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index medicus (107) 107
humans (91) 91
fused in sarcoma (83) 83
amyotrophic lateral sclerosis (81) 81
neurosciences (59) 59
amyotrophic-lateral-sclerosis (54) 54
sarcoma (53) 53
rna-binding protein fus - genetics (50) 50
frontotemporal lobar degeneration (49) 49
rna-binding protein fus - metabolism (48) 48
clinical neurology (47) 47
male (41) 41
als (37) 37
amyotrophic lateral sclerosis - genetics (37) 37
mutations (35) 35
animals (34) 34
tdp-43 (34) 34
female (33) 33
biochemistry & molecular biology (30) 30
frontotemporal dementia (29) 29
adult (28) 28
mutation (26) 26
pathology (26) 26
amyotrophic lateral sclerosis - pathology (25) 25
fus (25) 25
genetic aspects (25) 25
amyotrophic lateral sclerosis - metabolism (24) 24
neurology (24) 24
article (23) 23
dementia (23) 23
middle aged (23) 23
rna (23) 23
analysis (22) 22
protein binding (22) 22
proteins (22) 22
dna-binding proteins - metabolism (20) 20
inclusion bodies - pathology (19) 19
gene (18) 18
neurons (17) 17
dna-binding proteins - genetics (16) 16
fus/tls (16) 16
neurodegeneration (16) 16
rna-binding protein (16) 16
aged (15) 15
mice (15) 15
nervous system diseases (15) 15
stress granules (15) 15
brain - pathology (14) 14
degeneration (14) 14
frontotemporal lobar degeneration - pathology (14) 14
immunohistochemistry (14) 14
inclusion bodies - metabolism (14) 14
physiological aspects (14) 14
research (14) 14
binding proteins (13) 13
frontotemporal lobar degeneration - metabolism (13) 13
tls (13) 13
fus protein (12) 12
motor neurons - metabolism (12) 12
mutation - genetics (12) 12
protein (12) 12
disease progression (11) 11
neurons - metabolism (11) 11
neurons - pathology (11) 11
young adult (11) 11
aggregation (10) 10
cell biology (10) 10
disease (10) 10
medical research (10) 10
medicine & public health (10) 10
translocated in liposarcoma (10) 10
ubiquitin (10) 10
development and progression (9) 9
fet proteins (9) 9
fused in sarcoma/translocated in liposarcoma (9) 9
gene expression (9) 9
genes (9) 9
inclusion bodies (9) 9
neurodegenerative diseases (9) 9
oncology (9) 9
age of onset (8) 8
basophilic inclusions (8) 8
biophysics (8) 8
cell-free formation (8) 8
expression (8) 8
health aspects (8) 8
inclusions (8) 8
molecular biology (8) 8
motor neuron disease (8) 8
motor-neuron disease (8) 8
prion-like domains (8) 8
rna-binding protein fus - chemistry (8) 8
tar dna-binding protein 43 (8) 8
transcription (8) 8
adolescent (7) 7
basophilic inclusion body disease (7) 7
biocompatibility (7) 7
cancer (7) 7
dendritic spines (7) 7
disease models, animal (7) 7
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1. Full Text ALS-associated fused in sarcoma ( FUS ) mutations disrupt Transportin-mediated nuclear import
by Mackenzie, Ian R A and Capell, Anja and Neumann, Manuela and Dormann, Dorothee and Edbauer, Dieter and Fischer, Ingeborg and Schmid, Bettina and Rodde, Ramona and Bentmann, Eva and Hruscha, Alexander and Haass, Christian and Than, Manuel E
The EMBO Journal, ISSN 0261-4189, 08/2010, Volume 29, Issue 16, pp. 2841 - 2857
Mutations in fused in sarcoma (FUS) are a cause of familial amyotrophic lateral sclerosis (fALS). Patients carrying point mutations in the C‐terminus of FUS... 
