Results 51 to 60 of about 356,983 (328)
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho +3 more
wiley +1 more source
Endothelial cells, endoplasmic reticulum stress and oxysterols [PDF]
Oxysterols are bioactive lipids that act as regulators of lipid metabolism, inflammation, cell viability and are involved in several diseases, including atherosclerosis.
Canonico, B. +10 more
core +3 more sources
Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes +3 more
wiley +1 more source
The endoplasmic reticulum mediates essential processes such as protein folding, transport, and post-translational modifications. Disruptions in endoplasmic reticulum function can lead to the accumulation of unfolded or misfolded proteins, initiating ...
Yong Yang +7 more
doaj +1 more source
Doxorubicin (DOX) is a highly potent chemotherapeutic agent, but its usage is limited by dose-dependent cardiotoxicity. DOX-induced cardiotoxicity involves increased oxidative stress and activated endoplasmic reticulum-mediated apoptosis.
Jun-Jie Guo +8 more
doaj +1 more source
Gcn4p and novel upstream activating sequences regulate targets of the unfolded protein response. [PDF]
Eukaryotic cells respond to accumulation of unfolded proteins in the endoplasmic reticulum (ER) by activating the unfolded protein response (UPR), a signal transduction pathway that communicates between the ER and the nucleus.
Li, Hao +2 more
core +4 more sources
Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang +8 more
wiley +1 more source
Cancer microenvironment and endoplasmic reticulum stress response [PDF]
Different stressful conditions such as hypoxia, nutrient deprivation, pH changes, or reduced vascularization, potentially able to act as growth-limiting factors for tumor cells, activate the unfolded protein response (UPR).
Conti, S +5 more
core +4 more sources
Bone metastasis in prostate cancer (PCa) patients is a clinical hurdle due to the poor understanding of the supportive bone microenvironment. Here, we identify stearoyl‐CoA desaturase (SCD) as a tumor‐promoting enzyme and potential therapeutic target in bone metastatic PCa.
Alexis Wilson +7 more
wiley +1 more source
Protein kinase R-like endoplasmic reticulum kinase pathway and diabetic kidney disease
Endoplasmic reticulum stress is closely related to the occurrence and development of diabetic kidney disease.As an important signaling pathway induced by endoplasmic reticulum stress,protein kinase R-like endoplasmic reticulum kinase(PERK)pathway can ...
庞欣欣 +5 more
doaj

