PLAAC: A web and command-line application to identify proteins with prion-like amino acid composition

Bioinformatics

Volumn 30, Issue 17, 2014, Pages 2501-2502

  Lancaster, Alex K ^a,b,c   Nutter Upham, Andrew ^a   Lindquist, Susan ^a,d,e   King, Oliver D ^f  

^a WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

^b BETH ISRAEL DEACONESS MEDICAL CENTER   (United States)

^c Harvard Medical School Center for Biomedical Informatics   (United States)

^d Department of Biology ^*  (United States)

^e MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^f UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; PRION; SACCHAROMYCES CEREVISIAE PROTEIN;

ALGORITHM; CHEMISTRY; COMPUTER PROGRAM; INTERNET; PRION; SEQUENCE ANALYSIS;

ALGORITHMS; AMINO ACIDS; INTERNET; PRIONS; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ANALYSIS, PROTEIN; SOFTWARE;

EID: 84907029459     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btu310     Document Type: Article

References (8)

1. Alberti, S. et al. (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell, 137, 146-158.
2. Holmes, D.L. et al. (2013) Heritable remodeling of yeast multicellularity by an environmentally responsive prion. Cell, 153, 153-165.
3. Kim, H.J. et al. (2013) Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature, 495, 467-473.
4. King, O.D. et al. (2012) The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res., 1462, 61-80.
5. Newby, G.A. and Lindquist, S. (2013) Blessings in disguise: biological benefits of prion-like mechanisms. Trends Cell Biol., 23, 251-259.
6. Prilusky, J. et al. (2005) FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics, 21, 3435-3438.
7. Toombs, J.A. et al. (2010) Compositional determinants of prion formation in yeast. Mol. Cell. Biol, 30, 319-332.
8. Toombs, J.A. et al. (2012) De novo design of synthetic prion domains. Proc. Natl Acad. Sci. USA, 109, 6519-6524.