{"id":127,"date":"2021-12-08T15:55:05","date_gmt":"2021-12-08T15:55:05","guid":{"rendered":"http:\/\/localhost:81\/wordpress\/?page_id=127"},"modified":"2025-09-22T23:14:52","modified_gmt":"2025-09-22T23:14:52","slug":"publications","status":"publish","type":"page","link":"https:\/\/rosslab.colostate.edu\/?page_id=127","title":{"rendered":"Publications"},"content":{"rendered":"\t\t
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  1. Cascarina SM, Ross ED. Protein activities driven by amino acid composition. JBC<\/em>\u00a02025.\u00a0 Pubmed<\/a><\/strong><\/li>
  2. Baer MH*, Cascarina SM*, Paul KR*, Ross ED. Rational tuning of the concentration-independent enrichment of prion-like domains in stress granules. J Mol Biol<\/em> 2024.\u00a0 Pubmed<\/a><\/strong>\u00a0 *Co-first authors<\/em><\/li>
  3. Cascarina SM, Ross ED. Identification of low-complexity domains by compositional signatures reveals class-specific frequencies and functions across the domains of life.\u00a0PLOS Comput Biol<\/em> 2024.\u00a0 Pubmed<\/strong><\/a>\u00a0 Download PDF<\/strong><\/a><\/li>
  4. Cascarina SM, Ross ED. The LCD-Composer webserver: high-specificity identification and functional analysis of low-complexity domains in proteins. Bioinformatics<\/em> 2022.\u00a0\u00a0Pubmed<\/a><\/strong>\u00a0 Download PDF<\/a><\/strong><\/li>
  5. Cascarina SM, Ross ED. Expansion and functional analysis of the SR-related protein family across the domains of life.\u00a0RNA<\/em> 2022. \u00a0Pubmed<\/a><\/strong>\u00a0 Download PDF<\/strong><\/a><\/li>
  6. Cascarina SM, Ross ED. Phase separation by the SARS-CoV-2 nucleocapsid protein: consensus and open questions. JBC<\/em> 2022.\u00a0 Pubmed<\/a><\/strong>\u00a0 Download PDF<\/strong><\/a><\/li>
  7. Cascarina SM, Kaplan JP, Elder MR, Brookbank L, Ross ED. Generalizable compositional\u00a0features influencing the proteostatic fates of polar low-complexity domains.\u00a0IJMS<\/em> 2021.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
  8. Cascarina SM, King DC, Osborne Nishimura E, Ross ED. LCD-Composer: an intuitive, composition-centric method enabling the identification and detailed functional mapping of low-complexity domains.\u00a0NAR Genom & Bioinform<\/em> 2021.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
  9. Fomicheva A, Ross ED. From prions to stress granules: defining the compositional features of prion-like domains that promote different types of assemblies.\u00a0IJMS<\/em> 2021.\u00a0 Pubmed<\/a>\u00a0 <\/strong>Download PDF<\/strong><\/a><\/li>
  10. Cascarina SM, Ross ED. A proposed role for the SARS-CoV-2 nucleocapsid protein in the formation and regulation of biomolecular condensates.\u00a0FASEB J<\/em> 2020.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
  11. Boncella AE*, Shattuck JE*, Cascarina SM, Paul KR, Baer MH, Fomicheva A, Lamb AK, Ross ED. Composition-based prediction and rational manipulation of prion-like domain recruitment to stress granules. Proc Nat Acad Sci<\/em>\u00a02020.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a>\u00a0<\/strong> *Co-first authors<\/em><\/li>
  12. Cascarina SM, Elder MR, Ross ED. Atypical structural tendencies among low-complexity domains in the Protein Data Bank proteome.\u00a0PLOS Comput Biol<\/em> 2020.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
  13. Cascarina SM, Ross ED. Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes.\u00a0BMC Genom<\/em> 2020.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
  14. Shattuck JE, Cascarina SM, Paul KR, Ross ED. Sky1: at the intersection of prion-like proteins and stress granule regulation. Curr Genet<\/em> 2020. Pubmed<\/a><\/strong><\/li>
  15. Shattuck JE, Paul KR, Cascarina SM, Ross ED. The prion-like protein kinase Sky1 is required for efficient stress granule disassembly.\u00a0Nat Commun<\/em> 2019.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
  16. Cascarina SM, Ross ED. Aggregation and degradation scales for prion-like domains: sequence features and context weigh in.\u00a0Curr Genet<\/em> 2019.\u00a0 Pubmed<\/a><\/strong><\/li>
  17. Cascarina SM, Ross ED. Proteome-scale relationships between local amino acid composition and protein fates and functions.\u00a0PLOS Comput Biol<\/em> 2018.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