fused in sarcoma (FUS) | stress granules | Transportin | amyotrophic lateral sclerosis (ALS) | frontotemporal lobar degeneration (FTLD) | LOCALIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MAMMALIAN STRESS GRANULES | AMYOTROPHIC-LATERAL-SCLEROSIS | MOTOR-NEURON DISEASE | FRONTOTEMPORAL LOBAR DEGENERATION | CELL BIOLOGY | DENDRITIC SPINES | BINDING PROTEIN TLS | MESSENGER-RNA | TDP-43 | GENE-EXPRESSION | Protein Structure, Tertiary | Amino Acid Sequence | Neurons - pathology | RNA-Binding Protein FUS - analysis | Cytoplasmic Granules - pathology | Amyotrophic Lateral Sclerosis - genetics | Humans | Cells, Cultured | Molecular Sequence Data | RNA-Binding Protein FUS - genetics | RNA-Binding Protein FUS - metabolism | Zebrafish - embryology | Gene Knockdown Techniques | RNA-Binding Protein FUS - chemistry | Point Mutation | Amyotrophic Lateral Sclerosis - pathology | Animals | Karyopherins - metabolism | Amyotrophic Lateral Sclerosis - metabolism | Karyopherins - genetics | Active Transport, Cell Nucleus | HeLa Cells | Proteins | Neurosciences | Cellular biology | Neurodegeneration | Amyotrophic lateral sclerosis | Mutation | Molecular biology | Gene expression
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2. Full Text Combined fused in sarcoma‐positive (FUS+) basophilic inclusion body disease and atypical tauopathy presenting with an amyotrophic lateral sclerosis/motor neurone disease (ALS/MND)‐plus phenotype
by Wharton, S. B and Verber, N. S and Wagner, B. E and Highley, J. R and Fillingham, D. J and Waller, R and Strand, K and Ince, P. G and Shaw, P. J
Neuropathology and Applied Neurobiology, ISSN 0305-1846, 10/2019, Volume 45, Issue 6, pp. 586 - 596
Aims Amyotrophic lateral sclerosis/motor neurone disease (ALS/MND) is characterized by the presence of inclusions containing TDP‐43 within motor neurones. In... 
amyotrophic lateral sclerosis | motor neurone disease | basophilic inclusion body disease | fused in sarcoma | atypical tauopathy | DEMENTIA | DEPOSITION | TAU | PATHOLOGY | VARIANT | NEUROSCIENCES | CLINICAL NEUROLOGY | DEGENERATION | GENE | TDP-43 | MUTATIONS | PROGRESSIVE SUPRANUCLEAR PALSY | Proteins | Immunohistochemistry | Medical research | Nervous system diseases | Sarcoma | Gene mutations | Medicine, Experimental | Genetic aspects | Phenotypes | Neurodegenerative diseases | Motor neurone disease | Cognitive ability | Case reports | Amyotrophic lateral sclerosis | Coexistence | Pathology | FUS protein | Tau protein | Motor neuron diseases | Neurodegeneration | Inclusion bodies | Point mutation
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3. Full Text Requirements for stress granule recruitment of fused in sarcoma (FUS) and TAR DNA-binding protein of 43 kDa (TDP-43)
by Bentmann, Eva and Neumann, Manuela and Tahirovic, Sabina and Rodde, Ramona and Dormann, Dorothee and Haass, Christian
Journal of Biological Chemistry, ISSN 0021-9258, 06/2012, Volume 287, Issue 27, pp. 23079 - 23094
Cytoplasmic inclusions containing TAR DNA-binding protein of 43 kDa (TDP-43) or Fused in sarcoma (FUS) are a hallmark of amyotrophic lateral sclerosis (ALS)... 
