Results 21 to 30 of about 636,928 (251)

Endoplasmic Reticulum Stress in Liver Diseases

open access: yesHepatology, 2022
The endoplasmic reticulum (ER) is an intracellular organelle that fosters the correct folding of linear polypeptides and proteins, a process tightly governed by the ER-resident enzymes and chaperones.
Amir Ajoolabady   +6 more
semanticscholar   +1 more source

Prediction of endoplasmic reticulum resident proteins using fragmented amino acid composition and support vector machine [PDF]

open access: yesPeerJ, 2017
Background The endoplasmic reticulum plays an important role in many cellular processes, which includes protein synthesis, folding and post-translational processing of newly synthesized proteins.
Ravindra Kumar   +2 more
doaj   +2 more sources

c-Abl Phosphorylates MFN2 to Regulate Mitochondrial Morphology in Cells under Endoplasmic Reticulum and Oxidative Stress, Impacting Cell Survival and Neurodegeneration

open access: yesAntioxidants, 2023
The endoplasmic reticulum is a subcellular organelle key in the control of synthesis, folding, and sorting of proteins. Under endoplasmic reticulum stress, an adaptative unfolded protein response is activated; however, if this activation is prolonged ...
Alexis Martinez   +16 more
doaj   +1 more source

Calcium homeostasis and cancer: insights from endoplasmic reticulum-centered organelle communications.

open access: yesTrends in Cell Biology, 2022
Calcium ion (Ca2+) is a ubiquitous and versatile signaling molecule controlling a wide variety of cellular processes, such as proliferation, cell death, migration, and immune response, all fundamental processes essential for the establishment of cancer ...
Shanliang Zheng   +4 more
semanticscholar   +1 more source

Endoplasmic reticulum stress-mediated cell death in liver injury

open access: yesCell Death and Disease, 2022
The endoplasmic reticulum is an important intracellular organelle that plays an important role in maintaining cellular homeostasis. Endoplasmic reticulum stress (ERS) and unfolded protein response (UPR) are induced when the body is exposed to adverse ...
Jian Zhang   +5 more
semanticscholar   +1 more source

Endoplasmic reticulum stress and lipids in health and diseases.

open access: yesProgress in lipid research, 2022
The endoplasmic reticulum (ER) is a complex and dynamic organelle that regulates many cellular pathways, including protein synthesis, protein quality control and lipid synthesis. When one or multiple ER roles are dysregulated and saturated, the ER enters
Cenk Celik   +3 more
semanticscholar   +1 more source

The aftermath of the interplay between the endoplasmic reticulum stress response and redox signaling

open access: yesExperimental and Molecular Medicine, 2021
The endoplasmic reticulum (ER) is an essential organelle of eukaryotic cells. Its main functions include protein synthesis, proper protein folding, protein modification, and the transportation of synthesized proteins.
K. R. Bhattarai   +3 more
semanticscholar   +1 more source

Mitochondrial-Endoplasmic Reticulum Communication-Mediated Oxidative Stress and Autophagy

open access: yesBioMed Research International, 2022
Oxidative stress is an imbalance between free radicals and the antioxidant system causing overgeneration of free radicals (oxygen‐containing molecules) ultimately leading to oxidative damage in terms of lipid peroxidation, protein denaturation, and DNA ...
Xiao-qing Liu   +5 more
semanticscholar   +1 more source

Endoplasmic Reticulum-Associated Protein Degradation.

open access: yesCold Spring Harbor Perspectives in Biology, 2022
Misfolded, potentially toxic proteins in the lumen and membrane of the endoplasmic reticulum (ER) are eliminated by proteasomes in the cytosol through ER-associated degradation (ERAD).
L. Krshnan   +2 more
semanticscholar   +1 more source

Protein Folding in the Endoplasmic Reticulum [PDF]

open access: yesCold Spring Harbor Perspectives in Biology, 2013
In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum (ER), including the role of three types of covalent modifications: signal peptide removal, N-linked glycosylation, and disulfide bond formation, as well as the function and importance of resident ER folding factors.
Braakman, I., Hebert, D.N.
openaire   +3 more sources

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