Results 31 to 40 of about 261,000 (232)
Inhibition of IRE1α-mediated XBP1 mRNA cleavage by XBP1 reveals a novel regulatory process during the unfolded protein response [PDF]
Background: The mammalian endoplasmic reticulum (ER) continuously adapts to the cellular secretory load by the activation of an unfolded protein response (UPR).
Bulleid, Neil J. +4 more
core +2 more sources
Alpha-1 antitrypsin deficiency [PDF]
α-1 antitrypsin is synthesised in the liver and protects lung alveolar tissues from destruction by neutrophil elastase. α-1 antitrypsin deficiency is a common autosomal recessive condition (1:1600 to 1:1800) in which liver disease results from retention ...
Primhak, R.A., Tanner, M.S.
core +2 more sources
Evidence for the involvement of lipid rafts localized at the ER-mitochondria associated membranes in autophagosome formation [PDF]
Mitochondria-associated membranes (MAMs) are subdomains of the endoplasmic reticulum (ER) that interact with mitochondria. This membrane scrambling between ER and mitochondria appears to play a critical role in the earliest steps of autophagy.
Faggioni, Alberto +9 more
core +2 more sources
Mutation-induced protein misfolding of pancreatic secretory enzymes and consequent endoplasmic reticulum stress can cause chronic pancreatitis. A recent study revealed that cigarette smoke also increases the risk of the disease through endoplasmic ...
Norbert Kassay +3 more
doaj +2 more sources
The PIN-FORMED (PIN) protein family of auxin transporters [PDF]
The PIN-FORMED (PIN) proteins are secondary transporters acting in the efflux of the plant signal molecule auxin from cells. They are asymmetrically localized within cells and their polarity determines the directionality of intercellular auxin flow.
Friml, Jiri +6 more
core +3 more sources
The transport of newly synthesized cholesterol from its site of synthesis, the endoplasmic reticulum, to the plasma membrane was studied in CaCo-2 cells. The appearance of newly synthesized cholesterol on the cell surface was rapid. By 30 min, 50% of the
F. Jeffrey Field +3 more
doaj +1 more source
Endoplasmic Reticulum Stress and Inflammation [PDF]
Endoplasmic reticulum (ER) stress due to the presence of misfolded or unfolded proteins in the ER invokes a fundamental biological response, termed the unfolded protein response (UPR). The UPR is orchestrated by three main proximal effectors, of which the IRE1/XBP1 pathway represents the evolutionarily most conserved one.
Adolph TE +3 more
openaire +2 more sources
Obesity Induces Hypothalamic Endoplasmic Reticulum Stress and Impairs Proopiomelanocortin (POMC) Post-translational Processing [PDF]
It was shown previously that abnormal prohormone processing or inactive proconverting enzymes that are responsible for this processing cause profound obesity.
Cakir, Isin +6 more
core +1 more source
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
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