NEURONAL VULNERABILITY | NUCLEAR | SPLICING REGULATION | BASOPHILIC INCLUSIONS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | MUTATIONS | FRONTOTEMPORAL LOBAR DEGENERATION | HIPPOCAMPAL CORNU AMMONIS-1 | C-TERMINAL FRAGMENTS | Frontotemporal Lobar Degeneration - pathology | Glycine - metabolism | Spinal Cord - metabolism | Humans | Cerebral Cortex - pathology | Glutamine - metabolism | Cerebral Cortex - metabolism | DNA-Binding Proteins - metabolism | RNA-Binding Protein FUS - chemistry | Mutation - physiology | Frontotemporal Lobar Degeneration - metabolism | Spinal Cord - pathology | Binding Sites - physiology | Inclusion Bodies - metabolism | RNA - metabolism | Stress, Physiological - physiology | Poly(A)-Binding Protein I - metabolism | RNA-Binding Protein FUS - genetics | Hippocampus - pathology | RNA-Binding Protein FUS - metabolism | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Hippocampus - metabolism | Amyotrophic Lateral Sclerosis - pathology | Amyotrophic Lateral Sclerosis - metabolism | Inclusion Bodies - pathology | Zinc Fingers - physiology | HeLa Cells | Fused in Sarcoma (FUS) | Neurodegenerative Diseases | Frontotemporal Lobar Degeneration (FTLD) | Neurodegeneration | Stress Granule | Neurobiology | TAR DNA-binding Protein of 43 kDa (TDP-43) | Amyotrophic Lateral Sclerosis (Lou Gehrig's Disease) | RNA-binding Protein
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4. Full Text Nuclear carrier and RNA‐binding proteins in frontotemporal lobar degeneration associated with fused in sarcoma (FUS) pathological changes
by Davidson, Y. S and Robinson, A. C and Hu, Q and Mishra, M and Baborie, A and Jaros, E and Perry, R. H and Cairns, N. J and Richardson, A and Gerhard, A and Neary, D and Snowden, J. S and Bigio, E. H and Mann, D. M. A
Neuropathology and Applied Neurobiology, ISSN 0305-1846, 02/2013, Volume 39, Issue 2, pp. 157 - 165
Y. S. Davidson, A. C. Robinson, Q. Hu, M. Mishra, A. Baborie, E. Jaros, R. H. Perry, N. J. Cairns, A. Richardson, A. Gerhard, D. Neary, J. S. Snowden, E. H.... 
TATA‐binding protein‐associated factor 15 | transportins | TDP‐43 | Ewing's sarcoma protein | frontotemporal lobar degeneration | fused in sarcoma | Transportins | Frontotemporal lobar degeneration | Fused in sarcoma | TATA-binding protein-associated factor 15 | TDP-43 | EWS | TAF15 | DEMENTIA | INCLUSIONS | CONSENSUS | AMYOTROPHIC-LATERAL-SCLEROSIS | PATHOLOGY | NEUROSCIENCES | CLINICAL NEUROLOGY | EXPRESSION PATTERNS | HETEROGENEITY | GENE | MUTATIONS | DNA-Binding Proteins - metabolism | TATA-Binding Protein Associated Factors - metabolism | Frontotemporal Lobar Degeneration - metabolism | Humans | Middle Aged | Adult | Female | Male | RNA-Binding Protein FUS - metabolism | beta Karyopherins - metabolism | Inclusion Bodies - metabolism | RNA-Binding Protein EWS - metabolism | Neurosciences | Sarcoma | Questions and answers | Physiological aspects | Universities and colleges | Binding proteins | Protein binding | Proteins | Fused in Sarcoma | Frontotemporal Lobar degeneration | Ewing’s sarcoma protein
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5. Full Text Long noncoding RNA SchLAH suppresses metastasis of hepatocellular carcinoma through interacting with fused in sarcoma
by Ge, Zhouhong and Cheng, Zhuoan and Yang, Xinrong and Huo, Xisong and Wang, Ning and Wang, Hui and Wang, Cun and Gu, Dishui and Zhao, Fangyu and Yao, Ming and Fan, Jia and Qin, Wenxin
Cancer Science, ISSN 1347-9032, 04/2017, Volume 108, Issue 4, pp. 653 - 662
Emerging evidence has indicated that deregulation of long non‐coding RNAs (lncRNAs) can contribute to the progression and metastasis of human cancer, including... 
