Results 91 to 100 of about 989,519 (369)

ROS and Endoplasmic Reticulum Stress in Pulmonary Disease

open access: yesFrontiers in Pharmacology, 2022
Pulmonary diseases are main causes of morbidity and mortality worldwide. Current studies show that though specific pulmonary diseases and correlative lung-metabolic deviance own unique pathophysiology and clinical manifestations, they always tend to ...
Xiangning Cui   +3 more
doaj   +1 more source

Ethanol Induced Disordering of Pancreatic Acinar Cell Endoplasmic Reticulum: An ER Stress/Defective Unfolded Protein Response Model. [PDF]

open access: yes, 2018
Background & aimsHeavy alcohol drinking is associated with pancreatitis, whereas moderate intake lowers the risk. Mice fed ethanol long term show no pancreas damage unless adaptive/protective responses mediating proteostasis are disrupted. Pancreatic
Abrol, Ravinder   +13 more
core   +3 more sources

Thermal proteome profiling and proteome analysis using high‐definition mass spectrometry demonstrate modulation of cholesterol biosynthesis by next‐generation galeterone analog VNPP433‐3β in castration‐resistant prostate cancer

open access: yesMolecular Oncology, EarlyView.
Elevated level of cholesterol is positively correlated to prostate cancer development and disease severity. Cholesterol‐lowering drugs, such as statins, are demonstrated to inhibit prostate cancer. VNPP433‐3β interrupts multiple signaling and metabolic pathways, including cholesterol biosynthesis, AR‐mediated transcription of several oncogenes, mRNA 5′
Retheesh S. Thankan   +10 more
wiley   +1 more source

Unfolded protein response is activated in Lewy body dementias [PDF]

open access: yes, 2018
K
Aarsland, Dag   +8 more
core   +1 more source

Multidimensional OMICs reveal ARID1A orchestrated control of DNA damage, splicing, and cell cycle in normal‐like and malignant urothelial cells

open access: yesMolecular Oncology, EarlyView.
Loss of the frequently mutated chromatin remodeler ARID1A, a subunit of the SWI/SNF cBAF complex, results in less open chromatin, alternative splicing, and the failure to stop cells from progressing through the cell cycle after DNA damage in bladder (cancer) cells. Created in BioRender. Epigenetic regulators, such as the SWI/SNF complex, with important
Rebecca M. Schlösser   +11 more
wiley   +1 more source

The Unfolded Protein Response in Amelogenesis and Enamel Pathologies [PDF]

open access: yes, 2017
During the secretory phase of their life-cycle, ameloblasts are highly specialized secretory cells whose role is to elaborate an extracellular matrix that ultimately confers both form and function to dental enamel, the most highly mineralized of all ...
Barron   +98 more
core   +2 more sources

Escape from TGF‐β‐induced senescence promotes aggressive hallmarks in epithelial hepatocellular carcinoma cells

open access: yesMolecular Oncology, EarlyView.
Chronic TGF‐β exposure drives epithelial HCC cells from a senescent state to a TGF‐β resistant mesenchymal phenotype. This transition is characterized by the loss of Smad3‐mediated signaling, escape from senescence, enhanced invasiveness and metastatic potential, and upregulation of key resistance modulators such as MARK1 and GRM8, ultimately promoting
Minenur Kalyoncu   +11 more
wiley   +1 more source

Evolution of the unfolded protein response

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2013
The unfolded protein response (UPR) is a network of signaling pathways that responds to stress in the endoplasmic reticulum (ER). The general output of the UPR is to upregulate genes involved in ER function, thus restoring and/or increasing the capacity of the ER to fold and process proteins. In parallel, many organisms have mechanisms for limiting the
openaire   +3 more sources

The role of the unfolded protein response in myelination

open access: yesNeural Regeneration Research, 2016
The production, transport and integration of myelin components into the membrane during development is a highly coordinated and regulated process that relies heavily on the endoplasmic reticulum (ER), a sub-cellular organelle that is the principal site of membrane assembly.
FitzGerald, Una   +2 more
openaire   +5 more sources

Druggable sensors of the unfolded protein response [PDF]

open access: yesNature Chemical Biology, 2014
The inability of cells to properly fold, modify and assemble secretory and transmembrane proteins leads to accumulation of misfolded proteins in the endoplasmic reticulum (ER). Under these conditions of 'ER stress', cell survival depends on homeostatic benefits from an intracellular signaling pathway called the unfolded protein response (UPR).
Maly, Dustin J, Papa, Feroz R
openaire   +5 more sources

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