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Frederique Ness et al.
MOLECULAR MICROBIOLOGY (2017)
Amino Acid Proximities in Two Sup35 Prion Strains Revealed by Chemical Cross-linking
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MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS (2015)
The Hsp104 N-Terminal Domain Enables Disaggregase Plasticity and Potentiation
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Distinct Prion Strains Are Defined by Amyloid Core Structure and Chaperone Binding Site Dynamics
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CHEMISTRY & BIOLOGY (2014)
Hsp104 Overexpression Cures Saccharomyces cerevisiae [PSI+] by Causing Dissolution of the Prion Seeds
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Locating folds of the in-register parallel β-sheet of the Sup35p prion domain infectious amyloid
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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2014)
Schizosaccharomyces pombe Disaggregation Machinery Chaperones Support Saccharomyces cerevisiae Growth and Prion Propagation
Michael Reidy et al.
EUKARYOTIC CELL (2013)
Prokaryotic Chaperones Support Yeast Prions and Thermotolerance and Define Disaggregation Machinery Interactions
Michael Reidy et al.
GENETICS (2012)
Insight into Molecular Basis of Curing of [PSI+] Prion by Overexpression of 104-kDa Heat Shock Protein (Hsp104)
Christopher W. Helsen et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2012)
Regulation of Chaperone Effects on a Yeast Prion by Cochaperone Sgt2
Denis A. Kiktev et al.
MOLECULAR AND CELLULAR BIOLOGY (2012)
[PSI+] prion variant establishment in yeast
Jaya Sharma et al.
MOLECULAR MICROBIOLOGY (2012)
Prions are a common mechanism for phenotypic inheritance in wild yeasts
Randal Halfmann et al.
NATURE (2012)
Differences in the Curing of [PSI+] Prion by Various Methods of Hsp104 Inactivation
Yang-Nim Park et al.
PLOS ONE (2012)
Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation
Marika Miot et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2011)
Suicidal [PSI+] is a lethal yeast prion
Ryan P. McGlinchey et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2011)
The M-Domain Controls Hsp104 Protein Remodeling Activity in an Hsp70/Hsp40-Dependent Manner
Bernhard Sielaff et al.
JOURNAL OF MOLECULAR BIOLOGY (2010)
Sti1 Regulation of Hsp70 and Hsp90 Is Critical for Curing of Saccharomyces cerevisiae [PSI+] Prions by Hsp104
Michael Reidy et al.
MOLECULAR AND CELLULAR BIOLOGY (2010)
Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI+] prion but not for prion propagation
Behrooz Moosavi et al.
YEAST (2010)
Ssa1 Overexpression and [PIN+] Variants Cure [PSI+] by Dilution of Aggregates
Vidhu Mathur et al.
JOURNAL OF MOLECULAR BIOLOGY (2009)
The Schizosaccharomyces pombe Hsp104 Disaggregase Is Unable to Propagate the [PSI+] Prion
Patrick Senechal et al.
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Application of GFP-Labeling to Study Prions in Yeast
Lois E. Greene et al.
PROTEIN AND PEPTIDE LETTERS (2009)
Hsp104 and ClpB: protein disaggregating machines
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TRENDS IN BIOCHEMICAL SCIENCES (2009)
The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly
Ryder G. Mackay et al.
BIOCHEMISTRY (2008)
In Vivo Monitoring of the Prion Replication Cycle Reveals a Critical Role for Sis1 in Delivering Substrates to Hsp104
Kimberly A. Tipton et al.
MOLECULAR CELL (2008)
The structural basis of yeast prion strain variants
Brandon H. Toyama et al.
NATURE (2007)
Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance
Prasanna Satpute-Krishnan et al.
PLOS BIOLOGY (2007)
Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities
James Shorter et al.
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The physical basis of how prion conformations determine strain phenotypes
Motomasa Tanaka et al.
NATURE (2006)
N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression
Guo-Chiuan Hung et al.
GENETICS (2006)
Application of photobleaching for measuring diffusion of prion proteins in cytosol of yeast cells
Yue-Xuan Wu et al.
METHODS (2006)
The [PSI+] prion of Saccharomyces cerevisiae can be propagated by an Hsp104 orthologue from Candida albicans
JF Zenthon et al.
EUKARYOTIC CELL (2006)
Prion protein remodelling confers an immediate phenotypic switch
P Satpute-Krishnan et al.
NATURE (2005)
Conformational variations in an infectious protein determine prion strain differences
M Tanaka et al.
NATURE (2004)
Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation
JM Tkach et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
The structure of clpB: A molecular chaperone that rescues proteins from an aggregated state
S Lee et al.
CELL (2003)
Guanidine hydrochloride inhibits the generation of prion seeds but not prion protein aggregation in yeast
F Ness et al.
MOLECULAR AND CELLULAR BIOLOGY (2002)
Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein
AG Cashikar et al.
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The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation
PC Ferreira et al.
MOLECULAR MICROBIOLOGY (2001)
Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI+] of Saccharomyces cerevisiae
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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2000)