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Dis Model Mech (2016) 9 (8): 823–838.
Published: 01 August 2016
...Marc Brehme; Cindy Voisine ABSTRACT Chaperones and co-chaperones enable protein folding and degradation, safeguarding the proteome against proteotoxic stress. Chaperones display dynamic responses to exogenous and endogenous stressors and thus constitute a key component of the proteostasis network...
Erik Hermansson, Sebastian Schultz, Damian Crowther, Sara Linse, Bengt Winblad, Gunilla Westermark, Jan Johansson, Jenny Presto
Dis Model Mech (2014) 7 (6): 659–665.
Published: 01 June 2014
... chaperone domain are associated with amyloid disease and recent in vitro data show that BRICHOS efficiently delays Aβ42 oligomerization and fibril formation. We have generated transgenic Drosophila melanogaster flies that express the Aβ42 peptide and the BRICHOS domain in the central nervous system (CNS...
Includes: Supplementary data
Dis Model Mech (2014) 7 (3): 319–329.
Published: 01 March 2014
..., and are instead degraded by the ER-associated proteasomal degradation (ERAD) system. Molecular chaperones can assist the folding of the cytosolic domains of these transmembrane proteins; however, these chaperones are also involved in selecting misfolded forms for ERAD. Given this dual role of...
Michelle L. Thompson, Pan Chen, Xiaohui Yan, Hanna Kim, Akeem R. Borom, Nathan B. Roberts, Kim A. Caldwell, Guy A. Caldwell
Dis Model Mech (2014) 7 (2): 233–243.
Published: 01 February 2014
... molecular-chaperone-like activity, both in vitro and in vivo . Although mutations in DYT1 are associated with a rare form of heritable generalized dystonia, the native function of torsinA seems to be cytoprotective in maintaining the cellular threshold to endoplasmic reticulum (ER) stress. Here we explore...