE-TRANSITION | TARDBP MUTATIONS | HNRNP A1 | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS | NEURODEGENERATIVE DISEASES | Proteostasis Deficiencies - metabolism | RNA-Binding Proteins - genetics | TATA-Binding Protein Associated Factors - metabolism | Humans | Prion Proteins - metabolism | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | RNA-Binding Protein FUS - chemistry | TDP-43 Proteinopathies - genetics | Protein Domains | TDP-43 Proteinopathies - pathology | Prion Proteins - chemistry | Prion Proteins - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Frontotemporal Dementia - pathology | Calmodulin-Binding Proteins - genetics | Frontotemporal Dementia - genetics | Cytoplasmic Granules | Neurodegenerative Diseases - pathology | Amyotrophic Lateral Sclerosis - genetics | RNA-Binding Proteins - chemistry | TDP-43 Proteinopathies - metabolism | Proteostasis Deficiencies - pathology | RNA-Binding Protein FUS - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Neurodegenerative Diseases - genetics | Calmodulin-Binding Proteins - chemistry | Calmodulin-Binding Proteins - metabolism | RNA-Binding Protein FUS - metabolism | Neurodegenerative Diseases - metabolism | TATA-Binding Protein Associated Factors - chemistry | DNA-Binding Proteins - genetics | TATA-Binding Protein Associated Factors - genetics | DNA-Binding Proteins - chemistry | Heterogeneous Nuclear Ribonucleoprotein A1 | Proteostasis Deficiencies - genetics | Amyotrophic Lateral Sclerosis - pathology | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Mutation | RNA-Binding Proteins - metabolism | RNA-Binding Protein EWS
Journal Article
by Schormair, Barbara and Zhao, Chen and Bell, Steven and Bell, Robert K and Tilch, Erik and Salminen, Aaro V and Pütz, Benno and Dauvilliers, Yves and Stefani, Ambra and Högl, Birgit and Poewe, Werner and Kemlink, David and Sonka, Karel and Bachmann, Cornelius G and Paulus, Walter and Trenkwalder, Claudia and Oertel, Wolfgang H and Hornyak, Magdolna and Teder-Laving, Maris and Metspalu, Andres and Hadjigeorgiou, Georgios M and Polo, Olli and Fietze, Ingo and Ross, Owen A and Wszolek, Zbigniew and Butterworth, Adam S and Soranzo, Nicole and Ouwehand, Willem H and Roberts, David J and Danesh, John and Allen, Richard P and Earley, Christopher J and Ondo, William G and Xiong, Lan and Montplaisir, Jacques and Gan-Or, Ziv and Perola, Markus and Vodicka, Pavel and Dina, Christian and Franke, Andre and Tittmann, Lukas and Stewart, Alexandre F R and Shah, Svati H and Gieger, Christian and Peters, Annette and Rouleau, Guy A and Berger, Klaus and Oexle, Konrad and Di Angelantonio, Emanuele and Hinds, David A and Müller-Myhsok, Bertram and Winkelmann, Juliane and Balkau, B and Ducimetière, P and Eschwège, E and Rancière, F and Alhenc-Gelas, F and Gallois, Y and Girault, A and Fumeron, F and Marre, M and Roussel, R and Bonnet, F and Bonnefond, A and Cauchi, S and Froguel, P and Cogneau, J and Born, C and Caces, E and Cailleau, M and Lantieri, O and Moreau, JG and Rakotozafy, F and Tichet, J and Vol, S and Agee, Michelle and Alipanahi, Babak and Auton, Adam and Bryc, Katarzyna and Elson, Sarah L and Fontanillas, Pierre and Furlotte, Nicholas A and Hromatka, Bethann S and Huber, Karen E and Kleinman, Aaron and Litterman, Nadia K and McIntyre, Matthew H and Mountain, Joanna L and Northover, Carrie AM and Pitts, Steven J and Sathirapongsasuti, J Fah and Sazonova, Olga V and Shelton, Janie F and Shringarpure, Suyash and Tian, Chao and Tung, Joyce Y and Vacic, Vladimir and Wilson, Catherine H and Collaboration 23andMe Res Team and DESIR Study Grp and DESIR study group and 23andMe Research Team
The Lancet Neurology, ISSN 1474-4422, 11/2017, Volume 16, Issue 11, pp. 898 - 907
Journal Article
Annual Review of Biochemistry, ISSN 0066-4154, 6/2016, Volume 85, Issue 1, pp. 375 - 404
Inactivation of the transcription factor p53, through either direct mutation or aberrations in one of its many regulatory pathways, is a hallmark of virtually... 
cancer therapy | signaling pathways | protein evolution | drug design | p53 family | small-molecule stabilizers | Protein evolution | Signaling pathways | Drug design | Small-molecule stabilizers | P53 family | Cancer therapy | DNA-BINDING DOMAIN | TRANSIENT PROTEIN STATES | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-CYCLE ARREST | TUMOR-SUPPRESSOR P53 | CORE-DOMAIN | STRUCTURAL BASIS | SMALL-MOLECULE INHIBITORS | MUTANT P53 | TETRAMERIZATION DOMAIN | TRANSACTIVATION DOMAIN | Neoplasms - metabolism | Proto-Oncogene Proteins c-mdm2 - genetics | Antineoplastic Agents, Alkylating - chemical synthesis | Humans | Protein Multimerization | Gene Expression Regulation, Neoplastic | Proto-Oncogene Proteins - chemistry | Molecular Targeted Therapy | Proto-Oncogene Proteins c-mdm2 - chemistry | Tumor Suppressor Protein p53 - genetics | Neoplasms - genetics | Tumor Suppressor Protein p53 - agonists | Drug Design | Nuclear Proteins - genetics | Proto-Oncogene Proteins c-mdm2 - antagonists & inhibitors | Proto-Oncogene Proteins c-mdm2 - metabolism | Proto-Oncogene Proteins - metabolism | Proto-Oncogene Proteins - antagonists & inhibitors | Protein Structure, Secondary | Signal Transduction | Tumor Suppressor Protein p53 - metabolism | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | Clinical Trials as Topic | Nuclear Proteins - chemistry | Neoplasms - drug therapy | Antineoplastic Agents, Alkylating - therapeutic use | Animals | Nuclear Proteins - antagonists & inhibitors | Molecular Docking Simulation | Tumor Suppressor Protein p53 - chemistry | Mutation | Neoplasms - pathology | Transcription factors | Care and treatment | Health aspects | Methods | Cancer
Journal Article