Science 12 May 1995: Vol. 268. no. 5212, pp. 880 - 884 DOI: 10.1126/science.7754373

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Articles

Design and construction of diverse mammalian prion strains.

D. W. Colby, K. Giles, G. Legname, H. Wille, I. V. Baskakov, S. J. DeArmond, and S. B. Prusiner (2009)
PNAS 106, 20417-20422
 |  Abstract »  |  Full Text »  |  PDF »

A heritable switch in carbon source utilization driven by an unusual yeast prion.

J. C.S. Brown and S. Lindquist (2009)
Genes & Dev. 23, 2320-2332
 |  Abstract »  |  Full Text »  |  PDF »

Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine-HCl-treated [PSI+] cells.

S. Kawai-Noma, C.-G. Pack, T. Tsuji, M. Kinjo, and H. Taguchi (2009)
Genes Cells 14, 1045-1054
 |  Abstract »  |  Full Text »  |  PDF »

Mutants of the Paf1 Complex Alter Phenotypic Expression of the Yeast Prion [PSI+].

L. A. Strawn, C. A. Lin, E. M.H. Tank, M. M. Osman, S. A. Simpson, and H. L. True (2009)
Mol. Biol. Cell 20, 2229-2241
 |  Abstract »  |  Full Text »  |  PDF »

The Cellular Concentration of the Yeast Ure2p Prion Protein Affects Its Propagation as a Prion.

M. Crapeau, C. Marchal, C. Cullin, and L. Maillet (2009)
Mol. Biol. Cell 20, 2286-2296
 |  Abstract »  |  Full Text »  |  PDF »

A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen.

J. Nemecek, T. Nakayashiki, and R. B. Wickner (2009)
PNAS 106, 1892-1896
 |  Abstract »  |  Full Text »  |  PDF »

The Type I Hsp40 Ydj1 Utilizes a Farnesyl Moiety and Zinc Finger-like Region to Suppress Prion Toxicity.

D. W. Summers, P. M. Douglas, H.-Y. Ren, and D. M. Cyr (2009)
J. Biol. Chem. 284, 3628-3639
 |  Abstract »  |  Full Text »  |  PDF »

The NatA Acetyltransferase Couples Sup35 Prion Complexes to the [PSI+] Phenotype.

J. A. Pezza, S. X. Langseth, R. Raupp Yamamoto, S. M. Doris, S. P. Ulin, A. R. Salomon, and T. R. Serio (2009)
Mol. Biol. Cell 20, 1068-1080
 |  Abstract »  |  Full Text »  |  PDF »

A G-protein {gamma} subunit mimic is a general antagonist of prion propagation in Saccharomyces cerevisiae.

M. Ishiwata, H. Kurahashi, and Y. Nakamura (2009)
PNAS 106, 791-796
 |  Abstract »  |  Full Text »  |  PDF »

From the Cover: The yeast Sup35NM domain propagates as a prion in mammalian cells.

C. Krammer, D. Kryndushkin, M. H. Suhre, E. Kremmer, A. Hofmann, A. Pfeifer, T. Scheibel, R. B. Wickner, H. M. Schatzl, and I. Vorberg (2009)
PNAS 106, 462-467
 |  Abstract »  |  Full Text »  |  PDF »

Peptide and Protein Binding in the Axial Channel of Hsp104: INSIGHTS INTO THE MECHANISM OF PROTEIN UNFOLDING.

R. Lum, M. Niggemann, and J. R. Glover (2008)
J. Biol. Chem. 283, 30139-30150
 |  Abstract »  |  Full Text »  |  PDF »

From the Cover: Strain-specific sequences required for yeast [PSI+] prion propagation.

H.-Y. Chang, J.-Y. Lin, H.-C. Lee, H.-L. Wang, and C.-Y. King (2008)
PNAS 105, 13345-13350
 |  Abstract »  |  Full Text »  |  PDF »

Functionally Redundant Isoforms of a Yeast Hsp70 Chaperone Subfamily Have Different Antiprion Effects.

D. Sharma and D. C. Masison (2008)
Genetics 179, 1301-1311
 |  Abstract »  |  Full Text »  |  PDF »

Molecular Chaperones and the Assembly of the Prion Ure2p in Vitro.