long noncoding RNA | Fused in sarcoma | metastasis | hepatocellular carcinoma | SchLAH | CELLS | IDENTIFICATION | LIVER-CANCER | ONCOLOGY | SIGNALING PATHWAY | POOR-PROGNOSIS | BINDING PROTEINS | DISEASE | EPIGENETIC REGULATION | FUS/TLS | EXPRESSION | Prognosis | Humans | Gene Expression Regulation, Neoplastic | Transplantation, Heterologous | rhoA GTP-Binding Protein - metabolism | rhoA GTP-Binding Protein - genetics | Cell Movement - genetics | Neoplasm Metastasis | RNA Interference | Carcinoma, Hepatocellular - genetics | Liver Neoplasms - pathology | Liver Neoplasms - genetics | RNA-Binding Protein FUS - genetics | RNA, Long Noncoding - genetics | RNA-Binding Protein FUS - metabolism | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Hep G2 Cells | Animals | Mice, Nude | Carcinoma, Hepatocellular - pathology | Liver Neoplasms - metabolism | Cell Line, Tumor | Protein Binding | Mice, Inbred BALB C | RNA, Long Noncoding - metabolism | rac1 GTP-Binding Protein - metabolism | Carcinoma, Hepatocellular - metabolism | rac1 GTP-Binding Protein - genetics | Development and progression | Antisense RNA | Metastasis | Hepatoma | Sarcoma | Analysis | Index Medicus | Original
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6. Full Text The RNA-binding protein fused in sarcoma (FUS) functions downstream of poly(ADP-ribose) polymerase (PARP) in response to DNA damage
by Mastrocola, Adam S and Kim, Sang Hwa and Trinh, Anthony T and Rodenkirch, Lance A and Tibbetts, Randal S
Journal of Biological Chemistry, ISSN 0021-9258, 08/2013, Volume 288, Issue 34, pp. 24731 - 24741
The list of factors that participate in the DNA damage response to maintain genomic stability has expanded significantly to include a role for proteins... 
CELL-FREE FORMATION | REPAIR | ACTIVATION | GENE | PHOSPHORYLATION | TDP-43 | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | DOUBLE-STRAND BREAKS | HISTONE H2AX | AMYOTROPHIC-LATERAL-SCLEROSIS | Lasers - adverse effects | Protein Structure, Tertiary | Humans | DNA Repair - physiology | Genomic Instability - physiology | RNA-Binding Protein FUS - genetics | RNA-Binding Protein FUS - metabolism | DNA Breaks, Double-Stranded | Poly Adenosine Diphosphate Ribose - genetics | Poly Adenosine Diphosphate Ribose - metabolism | Poly(ADP-ribose) Polymerases - metabolism | Poly(ADP-ribose) Polymerases - genetics | Cell Line, Tumor | DNA Damage Response | DNA and Chromosomes | Fused in Sarcoma | DNA Repair | Radiation Biology | RNA-binding Proteins | Homologous Recombination | ATM | PARP
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7. Full Text Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative Diseases
by Chen, C and Ding, XF and Akram, N and Xue, S and Luo, SZ
MOLECULES, ISSN 1420-3049, 04/2019, Volume 24, Issue 8, p. 1622
Fused in sarcoma (FUS) is a DNA/RNA binding protein that is involved in RNA metabolism and DNA repair. Numerous reports have demonstrated by pathological and... 
