VIAF

Virtual International Authority File

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Leader 00000nz a2200037n 45 0
001 WKP|Q51184537 (VIAF cluster) (Authority/Source Record)
003 WKP
005 20241120235906.0
008 241120nneanz||abbn n and d
035 ‎‡a (WKP)Q51184537‏
024 ‎‡a 0000-0002-6473-9977‏ ‎‡2 orcid‏
024 ‎‡a 7202436864‏ ‎‡2 scopus‏
035 ‎‡a (OCoLC)Q51184537‏
100 0 ‎‡a اريك دي. روس‏ ‎‡9 ar‏
400 0 ‎‡a Eric D. Ross‏ ‎‡c researcher‏ ‎‡9 en‏
400 0 ‎‡a Eric D Ross‏ ‎‡c wetenschapper‏ ‎‡9 nl‏
670 ‎‡a Author's Atypical structural tendencies among low-complexity domains in the Protein Data Bank proteome‏
670 ‎‡a Author's Composition-based prediction and rational manipulation of prion-like domain recruitment to stress granules‏
670 ‎‡a Author's Compositional determinants of prion formation in yeast‏
670 ‎‡a Author's Controlling the prion propensity of glutamine/asparagine-rich proteins.‏
670 ‎‡a Author's Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1.‏
670 ‎‡a Author's Fitting yeast and mammalian prion aggregation kinetic data with the Finke-Watzky two-step model of nucleation and autocatalytic growth‏
670 ‎‡a Author's Generating new prions by targeted mutation or segment duplication.‏
670 ‎‡a Author's Genetic interaction of hnRNPA2B1 and DNAJB6 in a Drosophila model of multisystem proteinopathy‏
670 ‎‡a Author's HMG proteins and DNA flexibility in transcription activation‏
670 ‎‡a Author's Hop modulates Hsp70/Hsp90 interactions in protein folding‏
670 ‎‡a Author's Improved quantitation of DNA curvature using ligation ladders.‏
670 ‎‡a Author's Increasing prion propensity by hydrophobic insertion.‏
670 ‎‡a Author's Interactions between non-identical prion proteins.‏
670 ‎‡a Author's Intrinsic protein disorder, amino acid composition, and histone terminal domains.‏
670 ‎‡a Author's Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS‏
670 ‎‡a Author's Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes‏
670 ‎‡a Author's Prion genetics: new rules for a new kind of gene‏
670 ‎‡a Author's Prions: proteins as genes and infectious entities.‏
670 ‎‡a Author's Proteome-scale relationships between local amino acid composition and protein fates and functions‏
670 ‎‡a Author's [PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain.‏
670 ‎‡a Author's Reporter assay systems for [URE3] detection and analysis‏
670 ‎‡a Author's Sequence features governing aggregation or degradation of prion-like proteins‏
670 ‎‡a Author's Sky1: at the intersection of prion-like proteins and stress granule regulation‏
670 ‎‡a Author's Strategies for identifying new prions in yeast‏
670 ‎‡a Author's The effects of amino acid composition on yeast prion formation and prion domain interactions‏
670 ‎‡a Author's The prion-like protein kinase Sky1 is required for efficient stress granule disassembly‏
670 ‎‡a Author's Yeast prions and human prion-like proteins: sequence features and prediction methods‏
909 ‎‡a (scopus) 7202436864‏ ‎‡9 1‏
909 ‎‡a (orcid) 0000000264739977‏ ‎‡9 1‏
919 ‎‡a yeastprionsandhumanprionlikeproteinssequencefeaturesandpredictionmethods‏ ‎‡A Yeast prions and human prion-like proteins: sequence features and prediction methods‏ ‎‡9 1‏
919 ‎‡a effectsofaminoacidcompositiononyeastprionformationandpriondomaininteractions‏ ‎‡A The effects of amino acid composition on yeast prion formation and prion domain interactions‏ ‎‡9 1‏
919 ‎‡a strategiesforidentifyingnewprionsinyeast‏ ‎‡A Strategies for identifying new prions in yeast‏ ‎‡9 1‏
919 ‎‡a sky1attheintersectionofprionlikeproteinsandstressgranuleregulation‏ ‎‡A Sky1: at the intersection of prion-like proteins and stress granule regulation‏ ‎‡9 1‏
919 ‎‡a sequencefeaturesgoverningaggregationordegradationofprionlikeproteins‏ ‎‡A Sequence features governing aggregation or degradation of prion-like proteins‏ ‎‡9 1‏
