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Prion variants and species barriers among Saccharomyces Ure2 proteins.

Edskes HK, McCann LM, Hebert AM, Wickner RB.

Genetics. 2009 Mar;181(3):1159-67. doi: 10.1534/genetics.108.099929. Epub 2009 Jan 5.


Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein.

Edskes HK, Wickner RB.

Proc Natl Acad Sci U S A. 2002 Dec 10;99 Suppl 4:16384-91. Epub 2002 Aug 12.


The [URE3] prion is not conserved among Saccharomyces species.

Talarek N, Maillet L, Cullin C, Aigle M.

Genetics. 2005 Sep;171(1):23-34. Epub 2005 Jun 14.


Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae.

Shewmaker F, Mull L, Nakayashiki T, Masison DC, Wickner RB.

Genetics. 2007 Jul;176(3):1557-65. Epub 2007 May 16.


Primary sequence independence for prion formation.

Ross ED, Edskes HK, Terry MJ, Wickner RB.

Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12825-30. Epub 2005 Aug 25.


Conservation of the prion properties of Ure2p through evolution.

Baudin-Baillieu A, Fernandez-Bellot E, Reine F, Coissac E, Cullin C.

Mol Biol Cell. 2003 Aug;14(8):3449-58. Epub 2003 May 18.


Scrambled prion domains form prions and amyloid.

Ross ED, Baxa U, Wickner RB.

Mol Cell Biol. 2004 Aug;24(16):7206-13.


Prion-forming ability of Ure2 of yeasts is not evolutionarily conserved.

Edskes HK, Engel A, McCann LM, Brachmann A, Tsai HF, Wickner RB.

Genetics. 2011 May;188(1):81-90. doi: 10.1534/genetics.111.127217. Epub 2011 Mar 2.


Prion generation in vitro: amyloid of Ure2p is infectious.

Brachmann A, Baxa U, Wickner RB.

EMBO J. 2005 Sep 7;24(17):3082-92. Epub 2005 Aug 11.


The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation.

Masison DC, Maddelein ML, Wickner RB.

Proc Natl Acad Sci U S A. 1997 Nov 11;94(23):12503-8.


The cellular concentration of the yeast Ure2p prion protein affects its propagation as a prion.

Crapeau M, Marchal C, Cullin C, Maillet L.

Mol Biol Cell. 2009 Apr;20(8):2286-96. doi: 10.1091/mbc.E08-11-1097. Epub 2009 Feb 18.


A promiscuous prion: efficient induction of [URE3] prion formation by heterologous prion domains.

Ross CD, McCarty BR, Hamilton M, Ben-Hur A, Ross ED.

Genetics. 2009 Nov;183(3):929-40. doi: 10.1534/genetics.109.109322. Epub 2009 Sep 14.


Internal initiation drives the synthesis of Ure2 protein lacking the prion domain and affects [URE3] propagation in yeast cells.

Komar AA, Lesnik T, Cullin C, Merrick WC, Trachsel H, Altmann M.

EMBO J. 2003 Mar 3;22(5):1199-209.


Structure of the prion Ure2p in protein fibrils assembled in vitro.

Fay N, Redeker V, Savistchenko J, Dubois S, Bousset L, Melki R.

J Biol Chem. 2005 Nov 4;280(44):37149-58. Epub 2005 Aug 30.


In vitro analysis of SpUre2p, a prion-related protein, exemplifies the relationship between amyloid and prion.

Immel F, Jiang Y, Wang YQ, Marchal C, Maillet L, Perrett S, Cullin C.

J Biol Chem. 2007 Mar 16;282(11):7912-20. Epub 2007 Jan 17.


The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments.

Edskes HK, Gray VT, Wickner RB.

Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1498-503.


Hydrogen/deuterium exchange mass spectrometric analysis of conformational changes accompanying the assembly of the yeast prion Ure2p into protein fibrils.

Redeker V, Halgand F, Le Caer JP, Bousset L, Laprévote O, Melki R.

J Mol Biol. 2007 Jun 15;369(4):1113-25. Epub 2007 Apr 12.

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