J. Savistchenko, J. Krzewska, N. Fay, and R. Melki (2008)
J. Biol. Chem. 283, 15732-15739
 |  Abstract »  |  Full Text »  |  PDF »

Variant-specific [PSI+] Infection Is Transmitted by Sup35 Polymers within [PSI+] Aggregates with Heterogeneous Protein Composition.

S. N. Bagriantsev, E. O. Gracheva, J. E. Richmond, and S. W. Liebman (2008)
Mol. Biol. Cell 19, 2433-2443
 |  Abstract »  |  Full Text »  |  PDF »

Appearance and Propagation of Polyglutamine-based Amyloids in Yeast: TYROSINE RESIDUES ENABLE POLYMER FRAGMENTATION.

I. M. Alexandrov, A. B. Vishnevskaya, M. D. Ter-Avanesyan, and V. V. Kushnirov (2008)
J. Biol. Chem. 283, 15185-15192
 |  Abstract »  |  Full Text »  |  PDF »

Chaperone-dependent amyloid assembly protects cells from prion toxicity.

P. M. Douglas, S. Treusch, H.-Y. Ren, R. Halfmann, M. L. Duennwald, S. Lindquist, and D. M. Cyr (2008)
PNAS 105, 7206-7211
 |  Abstract »  |  Full Text »  |  PDF »

The 2008 Genetics Society of America Medal.

N. Hopkins (2008)
Genetics 178, 1125-1128
 |  Full Text »  |  PDF »

Unraveling prion strains with cell biology and organic chemistry.

A. Aguzzi (2008)
PNAS 105, 11-12
 |  Full Text »  |  PDF »

Role of Hsp104 in the Propagation and Inheritance of the [Het-s] Prion.

L. Malato, S. Dos Reis, L. Benkemoun, R. Sabate, and S. J. Saupe (2007)
Mol. Biol. Cell 18, 4803-4812
 |  Abstract »  |  Full Text »  |  PDF »

Probing the Role of PrP Repeats in Conformational Conversion and Amyloid Assembly of Chimeric Yeast Prions.

J. Dong, J. D. Bloom, V. Goncharov, M. Chattopadhyay, G. L. Millhauser, D. G. Lynn, T. Scheibel, and S. Lindquist (2007)
J. Biol. Chem. 282, 34204-34212
 |  Abstract »  |  Full Text »  |  PDF »

The Role of Sse1 in the de Novo Formation and Variant Determination of the [PSI+] Prion.

Q. Fan, K.-W. Park, Z. Du, K. A. Morano, and L. Li (2007)
Genetics 177, 1583-1593
 |  Abstract »  |  Full Text »  |  PDF »

Prion Protein Repeat Expansion Results in Increased Aggregation and Reveals Phenotypic Variability.

E. M. H. Tank, D. A. Harris, A. A. Desai, and H. L. True (2007)
Mol. Cell. Biol. 27, 5445-5455
 |  Abstract »  |  Full Text »  |  PDF »

Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride.

L. J. Byrne, B. S. Cox, D. J. Cole, M. S. Ridout, B. J. T. Morgan, and M. F. Tuite (2007)
PNAS 104, 11688-11693
 |  Abstract »  |  Full Text »  |  PDF »

Nucleotide Exchange Factors for Hsp70s Are Required for [URE3] Prion Propagation in Saccharomyces cerevisiae.

D. Kryndushkin and R. B. Wickner (2007)
Mol. Biol. Cell 18, 2149-2154
 |  Abstract »  |  Full Text »  |  PDF »

The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans.

M. L. Landsverk, S. Li, A. H. Hutagalung, A. Najafov, T. Hoppe, J. M. Barral, and H. F. Epstein (2007)
J. Cell Biol. 177, 205-210
 |  Abstract »  |  Full Text »  |  PDF »

Effects of Ubiquitin System Alterations on the Formation and Loss of a Yeast Prion.

K. D. Allen, T. A. Chernova, E. P. Tennant, K. D. Wilkinson, and Y. O. Chernoff (2007)
J. Biol. Chem. 282, 3004-3013
 |  Abstract »  |  Full Text »  |  PDF »

Importance of the Hsp70 ATPase Domain in Yeast Prion Propagation.

H. M. Loovers, E. Guinan, and G. W. Jones (2007)
Genetics 175, 621-630
 |  Abstract »  |  Full Text »  |  PDF »

N-Terminal Domain of Yeast Hsp104 Chaperone Is Dispensable for Thermotolerance and Prion Propagation but Necessary for Curing Prions by Hsp104 Overexpression.

