A transforming principle

Cell

Volumn 120, Issue 2, 2005, Pages 153-154

  Fink, Gerald R ^a  

^a WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL GENE; BACTERIAL VIRULENCE; CELL TRANSFORMATION; CHEMICAL COMPOSITION; MEIOSIS; NONHUMAN; PRIORITY JOURNAL; PROGENY; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FOLDING; SHORT SURVEY; YEAST;

BACTERIA (MICROORGANISMS);

EID: 12944324228     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2005.01.004     Document Type: Note

References (9)

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2. +], a heritable prion-like factor of S. cerevisiae. Cell. 89:1997;811-819
3. Griffith F. The significance of pneumococcal types. J. Hyg.(Lond.). 27:1928;113-159
4. King C.Y., Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature. 428:2004;319-323
5. Liebman S. Progress toward an ultimate proof of the prion hypothesis. Proc. Natl. Acad. Sci. USA. 99:2002;9098-9100
6. Maddelein M.L., Dos Reis S., Duvezin-Caubet S., Coulary-Salin B., Saupe S.J. Amyloid aggregates of the HET-s prion protein are infectious. Proc. Natl. Acad. Sci. USA. 99:2002;7402-7407
7. +] factor by in vitro-converted Sup35 protein Science. 289:2000;595-599
8. Tanaka M., Chien P., Naber N., Cooke R., Weissman J. Conformational variations in an infectious protein determine prion strain differences. Nature. 428:2004;323-327
9. Wickner R.B. [URE3] as an altered URE2 protein. evidence for a prion analog in Saccharomyces cerevisiae Science. 264:2001;566-569