Results 211 to 220 of about 636,928 (251)
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Endoplasmic reticulum stress and unfolded protein response in cardiovascular diseases
Nature Reviews Cardiology, 2021Jun Ren +4 more
semanticscholar +1 more source
The ubiquitylation machinery of the endoplasmic reticulum
Nature, 2009As proteins travel through the endoplasmic reticulum (ER), a quality-control system retains newly synthesized polypeptides and supports their maturation. Only properly folded proteins are released to their designated destinations. Proteins that cannot mature are left to accumulate, impairing the function of the ER.
Christian, Hirsch +4 more
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2013
This chapter focuses on the endoplasmic reticulum (ER), which forms part of the endomembrane system of eukaryotic cells. It clarifies that the ER membrane is continuous with the outer nuclear membrane and encloses a space called the lumen which is continuous with the perinuclear space. It also describes ER as a dynamic system, the structure of which is
Qiuyu Wang, Chris Smith, Emma Davis
openaire +1 more source
This chapter focuses on the endoplasmic reticulum (ER), which forms part of the endomembrane system of eukaryotic cells. It clarifies that the ER membrane is continuous with the outer nuclear membrane and encloses a space called the lumen which is continuous with the perinuclear space. It also describes ER as a dynamic system, the structure of which is
Qiuyu Wang, Chris Smith, Emma Davis
openaire +1 more source
ENDOPLASMIC RETICULUM–ASSOCIATED DEGRADATION
Annual Review of Cell and Developmental Biology, 2005Secretory and transmembrane proteins enter the secretory pathway through the protein-conducting Sec61 channel in the membrane of the endoplasmic reticulum. In the endoplasmic reticulum, proteins fold, are frequently covalently modified, and oligomerize before they are packaged into transport vesicles that shuttle them to the Golgi complex.
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Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
Nature, 2000T. Nakagawa +6 more
semanticscholar +1 more source
IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
Nature, 2002M. Calfon +7 more
semanticscholar +1 more source
Endoplasmic reticulum tethering by desmosomes
Nature Cell Biology, 2023Robert M. Harmon, Cara J. Gottardi
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