G.-C. Hung and D. C. Masison (2006)
Genetics 173, 611-620
 |  Abstract »  |  Full Text »  |  PDF »

De Novo Appearance and "Strain" Formation of Yeast Prion [PSI+] Are Regulated by the Heat-Shock Transcription Factor.

K.-W. Park, J.-S. Hahn, Q. Fan, D. J. Thiele, and L. Li (2006)
Genetics 173, 35-47
 |  Abstract »  |  Full Text »  |  PDF »

The [PSI+] Prion of Saccharomyces cerevisiae Can Be Propagated by an Hsp104 Orthologue from Candida albicans.

J. F. Zenthon, F. Ness, B. Cox, and M. F. Tuite (2006)
Eukaryot. Cell 5, 217-225
 |  Abstract »  |  Full Text »  |  PDF »

Primate Chaperones Hsc70 (Constitutive) and Hsp70 (Induced) Differ Functionally in Supporting Growth and Prion Propagation in Saccharomyces cerevisiae.

Y. Tutar, Y. Song, and D. C. Masison (2006)
Genetics 172, 851-861
 |  Abstract »  |  Full Text »  |  PDF »

Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division.

Y.-X. Wu, L. E. Greene, D. C. Masison, and E. Eisenberg (2005)
PNAS 102, 12789-12794
 |  Abstract »  |  Full Text »  |  PDF »

Strain-specific morphologies of yeast prion amyloid fibrils.

R. Diaz-Avalos, C.-Y. King, J. Wall, M. Simon, and D. L. D. Caspar (2005)
PNAS 102, 10165-10170
 |  Abstract »  |  Full Text »  |  PDF »

Modulation of Prion-dependent Polyglutamine Aggregation and Toxicity by Chaperone Proteins in the Yeast Model.

K. C. Gokhale, G. P. Newnam, M. Y. Sherman, and Y. O. Chernoff (2005)
J. Biol. Chem. 280, 22809-22818
 |  Abstract »  |  Full Text »  |  PDF »

Nonsense Suppression in Yeast Cells Overproducing Sup35 (eRF3) Is Caused by Its Non-heritable Amyloids.

A. B. Salnikova, D. S. Kryndushkin, V. N. Smirnov, V. V. Kushnirov, and M. D. Ter-Avanesyan (2005)
J. Biol. Chem. 280, 8808-8812
 |  Abstract »  |  Full Text »  |  PDF »

Hsp70 Chaperones as Modulators of Prion Life Cycle: Novel Effects of Ssa and Ssb on the Saccharomyces cerevisiae Prion [PSI+].

K. D. Allen, R. D. Wegrzyn, T. A. Chernova, S. Muller, G. P. Newnam, P. A. Winslett, K. B. Wittich, K. D. Wilkinson, and Y. O. Chernoff (2005)
Genetics 169, 1227-1242
 |  Abstract »  |  Full Text »  |  PDF »

Role for Hsp70 Chaperone in Saccharomyces cerevisiae Prion Seed Replication.

Y. Song, Y.-x. Wu, G. Jung, Y. Tutar, E. Eisenberg, L. E. Greene, and D. C. Masison (2005)
Eukaryot. Cell 4, 289-297
 |  Abstract »  |  Full Text »  |  PDF »

Hsp104 Binds to Yeast Sup35 Prion Fiber but Needs Other Factor(s) to Sever It.

Y. Inoue, H. Taguchi, A. Kishimoto, and M. Yoshida (2004)
J. Biol. Chem. 279, 52319-52323
 |  Abstract »  |  Full Text »  |  PDF »

Specificity of Prion Assembly in Vivo: [PSI+] AND [PIN+] FORM SEPARATE STRUCTURES IN YEAST.

S. Bagriantsev and S. W. Liebman (2004)
J. Biol. Chem. 279, 51042-51048
 |  Abstract »  |  Full Text »  |  PDF »

Cytotoxicity of diatom-derived oxylipins in organisms belonging to different phyla.

S. Adolph, S. Bach, M. Blondel, A. Cueff, M. Moreau, G. Pohnert, S. A. Poulet, T. Wichard, and A. Zuccaro (2004)
J. Exp. Biol. 207, 2935-2946
 |  Abstract »  |  Full Text »  |  PDF »

Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro.

