Articles

UofT Libraries is getting a new library services platform in January 2021.
Learn more about the change.

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
science & technology (445) 445
life sciences & biomedicine (358) 358
humans (341) 341
proteins (184) 184
animals (179) 179
amyotrophic lateral sclerosis (176) 176
neurosciences (158) 158
neurosciences & neurology (145) 145
biochemistry & molecular biology (117) 117
mutation (116) 116
male (107) 107
neurodegeneration (101) 101
nervous system diseases (96) 96
female (93) 93
nuclear magnetic resonance--nmr (88) 88
protein binding (88) 88
mice (87) 87
multidisciplinary sciences (87) 87
science & technology - other topics (87) 87
cell biology (86) 86
dna-binding proteins - metabolism (86) 86
rna (84) 84
amyotrophic lateral sclerosis - genetics (80) 80
neurons (78) 78
neurology (74) 74
research (74) 74
gene expression (73) 73
pathology (73) 73
neurodegenerative diseases (71) 71
ribonucleic acid--rna (71) 71
dementia (70) 70
frontotemporal dementia (70) 70
genetic aspects (63) 63
research article (63) 63
dna-binding proteins - genetics (62) 62
middle aged (62) 62
medicine (61) 61
amyotrophic lateral sclerosis - metabolism (60) 60
science (59) 59
mental disorders (57) 57
aged (56) 56
analysis (56) 56
nuclear proteins - metabolism (55) 55
clinical neurology (54) 54
physiological aspects (54) 54
disease (51) 51
nuclear proteins - genetics (50) 50
hela cells (49) 49
brain (48) 48
deoxyribonucleic acid--dna (47) 47
amyotrophic lateral sclerosis - pathology (45) 45
rna splicing (45) 45
tdp-43 (45) 45
rna-binding proteins - metabolism (43) 43
alternative splicing (41) 41
alzheimer's disease (41) 41
biology (41) 41
magnetic resonance imaging (40) 40
medical imaging (40) 40
molecular biology (40) 40
nervous system (40) 40
cell line (39) 39
neuroscience (39) 39
nutritional and metabolic diseases (39) 39
dementia disorders (38) 38
pathogenesis (38) 38
rna-binding protein (38) 38
rna-binding protein fus - metabolism (38) 38
genes (37) 37
hek293 cells (37) 37
localization (37) 37
genetics (36) 36
neuroimaging (36) 36
biochemistry (35) 35
studies (35) 35
disease models, animal (34) 34
medicine & public health (34) 34
nuclear transport (34) 34
binding proteins (33) 33
binding sites (33) 33
exons (33) 33
neurons - metabolism (33) 33
review (33) 33
splicing (33) 33
adult (32) 32
als (32) 32
cell nucleus - metabolism (32) 32
metabolism (32) 32
radiology, nuclear medicine & medical imaging (32) 32
alzheimers disease (31) 31
cytoplasm (31) 31
molecular sequence data (31) 31
rodents (31) 31
genetics & heredity (30) 30
genomes (30) 30
heterogeneous-nuclear ribonucleoprotein group a-b - metabolism (30) 30
patients (30) 30
rna-binding proteins - genetics (30) 30
aged, 80 and over (28) 28
atrophy (28) 28
more...
