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]

open access: yes, 2017
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]

open access: yes, 2001
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]

open access: yes, 2016
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

Cigarette smoke toxin hydroquinone and misfolding pancreatic lipase variant cooperatively promote endoplasmic reticulum stress and cell death.

open access: yesPLoS ONE, 2022
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]

open access: yes, 2009
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

Transport of cholesterol from the endoplasmic reticulum to the plasma membrane is constitutive in CaCo-2 cells and differs from the transport of plasma membrane cholesterol to the endoplasmic reticulum

open access: yesJournal of Lipid Research, 1998
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]

open access: yesDigestive Diseases, 2012
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]

open access: yes, 2013
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

Spatiotemporal and quantitative analyses of phosphoinositides – fluorescent probe—and mass spectrometry‐based approaches

open access: yesFEBS Letters, EarlyView.
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?

open access: yesFEBS Letters, EarlyView.
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

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