I. L. Derkatch, S. M. Uptain, T. F. Outeiro, R. Krishnan, S. L. Lindquist, and S. W. Liebman (2004)
PNAS 101, 12934-12939
 |  Abstract »  |  Full Text »  |  PDF »

Amino Acid Substitutions in the C-terminal AAA+ Module of Hsp104 Prevent Substrate Recognition by Disrupting Oligomerization and Cause High Temperature Inactivation.

J. M. Tkach and J. R. Glover (2004)
J. Biol. Chem. 279, 35692-35701
 |  Abstract »  |  Full Text »  |  PDF »

The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions.

Y. Kimura, S. Koitabashi, A. Kakizuka, and T. Fujita (2004)
Genes Cells 9, 685-696
 |  Abstract »  |  Full Text »  |  PDF »

Hsp104 Catalyzes Formation and Elimination of Self-Replicating Sup35 Prion Conformers.

J. Shorter and S. Lindquist (2004)
Science 304, 1793-1797
 |  Abstract »  |  Full Text »  |  PDF »

Propagation of Saccharomyces cerevisiae [PSI+] Prion Is Impaired by Factors That Regulate Hsp70 Substrate Binding.

G. Jones, Y. Song, S. Chung, and D. C. Masison (2004)
Mol. Cell. Biol. 24, 3928-3937
 |  Abstract »  |  Full Text »  |  PDF »

Dominant Gain-of-Function Mutations in Hsp104p Reveal Crucial Roles for the Middle Region.

E. C. Schirmer, O. R. Homann, A. S. Kowal, and S. Lindquist (2004)
Mol. Biol. Cell 15, 2061-2072
 |  Abstract »  |  Full Text »  |  PDF »

Prions: proteins as genes and infectious entities.

R. B. Wickner, H. K. Edskes, B. T. Roberts, U. Baxa, M. M. Pierce, E. D. Ross, and A. Brachmann (2004)
Genes & Dev. 18, 470-485
 |  Full Text »  |  PDF »

The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104.

V. Grimminger, K. Richter, A. Imhof, J. Buchner, and S. Walter (2004)
J. Biol. Chem. 279, 7378-7383
 |  Abstract »  |  Full Text »  |  PDF »

Prions of Yeast Are Genes Made of Protein: Amyloids and Enzymes.

R.B. WICKNER, H.K. EDSKES, E.D. ROSS, M.M. PIERCE, F. SHEWMAKER, U. BAXA, and A. BRACHMANN (2004)
Cold Spring Harb Symp Quant Biol 69, 489-496
 |  Abstract »  |  PDF »

Pleiotropic Effects of Ubp6 Loss on Drug Sensitivities and Yeast Prion Are Due to Depletion of the Free Ubiquitin Pool.

T. A. Chernova, K. D. Allen, L. M. Wesoloski, J. R. Shanks, Y. O. Chernoff, and K. D. Wilkinson (2003)
J. Biol. Chem. 278, 52102-52115
 |  Abstract »  |  Full Text »  |  PDF »

Yeast [PSI+] Prion Aggregates Are Formed by Small Sup35 Polymers Fragmented by Hsp104.

D. S. Kryndushkin, I. M. Alexandrov, M. D. Ter-Avanesyan, and V. V. Kushnirov (2003)
J. Biol. Chem. 278, 49636-49643
 |  Abstract »  |  Full Text »  |  PDF »

Destabilizing Interactions Among [PSI+] and [PIN+] Yeast Prion Variants.

M. E. Bradley and S. W. Liebman (2003)
Genetics 165, 1675-1685
 |  Abstract »  |  Full Text »  |  PDF »

Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/Hsp104.

S. Narayanan, B. Bosl, S. Walter, and B. Reif (2003)
PNAS 100, 9286-9291
 |  Abstract »  |  Full Text »  |  PDF »

Conservation of the Prion Properties of Ure2p through Evolution.

A. Baudin-Baillieu, E. Fernandez-Bellot, F. Reine, E. Coissac, and C. Cullin (2003)
Mol. Biol. Cell 14, 3449-3458
 |  Abstract »  |  Full Text »  |  PDF »

Specificity of Class II Hsp40 Sis1 in Maintenance of Yeast Prion [RNQ+].