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text Small-Molecule Modulation of TDP-43 Recruitment to Stress Granules Prevents Persistent TDP-43 Accumulation in ALS/FTD
by Fang, Mark Y and Markmiller, Sebastian and Vu, Anthony Q and Javaherian, Ashkan and Dowdle, William E and Jolivet, Philippe and Bushway, Paul J and Castello, Nicholas A and Baral, Ashmita and Chan, Michelle Y and Linsley, Jeremy W and Linsley, Drew and Mercola, Mark and Finkbeiner, Steven and Lecuyer, Eric and Lewcock, Joseph W and Yeo, Gene W
Neuron (Cambridge, Mass.), ISSN 0896-6273, 09/2019, Volume 103, Issue 5, pp. 802 - 819.e11
motor neurons | ALS-FTD | planar molecule | stress granule | TDP-43 | high-content screening | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Small Molecule Libraries - pharmacology | Humans | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | Cytoplasmic Granules - metabolism | HEK293 Cells | RNA Helicases - genetics | Stress, Physiological - drug effects | DNA Helicases - genetics | Motor Neurons - drug effects | Cell Line | Cytoplasmic Granules - drug effects | DNA-Binding Proteins - drug effects | Intrinsically Disordered Proteins | Neural Stem Cells - drug effects | Poly-ADP-Ribose Binding Proteins - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | RNA-Binding Protein FUS - metabolism | Motor Neurons - metabolism | High-Throughput Screening Assays | Amyotrophic Lateral Sclerosis - metabolism | RNA Recognition Motif Proteins - genetics | Induced Pluripotent Stem Cells | Neural Stem Cells - metabolism | Protein Aggregation, Pathological - metabolism | Proteins | Motor neurons | RNA-binding protein | Disease | Neurodegenerative diseases | Stem cells | Dementia disorders | Amyotrophic lateral sclerosis | Mutation | Ribonucleic acid--RNA | Frontotemporal dementia | Localization | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Full Text TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD
by Chou, Ching-Chieh and Zhang, Yi and Umoh, Mfon E and Vaughan, Spencer W and Lorenzini, Ileana and Liu, Feilin and Sayegh, Melissa and Donlin-Asp, Paul G and Chen, Yu Han and Duong, Duc M and Seyfried, Nicholas T and Powers, Maureen A and Kukar, Thomas and Hales, Chadwick M and Gearing, Marla and Cairns, Nigel J and Boylan, Kevin B and Dickson, Dennis W and Rademakers, Rosa and Zhang, Yong-Jie and Petrucelli, Leonard and Sattler, Rita and Zarnescu, Daniela C and Glass, Jonathan D and Rossoll, Wilfried
Nature neuroscience, ISSN 1097-6256, 02/2018, Volume 21, Issue 2, pp. 228 - 239
Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | C9orf72 Protein - genetics | Active Transport, Cell Nucleus - physiology | Humans | Nuclear Envelope - ultrastructure | Male | Drosophila Proteins - metabolism | Cerebral Cortex - cytology | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | Protein Aggregation, Pathological - pathology | Female | C9orf72 Protein - metabolism | Active Transport, Cell Nucleus - genetics | Neuroblastoma - pathology | Frontotemporal Dementia - pathology | Frontotemporal Dementia - genetics | Animals, Genetically Modified | Amyotrophic Lateral Sclerosis - genetics | Drosophila | Mice, Inbred C57BL | Cells, Cultured | Nuclear Pore - genetics | DNA-Binding Proteins - genetics | Nuclear Pore - metabolism | DNA-Binding Proteins - ultrastructure | Amyotrophic Lateral Sclerosis - pathology | Animals | Larva | Amyotrophic Lateral Sclerosis - metabolism | C9orf72 Protein - ultrastructure | Embryo, Nonmammalian | Mice | Drosophila Proteins - genetics | Nuclear Envelope - pathology | Protein Aggregation, Pathological - metabolism | Fibroblasts | Amyotrophic lateral sclerosis | Research | Protein binding | Brain | Neurons | Biotin | Ribonucleic acid--RNA | Pathology | DNA-binding protein | Nucleoporins | RNA transport | Aggregates | Stem cells | Dementia disorders | Mutation | Transport | Protein transport | Frontotemporal dementia | Pluripotency | Deoxyribonucleic acid--DNA | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
3. Full Text Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
