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Nature, ISSN 0028-0836, 03/2013, Volume 495, Issue 7442, pp. 467 - 473
Algorithms designed to identify canonical yeast prions predict that around 250 human proteins, including several RNA-binding proteins associated with... 
RNA-BINDING PROTEINS | DROSOPHILA MODEL | TDP-43 | MULTIDISCIPLINARY SCIENCES | FRONTOTEMPORAL DEMENTIA | VCP MUTATIONS | DISEASE | AMYOTROPHIC-LATERAL-SCLEROSIS | SACCHAROMYCES-CEREVISIAE | STRESS GRANULES | MULTIPLE ALIGNMENT | Prions - genetics | Humans | Molecular Sequence Data | Osteitis Deformans - metabolism | Male | Drosophila melanogaster - genetics | Osteitis Deformans - genetics | Drosophila melanogaster - metabolism | Frontotemporal Dementia - metabolism | Muscular Dystrophies, Limb-Girdle - genetics | Myositis, Inclusion Body - pathology | Female | Inclusion Bodies - metabolism | Muscular Dystrophies, Limb-Girdle - pathology | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Frontotemporal Dementia - pathology | RNA - metabolism | Frontotemporal Dementia - genetics | Amino Acid Sequence | Prions - metabolism | Peptide Termination Factors - genetics | Amyotrophic Lateral Sclerosis - genetics | Drosophila melanogaster - cytology | Mutant Proteins - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Mutant Proteins - metabolism | Protein Structure, Tertiary - genetics | Prions - chemistry | Saccharomyces cerevisiae Proteins - genetics | Mutation - genetics | Myositis, Inclusion Body - genetics | Peptide Termination Factors - metabolism | Amyotrophic Lateral Sclerosis - pathology | Inclusion Bodies - genetics | Osteitis Deformans - pathology | Animals | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - chemistry | Muscular Dystrophies, Limb-Girdle - metabolism | Mutant Proteins - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Inclusion Bodies - pathology | Myositis, Inclusion Body - metabolism | Mice | Peptide Termination Factors - chemistry | HeLa Cells | Saccharomyces cerevisiae Proteins - chemistry | Pathology | Insects | Genomics | Genetics | Software | Genomes | Mutation | Genetic testing | Patients | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 6, pp. e21045 - e21045
Rabbits are widely used in biomedical research, yet techniques for their precise genetic modification are lacking. We demonstrate that zinc finger nucleases... 
PRION PROTEIN | PIGS | CELLS | MOUSE | BIOLOGY | GENERATION | MODEL | MONOCLONAL-ANTIBODIES | KNOCKOUT RATS | GENOME | TRANSGENIC MICE | Rabbits | Reproducibility of Results | Zinc Fingers | Microinjections | Protein Engineering - methods | Oocytes - metabolism | Humans | Immunoglobulin M - deficiency | RNA, Messenger - genetics | Genetic Loci - genetics | Molecular Sequence Data | Exons - genetics | Male | Gene Knockout Techniques | Mutation - genetics | Deoxyribonucleases - genetics | Animals | Immunoglobulin G - genetics | Base Sequence | Alleles | Female | Deoxyribonucleases - chemistry | Immunoglobulin M - genetics | Immunoglobulin M | Nucleases | Genetic vectors | RNA | Immunoglobulin G | Genes | Genetically modified organisms | Animal genetic engineering | B cells | DNA binding proteins | Zinc finger proteins | Health aspects | Biotechnology | Exons | Homologous recombination | Antibodies | Homology | Genomes | mRNA | Inactivation | Oocytes | Immunology | Cattle | Lymphocytes | Gene disruption | Coinjection | Experimentation | Genetic modification | Deoxyribonucleic acid--DNA | Polyclonal antibodies | Deactivation | Nucleotide sequence | Fetuses | Cloning | Artificial chromosomes | Gene expression | Embryos | Loci | Zinc | Offspring | Lymphocytes B | Mutagenesis | Livestock | Genetic engineering | Gene manipulation | Mutation | Gene therapy | Laboratory animals | Index Medicus | Deoxyribonucleic acid | DNA
Journal Article
Neurobiology of Aging, ISSN 0197-4580, 2014, Volume 35, Issue 12, pp. 2881.e1 - 2881.e6
Journal Article
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2008, Volume 380, Issue 2, pp. 425 - 436
Journal Article
PLoS Genetics, ISSN 1553-7390, 07/2018, Volume 14, Issue 7, pp. e1007517 - e1007517
Enhanced protein aggregation and/or impaired clearance of aggregates can lead to neurodegenerative disorders such as Alzheimer's Disease, Huntington's Disease,... 
EXPOSED HYDROPHOBICITY | SUBSTRATE-SPECIFICITY | GENETICS & HEREDITY | QUALITY-CONTROL DEGRADATION | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | MUTATIONS | FRONTOTEMPORAL LOBAR DEGENERATION | CHAPERONE | SACCHAROMYCES-CEREVISIAE | YEAST PRION | Prions - metabolism | Neurodegenerative Diseases - pathology | Prions - genetics | Peptide Termination Factors - genetics | Humans | Glutamine - metabolism | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Neurodegenerative Diseases - genetics | Amino Acid Sequence - genetics | Saccharomyces cerevisiae Proteins - genetics | Peptide Termination Factors - metabolism | Protein Domains - genetics | Protein Aggregation, Pathological - pathology | Proteolysis | Asparagine - metabolism | Glutamine - genetics | Saccharomyces cerevisiae Proteins - metabolism | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Protein Aggregation, Pathological - genetics | Asparagine - genetics | Protein research | Nucleotide sequence | Protein folding | Prions | Genetic research | Genetic aspects | Research | Nervous system diseases | Analysis | Quality control | Control systems | Glycine | Genetic screening | Quality management | Biodegradation | Yeast | Disease | Neurodegenerative diseases | Amino acids | Biochemistry | Mammals | Proteins | Algorithms | Asparagine | Mutation | Molecular biology | Prion protein | Protein interaction | Glutamine | Index Medicus
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