N. Lopez, R. Aron, and E. A. Craig (2003)
Mol. Biol. Cell 14, 1172-1181
 |  Abstract »  |  Full Text »  |  PDF »

Saccharomyces cerevisiae Hsp70 Mutations Affect [PSI+] Prion Propagation and Cell Growth Differently and Implicate Hsp40 and Tetratricopeptide Repeat Cochaperones in Impairment of [PSI+].

G. W. Jones and D. C. Masison (2003)
Genetics 163, 495-506
 |  Abstract »  |  Full Text »  |  PDF »

Guanidine Hydrochloride Inhibits the Generation of Prion "Seeds" but Not Prion Protein Aggregation in Yeast.

F. Ness, P. Ferreira, B. S. Cox, and M. F. Tuite (2002)
Mol. Cell. Biol. 22, 5593-5605
 |  Abstract »  |  Full Text »  |  PDF »

A Heritable Structural Alteration of the Yeast Mitochondrion.

D. Lockshon (2002)
Genetics 161, 1425-1435
 |  Abstract »  |  Full Text »  |  PDF »

Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance.

G. Jung, G. Jones, and D. C. Masison (2002)
PNAS 99, 9936-9941
 |  Abstract »  |  Full Text »  |  PDF »

Increased Expression of Hsp40 Chaperones, Transcriptional Factors, and Ribosomal Protein Rpp0 Can Cure Yeast Prions.

D. S. Kryndushkin, V. N. Smirnov, M. D. Ter-Avanesyan, and V. V. Kushnirov (2002)
J. Biol. Chem. 277, 23702-23708
 |  Abstract »  |  Full Text »  |  PDF »

Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1.

A. B. Meriin, X. Zhang, X. He, G. P. Newnam, Y. O. Chernoff, and M. Y. Sherman (2002)
J. Cell Biol. 157, 997-1004
 |  Abstract »  |  Full Text »  |  PDF »

Antagonistic Interactions between Yeast [PSI+] and [URE3] Prions and Curing of [URE3] by Hsp70 Protein Chaperone Ssa1p but Not by Ssa2p.

C. Schwimmer and D. C. Masison (2002)
Mol. Cell. Biol. 22, 3590-3598
 |  Abstract »  |  Full Text »  |  PDF »

Poly(A)-Binding Protein Acts in Translation Termination via Eukaryotic Release Factor 3 Interaction and Does Not Influence [PSI+] Propagation.

B. Cosson, A. Couturier, S. Chabelskaya, D. Kiktev, S. Inge-Vechtomov, M. Philippe, and G. Zhouravleva (2002)
Mol. Cell. Biol. 22, 3301-3315
 |  Abstract »  |  Full Text »  |  PDF »

The Candida albicans Sup35p protein (CaSup35p): function, prion-like behaviour and an associated polyglutamine length polymorphism.

C. Resende, S. N. Parham, C. Tinsley, P. Ferreira, J. A. B. Duarte, and M. F. Tuite (2002)
Microbiology 148, 1049-1060
 |  Abstract »  |  Full Text »  |  PDF »

Novel Non-Mendelian Determinant Involved in the Control of Translation Accuracy in Saccharomyces cerevisiae.

K. V. Volkov, A. Yu. Aksenova, M. J. Soom, K. V. Osipov, A. V. Svitin, C. Kurischko, I. S. Shkundina, M. D. Ter-Avanesyan, S. G. Inge-Vechtomov, and L. N. Mironova (2002)
Genetics 160, 25-36
 |  Abstract »  |  Full Text »  |  PDF »

Hsp104 Interacts with Hsp90 Cochaperones in Respiring Yeast.

T. Abbas-Terki, O. Donze, P.-A. Briand, and D. Picard (2001)
Mol. Cell. Biol. 21, 7569-7575
 |  Abstract »  |  Full Text »  |  PDF »

Induction of Distinct [URE3] Yeast Prion Strains.

M. Schlumpberger, S. B. Prusiner, and I. Herskowitz (2001)
Mol. Cell. Biol. 21, 7035-7046
 |  Abstract »  |  Full Text »  |  PDF »

Molecular Population Genetics and Evolution of a Prion-like Protein in Saccharomyces cerevisiae.

