Results 101 to 110 of about 1,004,483 (288)

Silence without stress

open access: yeseLife, 2016
Two mechanisms ensure that the mRNA encoding Hac1 protein, a transcription factor involved in the unfolded protein response, is only translated when it is needed.
David J Young, Nicholas R Guydosh
doaj   +1 more source

Next-generation proteasome inhibitor oprozomib synergizes with modulators of the unfolded protein response to suppress hepatocellular carcinoma [PDF]

open access: yes, 2016
Hepatocellular carcinoma (HCC) responds poorly to conventional systemic therapies. The first-in-class proteasome inhibitor bortezomib has been approved in clinical use for hematologic malignancies and has shown modest activity in solid tumors, including ...
Bogaerts, Eliene   +12 more
core   +2 more sources

Unfolded protein response in hepatitis C virus infection

open access: yesFrontiers in Microbiology, 2014
Hepatitis C virus (HCV) is a single-stranded, positive-sense RNA virus of clinical importance. The virus establishes a chronic infection and can progress from chronic hepatitis, steatosis to fibrosis, cirrhosis and hepatocellular carcinoma.
Shiu-Wan eChan
doaj   +1 more source

Evolution of the unfolded protein response

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2013
The unfolded protein response (UPR) is a network of signaling pathways that responds to stress in the endoplasmic reticulum (ER). The general output of the UPR is to upregulate genes involved in ER function, thus restoring and/or increasing the capacity of the ER to fold and process proteins. In parallel, many organisms have mechanisms for limiting the
openaire   +3 more sources

The role of the unfolded protein response in myelination

open access: yesNeural Regeneration Research, 2016
The production, transport and integration of myelin components into the membrane during development is a highly coordinated and regulated process that relies heavily on the endoplasmic reticulum (ER), a sub-cellular organelle that is the principal site of membrane assembly.
FitzGerald, Una   +2 more
openaire   +5 more sources

Druggable sensors of the unfolded protein response [PDF]

open access: yesNature Chemical Biology, 2014
The inability of cells to properly fold, modify and assemble secretory and transmembrane proteins leads to accumulation of misfolded proteins in the endoplasmic reticulum (ER). Under these conditions of 'ER stress', cell survival depends on homeostatic benefits from an intracellular signaling pathway called the unfolded protein response (UPR).
Maly, Dustin J, Papa, Feroz R
openaire   +5 more sources

The unfolded protein response in hereditary haemochromatosis [PDF]

open access: yesJournal of Cellular and Molecular Medicine, 2007
AbstractTo cope with the accumulation of unfolded or misfolded proteins the endoplasmic reticulum (ER) has evolved specific signalling pathways collectively called the unfolded protein response (UPR). Elucidation of the mechanisms governing ER stress signallinghas linked this response to the regulation of diverse physiologic processes as well as to the
M. de Sousa, S. F. de Almeida
openaire   +3 more sources

Regulation of the unfolded protein response by microRNAs

open access: yesCellular and Molecular Biology Letters, 2013
AbstractThe unfolded protein response (UPR) is an adaptive response to the stress that is caused by an accumulation of misfolded proteins in the lumen of the endoplasmic reticulum (ER). It is an important component of cellular homeostasis. During ER stress, the UPR increases the protein-folding capacity of the endoplasmic reticulum to relieve the ...
Kinga Kochan   +6 more
openaire   +3 more sources

Putting the brakes on the unfolded protein response [PDF]

open access: yesJournal of Cell Biology, 2011
The unfolded protein response is an ancient cellular pathway for rapidly responding to endoplasmic reticulum stress. Two studies in this issue (Rubio et al. 2011. J. Cell. Biol. doi:10.1083/jcb.201007077 and Chawla et al. 2011. J. Cell. Biol. doi:10.1083/jcb.201008071) provide insight into how the unfolded protein response is tamped down to restore ...
Robert H. Silverman, Frank Sicheri
openaire   +3 more sources

Mitochondrial molecular chaperones [PDF]

open access: yes, 1994
After synthesis in the cytosol, most mitochondrial proteins must traverse mitochondrial membranes to reach their functional location. During this process, proteins become unfolded and then refold to attain their native conformation after crossing the ...
Atencio   +32 more
core   +1 more source

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