The Response to Heat Shock and Oxidative Stress in Saccharomyces cerevisiae

KA Morano, CM Grant, WS Moye-Rowley - Genetics, 2012 - academic.oup.com
A common need for microbial cells is the ability to respond to potentially toxic environmental
insults. Here we review the progress in understanding the response of the yeast …

Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system

J Verghese, J Abrams, Y Wang… - … and molecular biology …, 2012 - Am Soc Microbiol
The eukaryotic heat shock response is an ancient and highly conserved transcriptional
program that results in the immediate synthesis of a battery of cytoprotective genes in the …

Fungal survival under temperature stress: A proteomic perspective

NA Bakar, SA Karsani, SA Alias - PeerJ, 2020 - peerj.com
Background Increases in knowledge of climate change generally, and its impact on
agricultural industries specifically, have led to a greater research effort aimed at improving …

The unfolded protein response is induced by the cell wall integrity mitogen-activated protein kinase signaling cascade and is required for cell wall integrity in …

T Scrimale, L Didone, KL de Mesy Bentley… - Molecular biology of …, 2009 - Am Soc Cell Biol
The yeast cell wall is an extracellular structure that is dependent on secretory and
membrane proteins for its construction. We investigated the role of protein quality control …

Nucleotide exchange factors for Hsp70 molecular chaperones: GrpE, Hsp110/Grp170, HspBP1/Sil1, and BAG domain proteins

A Bracher, J Verghese - The Networking of Chaperones by Co …, 2022 - Springer
Molecular chaperones of the Hsp70 family are key components of the cellular protein-folding
machinery. Substrate folding is accomplished by iterative cycles of ATP binding, hydrolysis …

GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones

A Bracher, J Verghese - The Networking of Chaperones by Co …, 2015 - Springer
Molecular chaperones of the Hsp70 family are key components of the cellular protein folding
machinery. Substrate folding is accomplished by iterative cycles of ATP binding, hydrolysis …

Roles of six Hsp70 genes in virulence, cell wall integrity, antioxidant activity and multiple stress tolerance of Beauveria bassiana

J Wang, J Chen, Y Hu, SH Ying, MG Feng - Fungal Genetics and Biology, 2020 - Elsevier
Functions of most Hsp70-coding genes remain unknown in filamentous fungi. Here, we
show important roles of six Hsp70 homologs (Hsp70a-f) in Beauveria bassiana, a …

Surface Architecture of Histoplasma Capsulatum

AJ Guimarães, MD de Cerqueira… - Frontiers in …, 2011 - frontiersin.org
The dimorphic fungal pathogen Histoplasma capsulatum is the most frequent cause of
clinically significant fungal pneumonia in humans. H. capsulatum virulence is achieved, in …

Substrate binding by the yeast Hsp110 nucleotide exchange factor and molecular chaperone Sse1 is not obligate for its biological activities

VM Garcia, NB Nillegoda, B Bukau… - Molecular biology of the …, 2017 - Am Soc Cell Biol
The highly conserved heat shock protein 70 (Hsp70) is a ubiquitous molecular chaperone
essential for maintaining cellular protein homeostasis. The related protein Hsp110 …

Hsp110 chaperones control client fate determination in the Hsp70–Hsp90 chaperone system

AK Mandal, PA Gibney, NB Nillegoda… - Molecular biology of …, 2010 - Am Soc Cell Biol
Heat shock protein 70 (Hsp70) plays a central role in protein homeostasis and quality
control in conjunction with other chaperone machines, including Hsp90. The Hsp110 …