| scholarly article | Q13442814 |
| P2093 | author name string | Frank P Shewmaker | |
| Shannon N Rhoads | |||
| Debra S Yee | |||
| Zachary T Monahan | |||
| P2860 | cites work | Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis | Q24605104 |
| Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids | Q24614859 | ||
| Generating a prion with bacterially expressed recombinant prion protein | Q24626352 | ||
| Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS | Q24629495 | ||
| ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import | Q24630100 | ||
| A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions | Q24632492 | ||
| Prions | Q24633319 | ||
| A systematic survey identifies prions and illuminates sequence features of prionogenic proteins | Q24658451 | ||
| Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis | Q26749169 | ||
| Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease | Q26753190 | ||
| Phosphorylation modulates clearance of alpha-synuclein inclusions in a yeast model of Parkinson's disease | Q27316174 | ||
| Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation | Q27325625 | ||
| Yeast prions are useful for studying protein chaperones and protein quality control | Q28081556 | ||
| Engineering enhanced protein disaggregases for neurodegenerative disease | Q28083809 | ||
| Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis | Q28131672 | ||
| Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis | Q28236796 | ||
| Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6 | Q28236805 | ||
| [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae | Q28237493 | ||
| TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis | Q28270779 | ||
| Saccharomyces Genome Database: the genomics resource of budding yeast | Q29616757 | ||
| Compositional determinants of prion formation in yeast | Q33558139 | ||
| Biology and genetics of prions causing neurodegeneration | Q33567229 | ||
| Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis | Q33769272 | ||
| Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS | Q33889532 | ||
| A yeast model of FUS/TLS-dependent cytotoxicity | Q33889537 | ||
| Strain-specific morphologies of yeast prion amyloid fibrils | Q33900709 | ||
| Prion generation in vitro: amyloid of Ure2p is infectious | Q33947121 | ||
| Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers. | Q33947263 | ||
| PLAAC: a web and command-line application to identify proteins with prion-like amino acid composition | Q34103079 | ||
| Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms. | Q34155410 | ||
| Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins | Q34241138 | ||
| Prions are a common mechanism for phenotypic inheritance in wild yeasts. | Q34254667 | ||
| In vitro generation of infectious scrapie prions. | Q34413661 | ||
| The effect of PRMT1-mediated arginine methylation on the subcellular localization, stress granules, and detergent-insoluble aggregates of FUS/TLS. | Q34477890 | ||
| Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells | Q34529852 | ||
| Mammalian ribosomal and chaperone protein RPS3A counteracts α-synuclein aggregation and toxicity in a yeast model system | Q34908991 | ||
| Understanding the role of TDP-43 and FUS/TLS in ALS and beyond. | Q35587208 | ||
| A yeast functional screen predicts new candidate ALS disease genes | Q35641365 | ||
| TDP-43 is intercellularly transmitted across axon terminals | Q36310560 | ||
| The chimeric FUS/TLS-CHOP fusion protein specifically induces liposarcomas in transgenic mice. | Q52168068 | ||
| The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS. | Q54967377 | ||
| Potentiating Hsp104 activity via phosphomimetic mutations in the middle domain | Q58621634 | ||
| Sequence features governing aggregation or degradation of prion-like proteins | Q58622949 | ||
| The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localization | Q58806144 | ||
| Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits | Q59049636 | ||
| Human DnaJB6 Antiamyloid Chaperone Protects Yeast from Polyglutamine Toxicity Separately from Spatial Segregation of Aggregates | Q91493627 | ||
| Inhibition of RNA lariat debranching enzyme suppresses TDP-43 toxicity in ALS disease models | Q36434528 | ||
| ALS-associated mutant FUS induces selective motor neuron degeneration through toxic gain of function | Q36548825 | ||
| A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity | Q36609145 | ||
| RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations | Q36626888 | ||
| FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis | Q36922849 | ||
| "Prion-proof" for [PIN+]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+] | Q36943265 | ||
| Specificity of the J-protein Sis1 in the propagation of 3 yeast prions | Q36954907 | ||
| The yeast Sup35NM domain propagates as a prion in mammalian cells | Q37062021 | ||
| The evolutionary scope and neurological disease linkage of yeast-prion-like proteins in humans | Q37125870 | ||
| TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity | Q37339064 | ||
| Nervous yeast: modeling neurotoxic cell death | Q37635480 | ||
| Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy | Q37681653 | ||
| Modeling ALS and FTLD proteinopathies in yeast: an efficient approach for studying protein aggregation and toxicity | Q37952582 | ||
| Yeast genetic screen reveals novel therapeutic strategy for ALS. | Q38227177 | ||
| Therapeutic reduction of ataxin-2 extends lifespan and reduces pathology in TDP-43 mice | Q38288366 | ||
| Ubiquitin-dependent proteolysis in yeast cells expressing neurotoxic proteins. | Q38393072 | ||
| Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion | Q38826332 | ||
| Neuron-to-Neuron Transfer of FUS in Drosophila Primary Neuronal Culture Is Enhanced by ALS-Associated Mutations. | Q38827430 | ||
| Prions on the run: How extracellular vesicles serve as delivery vehicles for self-templating protein aggregates | Q39237605 | ||
| The seeds of neurodegeneration: prion-like spreading in ALS | Q39247056 | ||
| A yeast model of optineurin proteinopathy reveals a unique aggregation pattern associated with cellular toxicity | Q39256992 | ||
| Mechanism of prion loss after Hsp104 inactivation in yeast | Q39459936 | ||
| Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations | Q39464446 | ||
| The role of Sis1 in the maintenance of the [RNQ+] prion | Q39645207 | ||
| Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies. | Q41378010 | ||
| Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1. | Q41662138 | ||
| A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ]. | Q41858961 | ||
| Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events | Q41905072 | ||
| Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity. | Q42378053 | ||
| Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy | Q42732668 | ||
| Neurotoxic 43-kDa TAR DNA-binding protein (TDP-43) triggers mitochondrion-dependent programmed cell death in yeast | Q42740351 | ||
| A bioinformatics method for identifying Q/N-rich prion-like domains in proteins | Q43591340 | ||
| Conformational variations in an infectious protein determine prion strain differences | Q44187524 | ||
| Overexpression of a conserved HSP40 chaperone reduces toxicity of several neurodegenerative disease proteins | Q47199278 | ||
| Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains | Q47752760 | ||
| Protein-only transmission of three yeast prion strains | Q47929764 | ||
| Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. | Q48183466 | ||
| Prion-like seeding and nucleation of intracellular amyloid-β. | Q50055793 | ||
| P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | amyotrophic lateral sclerosis | Q206901 |
| P304 | page(s) | 453 | |
| P577 | publication date | 2018-01-01 | |
| P1433 | published in | Frontiers in Molecular Neuroscience | Q27721913 |
| P1476 | title | Yeast Models of Prion-Like Proteins That Cause Amyotrophic Lateral Sclerosis Reveal Pathogenic Mechanisms | |
| P478 | volume | 11 |
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