M. A. Jensen, H. L. True, Y. O. Chernoff, and S. Lindquist (2001)
Genetics 159, 527-535
 |  Abstract »  |  Full Text »  |  PDF »

Mechanism of Prion Loss after Hsp104 Inactivation in Yeast.

R. D. Wegrzyn, K. Bapat, G. P. Newnam, A. D. Zink, and Y. O. Chernoff (2001)
Mol. Cell. Biol. 21, 4656-4669
 |  Abstract »  |  Full Text »  |  PDF »

Prion Filament Networks in [Ure3] Cells of Saccharomyces cerevisiae.

V. V. Speransky, K. L. Taylor, H. K. Edskes, R. B. Wickner, and A. C. Steven (2001)
J. Cell Biol. 153, 1327-1336
 |  Abstract »  |  Full Text »  |  PDF »

Endless possibilities: translation termination and stop codon recognition.

G. Bertram, S. Innes, O. Minella, J. P. Richardson, and I. Stansfield (2001)
Microbiology 147, 255-269
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[URE3] Prion Propagation in Saccharomyces cerevisiae: Requirement for Chaperone Hsp104 and Curing by Overexpressed Chaperone Ydj1p.

H. Moriyama, H. K. Edskes, and R. B. Wickner (2000)
Mol. Cell. Biol. 20, 8916-8922
 |  Abstract »  |  Full Text »  |  PDF »

Yersinia enterocolitica ClpB Affects Levels of Invasin and Motility.

J. L. Badger, B. M. Young, A. J. Darwin, and V. L. Miller (2000)
J. Bacteriol. 182, 5563-5571
 |  Abstract »  |  Full Text »  |  PDF »

Prion-Dependent Switching between Respiratory Competence and Deficiency in the Yeast nam9-1 Mutant.

A. Chacinska, M. Boguta, J. Krzewska, and S. Rospert (2000)
Mol. Cell. Biol. 20, 7220-7229
 |  Abstract »  |  Full Text »  |  PDF »

A Role for Cytosolic Hsp70 in Yeast [PSI+] Prion Propagation and [PSI+] as a Cellular Stress.

G. Jung, G. Jones, R. D. Wegrzyn, and D. C. Masison (2000)
Genetics 156, 559-570
 |  Abstract »  |  Full Text »

Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant.

T. R. Serio, A. G. Cashikar, A. S. Kowal, G. J. Sawicki, J. J. Moslehi, L. Serpell, M. F. Arnsdorf, and S. L. Lindquist (2000)
Science 289, 1317-1321
 |  Abstract »  |  Full Text »

Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity.

N. R. Jana, M. Tanaka, G.-h. Wang, and N. Nukina (2000)
Hum. Mol. Genet. 9, 2009-2018
 |  Abstract »  |  Full Text »  |  PDF »

Evidence for the Prion Hypothesis: Induction of the Yeast [PSI+] Factor by in Vitro- Converted Sup35 Protein.

H. E. Sparrer, A. Santoso, F. C. Szoka Jr., and J. S. Weissman (2000)
Science 289, 595-599
 |  Abstract »  |  Full Text »

The [KIL-d] Element Specifically Regulates Viral Gene Expression in Yeast.

Z. Tallóczy, R. Mazar, D. E. Georgopoulos, F. Ramos, and M. J. Leibowitz (2000)
Genetics 155, 601-609
 |  Abstract »  |  Full Text »

Lysosomotropic Agents and Cysteine Protease Inhibitors Inhibit Scrapie-Associated Prion Protein Accumulation.

K. Doh-ura, T. Iwaki, and B. Caughey (2000)
J. Virol. 74, 4894-4897
 |  Abstract »  |  Full Text »  |  PDF »

Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins.

S. Krobitsch and S. Lindquist (2000)
PNAS 97, 1589-1594
 |  Abstract »  |  Full Text »  |  PDF »

Creating a Protein-Based Element of Inheritance.

L. Li and S. Lindquist (2000)
Science 287, 661-664
 |  Abstract »  |  Full Text »

Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI+] of Saccharomyces cerevisiae.

S. S. Eaglestone, L. W. Ruddock, B. S. Cox, and M. F. Tuite (2000)
PNAS 97, 240-244
 |  Abstract »  |  Full Text »  |  PDF »

Prions in Saccharomyces and Podospora spp.: Protein-Based Inheritance.

