Molecular Basis of a Yeast Prion Species Barrier

[1]  Y. Chernoff,et al.  Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae. , 1999, Genetics.

[2]  P. Lansbury,et al.  Amyloid diseases: abnormal protein aggregation in neurodegeneration. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[3]  S. Lindquist,et al.  Oligopeptide-repeat expansions modulate ‘protein-only’ inheritance in yeast , 1999, Nature.

[4]  B. Tabashnik,et al.  Development time and resistance to Bt crops , 1999, Nature.

[5]  B. Caughey,et al.  Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease‐resistant state , 1999, The EMBO journal.

[6]  M. Tuite,et al.  Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion‐mediated mechanism , 1999, The EMBO journal.

[7]  P. Lansbury Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[8]  S. Lindquist,et al.  The yeast non‐Mendelian factor [ETA+] is a variant of [PSI+], a prion‐like form of release factor eRF3 , 1999, The EMBO journal.

[9]  R. Wickner,et al.  The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[10]  R. Wickner,et al.  The [ URE 3 ] prion is an aggregated form of Ure 2 p that can be cured by overexpression of Ure 2 p fragments , 1999 .

[11]  Y. Nakamura,et al.  The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast. , 1998, RNA.

[12]  S. W. Davies,et al.  Polyglutamine expansion and Huntington's disease. , 1998, Biochemical Society transactions.

[13]  J. Weissman,et al.  A Critical Role for Amino-Terminal Glutamine/Asparagine Repeats in the Formation and Propagation of a Yeast Prion , 1998, Cell.

[14]  F. Cohen,et al.  Prion Protein Biology , 1998, Cell.

[15]  S. Paushkin,et al.  In vitro propagation of the prion-like state of yeast Sup35 protein. , 1997, Science.

[16]  K. Wüthrich,et al.  Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[17]  S. Lindquist,et al.  Self-Seeded Fibers Formed by Sup35, the Protein Determinant of [PSI +], a Heritable Prion-like Factor of S. cerevisiae , 1997, Cell.

[18]  S. Lindquist,et al.  Mad Cows Meet Psi-chotic Yeast: The Expansion of the Prion Hypothesis , 1997, Cell.

[19]  C. Blake,et al.  The structure of amyloid fibrils by electron microscopy and X-ray diffraction. , 1997, Advances in protein chemistry.

[20]  Y. Chernoff,et al.  Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. , 1996, Genetics.

[21]  J R Glover,et al.  Support for the Prion Hypothesis for Inheritance of a Phenotypic Trait in Yeast , 1996, Science.

[22]  S. Paushkin,et al.  Propagation of the yeast prion‐like [psi+] determinant is mediated by oligomerization of the SUP35‐encoded polypeptide chain release factor. , 1996, The EMBO journal.

[23]  J. Thompson,et al.  Using CLUSTAL for multiple sequence alignments. , 1996, Methods in enzymology.

[24]  R. Wickner,et al.  [PSI] and [URE3] as yeast prions , 1995, Yeast.

[25]  F. Cohen,et al.  Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein , 1995, Cell.

[26]  S W Liebman,et al.  Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. , 1995, Science.

[27]  P. Lansbury,et al.  Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[28]  P. Lansbury,et al.  The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease? , 1995, Chemistry & biology.

[29]  C. Kurtzman Molecular taxonomy of the yeasts , 1994, Yeast.

[30]  C. Nierras,et al.  The dominant PNM2- mutation which eliminates the psi factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. , 1994, Genetics.

[31]  R. Wickner,et al.  [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. , 1994, Science.

[32]  P E Fraser,et al.  A kinetic model for amyloid formation in the prion diseases: importance of seeding. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[33]  Y. Chernoff,et al.  Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non‐overlapping functional regions in the encoded protein , 1993, Molecular microbiology.

[34]  M. Frohman,et al.  Rapid amplification of complementary DNA ends for generation of full-length complementary DNAs: thermal RACE. , 1993, Methods in enzymology.

[35]  I. Tolstorukov,et al.  Divergence and conservation of SUP2(SUP35) gene of yeasts Pichia pinus and Saccharomyces cerevisiae , 1990, Yeast.

[36]  D. Agard,et al.  Fluorescence microscopy in three dimensions. , 1989, Methods in cell biology.

[37]  K. Struhl,et al.  Current Protocols in Molecular Biology (New York: Greene Publishing Associates and Wiley-Interscience). Host-Range Shuttle System for Gene Insertion into the Chromosomes of Gram-negative Bacteria. , 1988 .

[38]  M. Tuite,et al.  Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae. , 1981, Genetics.

[39]  a Kinetic Model , 2022 .

[40]  D. Cheresh URE 3 ] as an Altered URE 2 Protein : Evidence for a Prion Analog in Saccharomyces cerevisiae , 2022 .