by Lukavsky, Peter J and Daujotyte, Dalia and Tollervey, James R and Ule, Jernej and Stuani, Cristiana and Buratti, Emanuele and Baralle, Francisco E and Damberger, Fred F and Allain, Frédéric H.-T
Nature structural & molecular biology, ISSN 1545-9993, 12/2013, Volume 20, Issue 12, pp. 1443 - 1449
Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Protein Structure, Tertiary | Amino Acid Sequence | DNA-Binding Proteins - physiology | RNA-Binding Proteins - physiology | Humans | RNA-Binding Proteins - chemistry | Models, Molecular | Molecular Sequence Data | Cystic Fibrosis Transmembrane Conductance Regulator - metabolism | DNA-Binding Proteins - chemistry | DNA-Binding Proteins - metabolism | RNA Splicing - physiology | Base Composition | Nuclear Magnetic Resonance, Biomolecular | Cystic Fibrosis Transmembrane Conductance Regulator - genetics | Binding Sites | RNA-Binding Proteins - metabolism | Research | Binding proteins | Genetic regulation | Identification and classification | RNA splicing | Proteins | Cystic fibrosis | Molecular structure | Ribonucleic acid--RNA | Neurodegeneration | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
4. Full Text TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
by Buratti, Emanuele and Brindisi, Antonia and Giombi, Maurizio and Tisminetzky, Sergio and Ayala, Youhna M and Baralle, Francisco E
The Journal of biological chemistry, ISSN 0021-9258, 11/2005, Volume 280, Issue 45, pp. 37572 - 37584
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | DNA-Binding Proteins - metabolism | Multigene Family | Alternative Splicing - genetics | Humans | RNA Splicing - genetics | Protein Binding | Cystic Fibrosis Transmembrane Conductance Regulator - genetics | Exons - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Cystic Fibrosis Transmembrane Conductance Regulator - metabolism | HeLa Cells | DNA-Binding Proteins - chemistry | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
5. Full Text Cytoplasmic poly-GA aggregates impair nuclear import of TDP-43 in C9orf72 ALS/FTLD
by Khosravi, Bahram and Hartmann, Hannelore and May, Stephanie and Möhl, Christoph and Ederle, Helena and Michaelsen, Meike and Schludi, Martin H and Dormann, Dorothee and Edbauer, Dieter
Human molecular genetics, ISSN 0964-6906, 02/2017, Volume 26, Issue 4, pp. 790 - 800
Biochemistry & Molecular Biology | Genetics & Heredity | Life Sciences & Biomedicine | Science & Technology | Tumor Necrosis Factor-alpha - metabolism | alpha Karyopherins - metabolism | Frontotemporal Lobar Degeneration - pathology | Membrane Glycoproteins - metabolism | Nuclear Localization Signals - genetics | Humans | Tumor Necrosis Factor-alpha - genetics | DNA-Binding Proteins - metabolism | Nuclear Pore Complex Proteins - genetics | DNA Repeat Expansion | Frontotemporal Lobar Degeneration - metabolism | C9orf72 Protein | Neurons - metabolism | Inclusion Bodies - metabolism | Nuclear Pore Complex Proteins - metabolism | Amyotrophic Lateral Sclerosis - genetics | Nuclear Localization Signals - metabolism | Rats | DNA-Binding Proteins - genetics | Membrane Glycoproteins - genetics | Proteins - genetics | Amyotrophic Lateral Sclerosis - pathology | Inclusion Bodies - genetics | Animals | Proteins - metabolism | Amyotrophic Lateral Sclerosis - metabolism | alpha Karyopherins - genetics | Frontotemporal Lobar Degeneration - genetics | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text Depletion of TDP-43 decreases fibril and plaque β-amyloid and exacerbates neurodegeneration in an Alzheimer’s mouse model
by LaClair, Katherine D and Donde, Aneesh and Ling, Jonathan P and Jeong, Yun Ha and Chhabra, Resham and Martin, Lee J and Wong, Philip C
Acta neuropathologica, ISSN 0001-6322, 12/2016, Volume 132, Issue 6, pp. 859 - 873