R. B. Wickner, K. L. Taylor, H. K. Edskes, M.-L. Maddelein, H. Moriyama, and B. T. Roberts (1999)
Microbiol. Mol. Biol. Rev. 63, 844-861
 |  Abstract »  |  Full Text »  |  PDF »

Evidence for a Protein Mutator in Yeast: Role of the Hsp70-Related Chaperone Ssb in Formation, Stability, and Toxicity of the [PSI] Prion.

Y. O. Chernoff, G. P. Newnam, J. Kumar, K. Allen, and A. D. Zink (1999)
Mol. Cell. Biol. 19, 8103-8112
 |  Abstract »  |  Full Text »  |  PDF »

Mutational Analysis of the [Het-s] Prion Analog of Podospora anserina: A Short N-Terminal Peptide Allows Prion Propagation.

V. Coustou, C. Deleu, S. J. Saupe, and J. Bégueret (1999)
Genetics 153, 1629-1640
 |  Abstract »  |  Full Text »

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.

P. Goloubinoff, A. Mogk, A. P. B. Zvi, T. Tomoyasu, and B. Bukau (1999)
PNAS 96, 13732-13737
 |  Abstract »  |  Full Text »  |  PDF »

The Cytoplasmic Chaperone Hsp104 Is Required for Conformational Repair of Heat-denatured Proteins in the Yeast Endoplasmic Reticulum.

A.-L. Hänninen, M. Simola, N. Saris, and M. Makarow (1999)
Mol. Biol. Cell 10, 3623-3632
 |  Abstract »  |  Full Text »

Genetic Study of Interactions Between the Cytoskeletal Assembly Protein Sla1 and Prion-Forming Domain of the Release Factor Sup35 (eRF3) in Saccharomyces cerevisiae.

P. A. Bailleul, G. P. Newnam, J. N. Steenbergen, and Y. O. Chernoff (1999)
Genetics 153, 81-94
 |  Abstract »  |  Full Text »

Concurrent Chaperone and Protease Activities of ClpAP and the Requirement for the N-terminal ClpA ATP Binding Site for Chaperone Activity.

M. Pak, J. R. Hoskins, S. K. Singh, M. R. Maurizi, and S. Wickner (1999)
J. Biol. Chem. 274, 19316-19322
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Cellular Biology of Prion Diseases.

D. A. Harris (1999)
Clin. Microbiol. Rev. 12, 429-444
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Two Prion-Inducing Regions of Ure2p Are Nonoverlapping.

M.-L. Maddelein and R. B. Wickner (1999)
Mol. Cell. Biol. 19, 4516-4524
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Recognition, Targeting, and Hydrolysis of the lambda  O Replication Protein by the ClpP/ClpX Protease.

M. Gonciarz-Swiatek, A. Wawrzynow, S.-J. Um, B. A. Learn, R. McMacken, W. L. Kelley, C. Georgopoulos, O. Sliekers, and M. Zylicz (1999)
J. Biol. Chem. 274, 13999-14005
 |  Abstract »  |  Full Text »  |  PDF »

Prion Domain Initiation of Amyloid Formation in Vitro from Native Ure2p.

K. L. Taylor, N. Cheng, R. W. Williams, A. C. Steven, and R. B. Wickner (1999)
Science 283, 1339-1343
 |  Abstract »  |  Full Text »

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

H. K. Edskes, V. T. Gray, and R. B. Wickner (1999)
PNAS 96, 1498-1503
 |  Abstract »  |  Full Text »  |  PDF »

Antagonistic Interactions between Yeast Chaperones Hsp104 and Hsp70 in Prion Curing.

G. P. Newnam, R. D. Wegrzyn, S. L. Lindquist, and Y. O. Chernoff (1999)
Mol. Cell. Biol. 19, 1325-1333
 |  Abstract »  |  Full Text »  |  PDF »

The Yeast [PSI+] Prion: Making Sense of Nonsense.

S. W. Liebman and I. L. Derkatch (1999)
J. Biol. Chem. 274, 1181-1184
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Propagation of a Novel Cytoplasmic, Infectious and Deleterious Determinant Is Controlled by Translational Accuracy in Podospora anserina.

P. Silar, V. Haedens, M. Rossignol, and H. Lalucque (1999)
Genetics 151, 87-95
 |  Abstract »  |  Full Text »

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