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Published in 2023 at "Biopolymers"
DOI: 10.1002/bip.23532
Abstract: Perturbations in the native structure, often caused by stressing cellular conditions, not only impair protein function but also lead to the formation of aggregates, which can accumulate in the cell leading to harmful effects. Some…
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Keywords:
hsp110;
disaggregation;
hsph1;
sorghum bicolor ... See more keywords
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Published in 2017 at "Human pathology"
DOI: 10.1016/j.humpath.2017.08.001
Abstract: Deletion of the HSP110 T17 mononucleotide repeat has recently been identified as a prognostic marker that is correlated with wild-type HSP110 (HSP110wt) expression in microsatellite instability-high (MSI-H) colorectal cancers. The aim of this study was…
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Keywords:
hsp110 t17;
deletion hsp110;
hsp110;
expression ... See more keywords
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Published in 2017 at "Oncogene"
DOI: 10.1038/onc.2016.403
Abstract: Heat shock protein 110 (HSP110) is induced by different stresses and, through its anti-apoptotic and chaperoning properties, helps cells survive these adverse situations. In colon cancers, HSP110 is abnormally abundant. We have recently shown that…
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Keywords:
colorectal cancer;
colon cancer;
cancer;
growth ... See more keywords
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Published in 2018 at "Journal of Cell Science"
DOI: 10.1242/jcs.210948
Abstract: ABSTRACT During protein quality control, proteotoxic misfolded proteins are recognized by molecular chaperones, ubiquitylated by dedicated quality control ligases and delivered to the 26S proteasome for degradation. Proteins belonging to the Hsp70 chaperone and Hsp110…
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Keywords:
degradation;
hsp70;
26s proteasome;
proteolysis yeast ... See more keywords