The glucose-regulated proteins: stress induction and clinical applications.
By Amy S. Lee. TIBS -Trends in Biochemical Sciences. Regular ed, 2001
1,071 citations recorded by the source corpus.
Subfields: Cell Biology, Epidemiology, Surgery
View Paper: https://www.semanticscholar.org/paper/65d331191f8c005e6e0478bf35b9970e31c4b812
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Citations in the corpus
- Orchestrating the unfolded protein response in health and disease. (2002, background): “Induction of the ER stress response genes, for example BiP and GRP94, in cancerous tissue correlates with malignancy, consistent with their antiapoptotic function (82).”
- ER chaperones in mammalian development and human diseases (2007, background): “GRP78, also known as BiP, is the ER homologue of HSP70 proteins with a conserved ATPase domain and a peptide-binding domain [12,13].”
- In and out of the ER: protein folding, quality control, degradation, and related human diseases. (2007, background): “Cytosolic members of the Hsp families are transcriptionally induced upon temperature stress; ER-resident members are not, but their synthesis is strongly enhanced under conditions of ER overload, glucose deprivation, or upon unbalanced calcium or redox conditions homeostasis (220, 347).”
- The role of the unfolded protein response in tumour development: friend or foe? (2004, neutral): “The UPR is also induced in response to viral infectio”
- GRP78 induction in cancer: therapeutic and prognostic implications. (2007, background): “When the protein load exceeds the folding capacity of the ER, the cells trigger the unfolded protein response (UPR), which activates the PERK, IRE1/X-box binding protein-1 (XBP-1), and activating transcription factor-6 (ATF6) signaling pathways as protective measures, resulting in general translatio”
- Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications. (2006, background): “” The GRPs, multiple members of several molecular mass classes (75, 78–80, and 94–100 kDa), respond to transcriptional upregulation after glucose starvation, disruption of intracellular calcium homeostasis, protein glycosylation interference, and expression of malfolded proteins (361).”