FUS/TLS GENE | self-assemble | BIOCHEMISTRY & MOLECULAR BIOLOGY | aggregation | AMYOTROPHIC-LATERAL-SCLEROSIS | prion-like domains | FRONTOTEMPORAL LOBAR DEGENERATION | NUCLEAR-LOCALIZATION SIGNAL | CHEMISTRY, MULTIDISCIPLINARY | RNA-BINDING PROTEINS | neurodegenerative diseases | FET PROTEINS | phase separation | CELL-FREE FORMATION | ABERRANT PHASE-TRANSITIONS | fused in sarcoma (FUS) | phase transition | IMPORT RECEPTOR
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8. Full Text Fused in sarcoma silences HIV gene transcription and maintains viral latency through suppressing AFF4 gene activation
by Krasnopolsky, S and Marom, L and Victor, RA and Kuzmina, A and Schwartz, JC and Fujinaga, K and Taube, R
RETROVIROLOGY, ISSN 1742-4690, 06/2019, Volume 16, Issue 1, pp. 16 - 19
BackgroundThe human immunodeficiency virus (HIV) cell reservoir is currently a main obstacle towards complete eradication of the virus. This infected pool is... 
RNA-POLYMERASE-II | DOMAIN | Transcription | PHOSPHORYLATION | Positive transcription elongation factor b | LIQUID DROPLETS | ELONGATION COMPLEX SEC | BINDING PROTEIN | Cyclin kinase 9 | Latency | AF4 | P-TEFB | PHASE-SEPARATION | FACTOR B | VIROLOGY | Super elongation complex | CYCLIN T1 | Phase separation | Elongation factor for RNA polymerase II 2ELL2 | FMR2 family member 4 | Fused in sarcomaFUS | Human immunodeficiency virus | RNA polymerase II | Antiviral agents | Sarcoma | RNA | Genes | Genomics | Genetic aspects | Genetic engineering | Genetic transcription | HIV (Viruses) | T cells | AF4/FMR2 family member 4
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9. Full Text Interaction of amyotrophic lateral sclerosis/frontotemporal lobar degeneration–associated fused-in-sarcoma with proteins involved in metabolic and protein degradation pathways
by Wang, Tao and Jiang, Xin and Chen, Gang and Xu, Jin
Neurobiology of Aging, ISSN 0197-4580, 2015, Volume 36, Issue 1, pp. 527 - 535
Abstract Fused-in-sarcoma (FUS) is a nuclear protein linked to amyotrophic lateral sclerosis and frontotemporal dementia. Under pathologic conditions, FUS... 
Neurology | Internal Medicine | Protein degradation | Valocin-containing protein (VCP) | Metabolic | Fused-in-sarcoma (FUS) | Amyotrophic lateral sclerosis (ALS) | Frontotemporal dementia (FTD) | SPINOCEREBELLAR ATAXIA TYPE-2 | PRION-LIKE DOMAINS | FRONTOTEMPORAL DEMENTIA | DNA-DAMAGE | SCLEROSIS | ALS | NEUROSCIENCES | GERIATRICS & GERONTOLOGY | RNA-BINDING PROTEINS | MESSENGER-RNAS | VCP MUTATIONS | STRESS GRANULES | Protein Interaction Maps - physiology | Amyotrophic Lateral Sclerosis - genetics | Humans | Valosin Containing Protein | Mutant Proteins - genetics | RNA-Binding Protein FUS - genetics | Mutant Proteins - metabolism | RNA-Binding Protein FUS - metabolism | RNA, Messenger - metabolism | Frontotemporal Lobar Degeneration - metabolism | Protein Interaction Maps - genetics | Proteolysis | Adenosine Triphosphate - metabolism | Amyotrophic Lateral Sclerosis - metabolism | HEK293 Cells | Protein Binding | Frontotemporal Lobar Degeneration - genetics | Energy Metabolism - genetics | Adenosine Triphosphatases - physiology | Cell Cycle Proteins - physiology | Ubiquitin | Sarcoma | Physiological aspects | Amyotrophic lateral sclerosis | Adenosine triphosphatase | Protein binding
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10. Full Text The RRM domain of human fused in sarcoma protein reveals a non-canonical nucleic acid binding site
by Liu, Xuehui and Niu, Chunyan and Ren, Jintao and Zhang, Jiayu and Xie, Xiaodong and Zhu, Haining and Feng, Wei and Gong, Weimin
BBA - Molecular Basis of Disease, ISSN 0925-4439, 02/2013, Volume 1832, Issue 2, pp. 375 - 385
Fused in sarcoma (FUS) is involved in many processes of RNA metabolism. FUS and another RNA binding protein, TDP-43, are implicated in amyotrophic lateral... 
