Hsp90 orchestrates transcriptional regulation by Hsf1 and cell wall remodelling by MAPK signalling during thermal adaptation in a pathogenic yeast. [PDF]
PLoS Pathogens, 2012 Thermal adaptation is essential in all organisms. In yeasts, the heat shock response is commanded by the heat shock transcription factor Hsf1. Here we have integrated unbiased genetic screens with directed molecular dissection to demonstrate that ...
Michelle D Leach +5 more
doaj +2 more sources
Hsp90 as a molecular target [PDF]
Heat shock protein 90 (Hsp90), a highly conserved molecular chaperone, has been proposed to play a vital role in tumorigenesis. Hsp90 has two isoforms, of which Hsp90α is the major isoform of the Hsp90 complex and has an inducible expression profile. The
Munje, Chinmay
core +6 more sources
Heat Shock Protein 90 (Hsp90) Expression and Breast Cancer [PDF]
Pharmaceuticals, 2012 Hsp90 is an abundant protein in mammalian cells. It forms several discrete complexes, each containing distinct groups of co-chaperones that assist protein folding and refolding during stress, protein transport and degradation. It interacts with a variety of proteins that play key roles in breast neoplasia including estrogen receptors, tumor suppressor ...
Zagouri, F. +3 more
openaire +4 more sources
The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer. [PDF]
Mol OncolMutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Abad L, Tosatto SCE, Leonardi E.
europepmc +2 more sources
Expression of heat shock protein (Hsp90) paralogues is regulated by amino acids in skeletal muscle of Atlantic salmon [PDF]
, 2013 Heat shock proteins 90 (Hsp90) have an essential role in sarcomere formation and differentiation in skeletal muscle and also act as molecular chaperones during protein folding impacting a wide range of physiological processes.
Daniel Garcia de la Serrana +7 more
core +1 more source
Heat shock proteins in tendinopathy: novel molecular regulators [PDF]
, 2012 Tendon disorders-tendinopathies-are the primary reason for musculoskeletal consultation in primary care and account for up to 30% of rheumatological consultations.
Neal L. Millar +3 more
core +1 more source
Heat shock protein 90 in neurodegenerative diseases
Molecular Neurodegeneration, 2010 Hsp90 is a molecular chaperone with important roles in regulating pathogenic transformation. In addition to its well-characterized functions in malignancy, recent evidence from several laboratories suggests a role for Hsp90 in maintaining the functional ...
Rodina Anna +4 more
doaj +1 more source
Heat shock induces rapid resorption of primary cilia [PDF]
, 2012 Primary cilia are involved in important developmental and disease pathways, such as the regulation of neurogenesis and tumorigenesis. They function as sensory antennae and are essential in the regulation of key extracellular signalling systems.
Ashworth, R +7 more
core +1 more source
The small-molecule kinase inhibitor D11 counteracts 17-AAG-mediated up-regulation of HSP70 in brain cancer cells. [PDF]
PLoS ONE, 2017 Many types of cancer express high levels of heat shock proteins (HSPs) that are molecular chaperones regulating protein folding and stability ensuring protection of cells from potentially lethal stress.
Susanne Schaefer +2 more
doaj +1 more source
Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70–Hsp40 Substrates
Frontiers in Molecular Biosciences, 2021 In eukaryotes, the 90-kDa heat shock proteins (Hsp90s) are profusely studied chaperones that, together with 70-kDa heat shock proteins (Hsp70s), control protein homeostasis.
Bruno Fauvet +6 more
doaj +1 more source