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Journal Article
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
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2011, Volume 108, Issue 52, pp. 20881 - 20890
Amyotrophic lateral sclerosis (ALS) is a devastating and universally fatal neurodegenerative disease. Mutations in two related RNA-binding proteins, TDP-43 and... 
Aggregation | Proteins | Yeasts | Nervous system diseases | Neurodegenerative diseases | Neurons | Drosophila | Prions | Amyotrophic lateral sclerosis | Genetic mutation | WILD-TYPE | TDP-43 PROTEINOPATHY | DROSOPHILA MODEL | MULTIDISCIPLINARY SCIENCES | NEURODEGENERATION | AMYLOID PORES | TOXICITY | AMYOTROPHIC-LATERAL-SCLEROSIS | FUS MUTATIONS | FRONTOTEMPORAL LOBAR DEGENERATION | AGGREGATION | Immunohistochemistry | Protein Structure, Tertiary | RNA-Binding Proteins - genetics | TATA-Binding Protein Associated Factors - metabolism | Saccharomyces cerevisiae - genetics | Amyotrophic Lateral Sclerosis - genetics | Humans | Cells, Cultured | Computational Biology | Genetic Association Studies - methods | TATA-Binding Protein Associated Factors - genetics | Drosophila melanogaster - genetics | Mutation, Missense - genetics | Motor Neurons - metabolism | Animals | Spinal Cord - cytology | Yeast fungi | Gene mutations | Physiological aspects | Development and progression | Genetic aspects | Research | Binding proteins | Health aspects | Biological Sciences | amyotrophic-lateral-sclerosis; frontotemporal lobar degeneration; drosophila model; fus mutations; tdp-43 proteinopathy; amyloid pores; wild-type; toxicity; neurodegeneration; aggregation | Basic Medicine | Neurosciences | Medical and Health Sciences | Medicin och hälsovetenskap | Medicinska och farmaceutiska grundvetenskaper | Neurovetenskaper
Journal Article
Journal Article
Cell, ISSN 0092-8674, 04/2018, Volume 173, Issue 3, pp. 677 - 692.e20
Journal Article
Human Molecular Genetics, ISSN 0964-6906, 07/2012, Volume 21, Issue 13, pp. 2899 - 2911
Journal Article
Nature, ISSN 0028-0836, 3/2013, Volume 495, Issue 7442, pp. 467 - 473
Algorithms designed to identify canonical yeast prions predict that ~250 human proteins, including several RNA-binding proteins associated with... 
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2011, Volume 108, Issue 52, p. 20881
Amyotrophic lateral sclerosis (ALS) is a devastating and universally fatal neurodegenerative disease. Mutations in two related RNA-binding proteins, TDP-43 and... 
Immunohistochemistry | Proteins | Yeast | Genes | Amyotrophic lateral sclerosis | Ribonucleic acid--RNA
Journal Article
Caldasia, ISSN 0366-5232, 2011, Volume 33, Issue 1, pp. 105 - 119
Se evaluo el grado de amenaza de la Malvacea bombacoide Cavanillesia chicamochae Fern. Alonso, especie recientemente descrita y considerada endemica del canon... 
Malvaceae | Colombia | Bombacoideae | Categorization IUCN | Cavanillesia chicamochae | Conservation
Journal Article
Revista Colombiana de Química, ISSN 0120-2804, 05/2019, Volume 48, Issue 2, p. 27
La gulupa es una fruta originaria de la región amazónica, cuyo epicarpio es un subproducto con alto potencial en antioxidantes como las antocianinas. Por lo... 
Antioxidants | Passion fruit | Degradation | Solvents | Ascorbic acid | Vitamin C | Storage temperature | Anthocyanins | Solvent extraction
Journal Article