Amyotrophic lateral sclerosis | NMR | Fused in sarcoma | Surface plasmon resonance | Nucleic acid binding | RNA recognition motif | RNA-POLYMERASE-II | TET FAMILY | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | NMR SYSTEM | TLS/FUS | BIOPHYSICS | TDP-43 | DNA | TLS | PROTEOMIC ANALYSIS | Sequence Homology, Amino Acid | Surface Plasmon Resonance | Amino Acid Sequence | Animals | Humans | RNA-Binding Proteins - chemistry | Models, Molecular | Molecular Sequence Data | Nuclear Magnetic Resonance, Biomolecular | Nucleic Acids - metabolism | Binding Sites | RNA-Binding Proteins - metabolism | Sarcoma | RNA | Analysis | Physiological aspects | Chemical properties | Protein binding | Index Medicus
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11. Full Text Expression of Fused in sarcoma mutations in mice recapitulates the neuropathology of FUS proteinopathies and provides insight into disease pathogenesis
by Verbeeck, Christophe and Deng, Qiudong and Dejesus-Hernandez, Mariely and Taylor, Georgia and Ceballos-Diaz, Carolina and Kocerha, Jannet and Golde, Todd and Das, Pritam and Rademakers, Rosa and Dickson, Dennis W and Kukar, Thomas
Molecular Neurodegeneration, ISSN 1750-1326, 2012, Volume 7, Issue 1, pp. 53 - 53
Background: Mutations in the gene encoding the RNA-binding protein fused in sarcoma (FUS) can cause familial and sporadic amyotrophic lateral sclerosis (ALS)... 
Ubiquitin | Neuronal cytoplasmic inclusions | Adeno-associated virus | PABP-1 | RNA dysfunction | α-internexin | Amyotrophic lateral sclerosis | Frontotemporal lobar degeneration | p62/SQSTM1 | Transgenic mouse models | Fused in sarcoma proteinopathies | Stress granules | INCLUSIONS | DROSOPHILA MODEL | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | NEUROSCIENCES | BETA | RNA-BINDING PROTEINS | MESSENGER-RNA | GENE | TDP-43 | FUS/TLS | alpha-internexin | Immunohistochemistry | Neurons - pathology | Amyotrophic Lateral Sclerosis - genetics | Humans | Nerve Degeneration - genetics | RNA-Binding Protein FUS - genetics | Mice, Transgenic | RNA-Binding Protein FUS - metabolism | Nerve Degeneration - metabolism | Nerve Degeneration - pathology | Brain - metabolism | Amyotrophic Lateral Sclerosis - pathology | Inclusion Bodies - genetics | Animals | Amyotrophic Lateral Sclerosis - metabolism | Brain - pathology | Inclusion Bodies - pathology | Mice | Neurons - metabolism | Mutation | Inclusion Bodies - metabolism | Disease Models, Animal | Nervous system diseases | Sarcoma | RNA | Neurons | Physiological aspects | Genetic aspects | Health aspects | Dementia | Protein binding | Proteins | Pathology | Medical research | Disease | Brain | Neurodegenerative diseases | Neuropathology | Intermediate filaments | Data processing | Angiogenin | Metabolism | Cytomegalic inclusion disease | FUS protein | RNA-binding protein | Inclusion bodies | Dementia disorders | Frontotemporal dementia | Cytoplasm
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