Prions in yeast
SW Liebman, YO Chernoff - Genetics, 2012 - academic.oup.com
The concept of a prion as an infectious self-propagating protein isoform was initially
proposed to explain certain mammalian diseases. It is now clear that yeast also has …
proposed to explain certain mammalian diseases. It is now clear that yeast also has …
Yeast prions: structure, biology, and prion-handling systems
RB Wickner, FP Shewmaker, DA Bateman… - Microbiology and …, 2015 - Am Soc Microbiol
SUMMARY A prion is an infectious protein horizontally transmitting a disease or trait without
a required nucleic acid. Yeast and fungal prions are nonchromosomal genes composed of …
a required nucleic acid. Yeast and fungal prions are nonchromosomal genes composed of …
The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system
J Shorter - PloS one, 2011 - journals.plos.org
Bacteria, fungi, protozoa, chromista and plants all harbor homologues of Hsp104, a AAA+
ATPase that collaborates with Hsp70 and Hsp40 to promote protein disaggregation and …
ATPase that collaborates with Hsp70 and Hsp40 to promote protein disaggregation and …
Multiple hsp70 isoforms in the eukaryotic cytosol: mere redundancy or functional specificity?
M Kabani, CN Martineau - Current genomics, 2008 - ingentaconnect.com
Hsp70 molecular chaperones play a variety of functions in every organism, cell type and
organelle, and their activities have been implicated in a number of human pathologies …
organelle, and their activities have been implicated in a number of human pathologies …
Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae
JM Kaimal, G Kandasamy, F Gasser… - Molecular and cellular …, 2017 - Taylor & Francis
Protein aggregation is intimately associated with cellular stress and is accelerated during
aging, disease, and cellular dysfunction. Yeast cells rely on the ATP-consuming chaperone …
aging, disease, and cellular dysfunction. Yeast cells rely on the ATP-consuming chaperone …
Variant-specific [PSI+] Infection Is Transmitted by Sup35 Polymers within [PSI+] Aggregates with Heterogeneous Protein Composition
SN Bagriantsev, EO Gracheva… - Molecular biology of …, 2008 - Am Soc Cell Biol
The [PSI+] prion is the aggregated self-propagating form of the Sup35 protein from the yeast
Saccharomyces cerevisiae. Aggregates of Sup35 in [PSI+] cells exist in different heritable …
Saccharomyces cerevisiae. Aggregates of Sup35 in [PSI+] cells exist in different heritable …
Prions, chaperones, and proteostasis in yeast
TA Chernova, KD Wilkinson… - Cold Spring Harbor …, 2017 - cshperspectives.cshlp.org
Prions are alternatively folded, self-perpetuating protein isoforms involved in a variety of
biological and pathological processes. Yeast prions are protein-based heritable elements …
biological and pathological processes. Yeast prions are protein-based heritable elements …
Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity
The molecular chaperone 70-kDa heat-shock proteins (Hsp70s) play essential roles in
maintaining protein homeostasis. Hsp110, an Hsp70 homolog, is highly efficient in …
maintaining protein homeostasis. Hsp110, an Hsp70 homolog, is highly efficient in …
Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines
M Reidy, R Sharma, S Shastry, BL Roberts… - PLoS …, 2014 - journals.plos.org
Hsp100 family chaperones of microorganisms and plants cooperate with the
Hsp70/Hsp40/NEF system to resolubilize and reactivate stress-denatured proteins. In yeast …
Hsp70/Hsp40/NEF system to resolubilize and reactivate stress-denatured proteins. In yeast …
A first-in-class inhibitor of Hsp110 molecular chaperones of pathogenic fungi
Proteins of the Hsp110 family are molecular chaperones that play important roles in protein
homeostasis in eukaryotes. The pathogenic fungus Candida albicans, which causes …
homeostasis in eukaryotes. The pathogenic fungus Candida albicans, which causes …