  18. Cascarina SM, Paul KR, Machihara S, Ross ED. Sequence features governing aggregation or degradation of prion-like proteins.\u00a0PLOS Genet<\/em> 2018.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
  19. Cascarina SM, Paul KR, Ross ED. Manipulating the aggregation activity of human prion-like proteins.\u00a0Prion<\/em> 2017.\u00a0 Pubmed<\/a><\/strong><\/li>
  20. Shattuck JE, Waechter AC, Ross ED. The effects of glutamine\/asparagine content on aggregation and heterologous prion induction by yeast prion-like domains.\u00a0Prion<\/em> 2017.\u00a0 Pubmed<\/a><\/strong><\/li>
  21. Afsar Minhas F ul A, Ross ED, Ben-Hur A. Amino acid composition predicts prion activity.\u00a0PLOS Comput Biol<\/em> 2017.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
  22. Paul KR, Molliex A, Cascarina S, Boncella AE, Taylor J, Ross ED. Effects of mutations on the aggregation propensity of the human prion-like protein hnRNPA2B1.\u00a0Mol Cell Biol<\/em> 2017.\u00a0 Pubmed<\/a><\/strong><\/li><\/ol>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t
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    Select Prior Publications<\/h2>\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t
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    1. Paul KR, Hendrich CG, Waechter A, Harman MR, Ross ED. Generating new prions by targeted mutation or segment duplication.\u00a0Proc Natl Acad Sci<\/em> 2015.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
    2. Gonzalez Nelson AC, Paul KR, Petri M, Flores N, Rogge RA, Cascarina SM, Ross ED. Increasing prion propensity by hydrophobic insertion.\u00a0PLOS One<\/em> 2014.\u00a0 Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
    3. Cascarina SM, Ross ED. Yeast prions and human prion-like proteins: sequence features and prediction methods.\u00a0Cell Mol Life Sci<\/em> 2014.\u00a0 Pubmed<\/a><\/strong><\/li>
    4. Kim\u00a0et al.<\/em>. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS.\u00a0Nature<\/em> 2013.\u00a0 Pubmed<\/a><\/strong><\/li>
    5. Toombs JA, Petri M, Paul KR, Kan GY, Ben-Hur A, Ross ED. De novo design of synthetic prion domains.\u00a0Proc Natl Acad Sci<\/em> 2012. Pubmed<\/a>\u00a0 Download PDF<\/a><\/strong><\/li>
    6. Toombs JA, McCarty BR, Ross ED. Compositional determinants of prion formation in yeast.\u00a0Mol Cell Biol<\/em> 2010.\u00a0 Pubmed<\/a><\/strong><\/li>
    7. Ross ED, Edskes HK, Terry MJ, Wickner RB. Primary sequence independence for prion formation.\u00a0Proc Natl Acad Sci<\/em> 2005.\u00a0 Pubmed<\/a><\/strong><\/li>
    8. Ross ED, Baxa U, Wickner RB. Scrambled prion domains form prions and amyloid.\u00a0Mol Cell Biol<\/em> 2004.\u00a0 Pubmed<\/a><\/strong><\/li><\/ol>\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t<\/section>\n\t\t\t\t<\/div>\n\t\t","protected":false},"excerpt":{"rendered":"

      Recent Publications Cascarina SM, Ross ED. Protein activities driven by amino acid composition. JBC\u00a02025.\u00a0 Pubmed Baer MH*, Cascarina SM*, Paul KR*, Ross ED. Rational tuning of the concentration-independent enrichment of […]<\/p>\n","protected":false},"author":2,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_monsterinsights_skip_tracking":false,"_monsterinsights_sitenote_active":false,"_monsterinsights_sitenote_note":"","_monsterinsights_sitenote_category":0,"footnotes":""},"class_list":["post-127","page","type-page","status-publish","hentry","post-preview"],"aioseo_notices":[],"_links":{"self":[{"href":"https:\/\/rosslab.colostate.edu\/index.php?rest_route=\/wp\/v2\/pages\/127","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/rosslab.colostate.edu\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/rosslab.colostate.edu\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/rosslab.colostate.edu\/index.php?rest_route=\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"https:\/\/rosslab.colostate.edu\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=127"}],"version-history":[{"count":57,"href":"https:\/\/rosslab.colostate.edu\/index.php?rest_route=\/wp\/v2\/pages\/127\/revisions"}],"predecessor-version":[{"id":557,"href":"https:\/\/rosslab.colostate.edu\/index.php?rest_route=\/wp\/v2\/pages\/127\/revisions\/557"}],"wp:attachment":[{"href":"https:\/\/rosslab.colostate.edu\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=127"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}