Pathology | Neurosciences | Medicine & Public Health | Alzheimer’s disease | TDP-43 | β-Amyloid | Forebrain | Nuclear depletion | Clinical Neurology | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Alzheimer Disease - complications | Neurodegenerative Diseases - etiology | Humans | Male | DNA-Binding Proteins - deficiency | Alzheimer Disease - pathology | Antineoplastic Agents, Hormonal - therapeutic use | Cognition Disorders - etiology | Amyloid beta-Peptides - metabolism | Amyloid beta-Protein Precursor - metabolism | Plaque, Amyloid - etiology | Female | Autophagy - genetics | Disease Models, Animal | Prosencephalon - pathology | Plaque, Amyloid - pathology | Mice, Inbred C57BL | Alzheimer Disease - drug therapy | Presenilin-1 - genetics | Mice, Transgenic | Cognition Disorders - genetics | Mitochondria - metabolism | Mitochondria - pathology | DNA-Binding Proteins - genetics | Plaque, Amyloid - genetics | Amyloid beta-Protein Precursor - genetics | Animals | Presenilin-1 - metabolism | Tamoxifen - therapeutic use | Mice | Alzheimer Disease - genetics | Index Medicus | Alzheimer's disease
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text Structural determinants of the cellular localization and shuttling of TDP-43
by Ayala, Youhna M and Zago, Paola and D'Ambrogio, Andrea and Xu, Ya-Fei and Petrucelli, Leonard and Buratti, Emanuele and Baralle, Francisco E
Journal of cell science, ISSN 0021-9533, 11/2008, Volume 121, Issue 22, pp. 3778 - 3785
RNA recognition motifs | Nuclear-cytoplasmic shuttling | hnRNP | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Cytoplasm - chemistry | Protein Structure, Tertiary | Cell Line | Sequence Deletion | Nuclear Localization Signals - genetics | Humans | Cytoplasm - metabolism | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Amino Acid Motifs | Protein Transport | DNA-Binding Proteins - metabolism | Cell Nucleus - metabolism | Cell Nucleus - genetics | Cell Nucleus - chemistry | Cytoplasm - genetics | HeLa Cells | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. Full Text Aberrant activation of non-coding RNA targets of transcriptional elongation complexes contributes to TDP-43 toxicity
by Chung, Chia-Yu and Berson, Amit and Kennerdell, Jason R and Sartoris, Ashley and Unger, Travis and Porta, Sílvia and Kim, Hyung-Jun and Smith, Edwin R and Shilatifard, Ali and Van Deerlin, Vivianna and Lee, Virginia M.-Y and Chen-Plotkin, Alice and Bonini, Nancy M
Nature communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 4406 - 13
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Polytene Chromosomes - metabolism | DNA-Binding Proteins - toxicity | Humans | Male | Nuclear Proteins - metabolism | Genetic Loci | Drosophila Proteins - metabolism | RNA, Untranslated - genetics | Transcription Elongation, Genetic | Drosophila melanogaster - metabolism | Transcription Factors - metabolism | Transcriptional Elongation Factors - metabolism | Animals | Models, Biological | RNA, Small Nuclear - genetics | HEK293 Cells | Protein Binding | Female | Immunoprecipitation | Target recognition | Toxicity | Amyotrophic lateral sclerosis | Ribonucleic acid--RNA | snRNA | Proteins | Neurodegeneration | Coding | Degeneration | Frontotemporal dementia | Non-coding RNA | Elongation | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
9. Full Text TDP-43 regulates site-specific 2′-O-methylation of U1 and U2 snRNAs via controlling the Cajal body localization of a subset of C/D scaRNAs
by Izumikawa, Keiichi and Nobe, Yuko and Ishikawa, Hideaki and Yamauchi, Yoshio and Taoka, Masato and Sato, Ko and Nakayama, Hiroshi and Simpson, Richard J and Isobe, Toshiaki and Takahashi, Nobuhiro
Nucleic acids research, ISSN 0305-1048, 03/2019, Volume 47, Issue 5, pp. 2487 - 2505
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Coiled Bodies - genetics | Molecular Chaperones | Cell Nucleolus - genetics | RNA, Guide - genetics | Amyotrophic Lateral Sclerosis - genetics | Humans | Ribonucleoproteins, Small Nuclear - genetics | Cytidine - analogs & derivatives | DNA-Binding Proteins - genetics | Proteins - genetics | Amyotrophic Lateral Sclerosis - pathology | RNA, Small Nuclear - genetics | Cytidine - genetics | Coiled Bodies - metabolism | HeLa Cells | Telomerase | Index Medicus | Molecular Biology
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights