scholarly journals Endoplasmic reticulum stress-induced apoptosis accompanies enhanced expression of multiple inositol polyphosphate phosphatase 1 (Minpp1): a possible role for Minpp1 in cellular stress response

2016 ◽  
Vol 21 (4) ◽  
pp. 593-608 ◽  
Author(s):  
Surya P. Kilaparty ◽  
Rakhee Agarwal ◽  
Pooja Singh ◽  
Krishnaswamy Kannan ◽  
Nawab Ali
Keyword(s):  
Endoplasmic Reticulum ◽  
Stress Response ◽  
Endoplasmic Reticulum Stress ◽  
Cellular Stress ◽  
Cellular Stress Response ◽  
Inositol Polyphosphate ◽  
Enhanced Expression ◽  
Induced Apoptosis

scholarly journals CSB ablation induced apoptosis is mediated by increased endoplasmic reticulum stress response

PLoS ONE ◽  
2017 ◽  
Vol 12 (3) ◽  
pp. e0172399 ◽  
Author(s):  
Manuela Caputo ◽  
Alessio Balzerano ◽  
Ivan Arisi ◽  
Mara D’Onofrio ◽  
Rossella Brandi ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Stress Response ◽  
Endoplasmic Reticulum Stress ◽  
Endoplasmic Reticulum Stress Response ◽  
Induced Apoptosis

scholarly journals A novel cellular stress response characterised by a rapid reorganisation of membranes of the endoplasmic reticulum

2012 ◽  
Vol 19 (12) ◽  
pp. 1896-1907 ◽  
Author(s):  
S Varadarajan ◽  
E T W Bampton ◽  
J L Smalley ◽  
K Tanaka ◽  
R E Caves ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Stress Response ◽  
Cellular Stress ◽  
Cellular Stress Response

scholarly journals Regulation der Chaperonaktivität im endoplasmatischen Retikulum

BIOspektrum ◽  
2020 ◽  
Vol 26 (6) ◽  
pp. 612-614
Author(s):  
Steffen Preissler
Keyword(s):  
Gene Expression ◽  
Endoplasmic Reticulum ◽  
Stress Response ◽  
Cellular Stress ◽  
Cellular Stress Response ◽  
Protein Homeostasis ◽  
Short Term ◽  
Adaptive Changes ◽  
Unfolded Protein ◽  
Protein Load

Abstract Maintenance of protein homeostasis depends on cellular stress response pathways that mediate adaptive changes in gene expression. In the endoplasmic reticulum additional mechanisms adjust the availability of the abundant Hsp70-type chaperone, BiP, during short-term fluctuations in the unfolded protein load. Here, recent insights into the regulation of BiP by incorporation into inactive oligomers and reversible AMPylation are discussed.

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