919 ‎‡a reporterassaysystemsfordetectionandanalysis‏ ‎‡A Reporter assay systems for [URE3] detection and analysis‏ ‎‡9 1‏
919 ‎‡a prionlikeproteinkinasesky1isrequiredforefficientstressgranuledisassembly‏ ‎‡A The prion-like protein kinase Sky1 is required for efficient stress granule disassembly‏ ‎‡9 1‏
919 ‎‡a proteomescalerelationshipsbetweenlocalaminoacidcompositionandproteinfatesandfunctions‏ ‎‡A Proteome-scale relationships between local amino acid composition and protein fates and functions‏ ‎‡9 1‏
919 ‎‡a prionsproteinsasgenesandinfectiousentities‏ ‎‡A Prions: proteins as genes and infectious entities.‏ ‎‡9 1‏
919 ‎‡a priongeneticsnewrulesforanewkindofgene‏ ‎‡A Prion genetics: new rules for a new kind of gene‏ ‎‡9 1‏
919 ‎‡a naturalandpathogenicproteinsequencevariationaffectingprionlikedomainswithinandacrosshumanproteomes‏ ‎‡A Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes‏ ‎‡9 1‏
919 ‎‡a mutationsinprionlikedomainsinhnrnpa2b1andhnrnpa1causemultisystemproteinopathyandals‏ ‎‡A Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS‏ ‎‡9 1‏
919 ‎‡a intrinsicproteindisorderaminoacidcompositionandhistoneterminaldomains‏ ‎‡A Intrinsic protein disorder, amino acid composition, and histone terminal domains.‏ ‎‡9 1‏
919 ‎‡a interactionsbetweennonidenticalprionproteins‏ ‎‡A Interactions between non-identical prion proteins.‏ ‎‡9 1‏
919 ‎‡a increasingprionpropensitybyhydrophobicinsertion‏ ‎‡A Increasing prion propensity by hydrophobic insertion.‏ ‎‡9 1‏
919 ‎‡a improvedquantitationofdnacurvatureusingligationladders‏ ‎‡A Improved quantitation of DNA curvature using ligation ladders.‏ ‎‡9 1‏
919 ‎‡a hmgproteinsanddnaflexibilityintranscriptionactivation‏ ‎‡A HMG proteins and DNA flexibility in transcription activation‏ ‎‡9 1‏
919 ‎‡a fittingyeastandmammalianprionaggregationkineticdatawiththefinkewatzky2stepmodelofnucleationandautocatalyticgrowth‏ ‎‡A Fitting yeast and mammalian prion aggregation kinetic data with the Finke-Watzky two-step model of nucleation and autocatalytic growth‏ ‎‡9 1‏
919 ‎‡a effectsofmutationsontheaggregationpropensityofthehumanprionlikeproteinhnrnpa2b1‏ ‎‡A Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1.‏ ‎‡9 1‏
919 ‎‡a maintenanceisdependentonthecompositionnotprimarysequenceoftheoligopeptiderepeatdomain‏ ‎‡A [PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain.‏ ‎‡9 1‏
919 ‎‡a controllingtheprionpropensityofglutamineasparaginerichproteins‏ ‎‡A Controlling the prion propensity of glutamine/asparagine-rich proteins.‏ ‎‡9 1‏
919 ‎‡a compositionaldeterminantsofprionformationinyeast‏ ‎‡A Compositional determinants of prion formation in yeast‏ ‎‡9 1‏
919 ‎‡a compositionbasedpredictionandrationalmanipulationofprionlikedomainrecruitmenttostressgranules‏ ‎‡A Composition-based prediction and rational manipulation of prion-like domain recruitment to stress granules‏ ‎‡9 1‏
919 ‎‡a atypicalstructuraltendenciesamonglowcomplexitydomainsintheproteindatabankproteome‏ ‎‡A Atypical structural tendencies among low-complexity domains in the Protein Data Bank proteome‏ ‎‡9 1‏
919 ‎‡a geneticinteractionofhnrnpa2b1anddnajb6inadrosophilamodelofmultisystemproteinopathy‏ ‎‡A Genetic interaction of hnRNPA2B1 and DNAJB6 in a Drosophila model of multisystem proteinopathy‏ ‎‡9 1‏
919 ‎‡a hopmodulateshsp70hsp90interactionsinproteinfolding‏ ‎‡A Hop modulates Hsp70/Hsp90 interactions in protein folding‏ ‎‡9 1‏
919 ‎‡a generatingnewprionsbytargetedmutationorsegmentduplication‏ ‎‡A Generating new prions by targeted mutation or segment duplication.‏ ‎‡9 1‏
996 ‎‡2 SUDOC|230554431
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996 ‎‡2 LIH|LNB:C_j_ER;=B_a_
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997 ‎‡a 0 0 lived 0 0‏ ‎‡9 1‏