Sentences with phrase «of endoplasmic reticulum»

Within the cell, these calcium ions bind to activator proteins, which help release a flood of calcium ions from storage vesicles of the endoplasmic reticulum (ER) inside the cell.
Electron microscopic evidence showed degeneration of microvilli, disruption of mitochondrial structure, and swelling of the endoplasmic reticulum after exposure of the intestinal loops to the supernatant or deoxycholate.»
The second phase (Phase II) of detoxification occurs in the cytochrome P - 450 enzyme system in the membranes of the endoplasmic reticulum, resulting in conjugation.
The corrected paper is a review in the Journal of Virology — known there as a Gem — which discusses how viruses use the membranes of endoplasmic reticulum (ER) to replicate.
Jokitalo, Eija, et al. «Golgi clusters and vesicles mediate mitotic inheritance independently of the endoplasmic reticulum
Confocal cryomicroscopic analysis and cryodynamics of endoplasmic reticulum in herbaceous plant cells.
Spatial Reorganization of the Endoplasmic Reticulum during Mitosis Relies on Mitotic Kinase Cyclin A in the Early Drosophila Embryo.
Regulation of endoplasmic reticulum - associated degradation by RNF5 - dependent ubiquitination of JNK - associated membrane protein (JAMP).
Junctophilin - 4, a component of the endoplasmic reticulum — plasma membrane junctions, regulates Ca2 + dynamics in T cells.
Revisiting PC1 / 3 mutants: dominant - negative effect of endoplasmic reticulum - retained mutants.
Cisternal organization of the endoplasmic reticulum during mitosis.
Role of endoplasmic reticulum calcium stores in beta - cell ER stress and lipotoxicity.
In fact, genetic and pharmacological targeting of the IRE - 1 / XBP - 1 pathway of the endoplasmic reticulum stress response, which is critical for antibody production, results in decreased numbers and reduced functions of MDSCs.
When the research team used pharmaceuticals to inhibit one function of the endoplasmic reticulum (the building of so - called lipoprotein particles that will export fats out of the cell), the gene activation process was inhibited for many key genes and nuclear ruffling was also altered.
They homed in on the function of the endoplasmic reticulum (ER)-- a «mini-organ» inside cells where proteins and lipids are processed and packaged and undergo quality control before they reach their destinations in the body.
Wolfram syndrome is caused by a mutation in the gene encoding a protein called wolframin, which resides in the membrane of the endoplasmic reticulum — another cellular compartment that functions as a manufacturing and packaging system and also acts as a reservoir for calcium ions.
Scientists at The Institute of Cancer Research, London, identified a molecular trigger responsible for ratcheting up activity of the endoplasmic reticulum (ER)-- the cellular factory that makes the building blocks cancer cells need to keep growing.
Bottom: Human epithelial cells from breast tissue showing the effects of endoplasmic reticulum stress (blue) which fills the entire cell structure.
«We have discovered the key role played by the TOR signalling pathway in driving the expansion of the endoplasmic reticulum, and sending a cell's factories into overdrive.
The researchers also examined BRAF mutant melanoma cell lines, and found that BRAF inhibition induced autophagy by way of an endoplasmic reticulum (ER) stress response.
The UPR is triggered when the normal functions of the endoplasmic reticulum — the cell's largest organelle in charge of making and folding proteins — are compromised.
Fat - induced stress and metabolic overload of the endoplasmic reticulum can alter its function, triggering chronic inflammation, which plays an important role in the development of atherosclerosis.
In the online issue of the journal Nature, the researchers report a new function of FAM134B in the constant renewal of the endoplasmic reticulum (ER), an important cell organelle.

Not exact matches

Using a embroidery thread make french knots along the outer edge of the rough endoplasmic reticulum.
Protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus involves specific uptake into coat protein complex II (COPII)-- coated vesicles of secretory and of vesicle targeting (v - SNARE) proteins.
Regulation of Protein Secretion Through Controlled Aggregation in the Endoplasmic Reticulum
When it reaches the brain, Zika virus infects neuronal stem cells, which will generate fewer neurons, and by inducing chronic stress in the endoplasmic reticulum, it promotes apoptosis, i.e. the early death of these neuronal cells.
They showed that ZIKV infection of cortical progenitors (stem cells for cortical neurons) controlling neurogenesis triggers a stress in the endoplasmic reticulum (where some of the cellular proteins and lipids are synthetized) in the embryonic brain, inducing signals in response to incorrect protein con - formation (referred to as «unfolded protein response»).
Though the UPR usually promotes healthy endoplasmic reticulum function, sustained UPR activation sometimes results in diseases such as atherosclerosis, the deposition of fatty plaques on artery walls, among other conditions.
In the case of cells, one such bad consequence is the accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER), the cell's protein - making factory.
Autophagosomes arise from the endoplasmic reticulum (ER)-- a network of tubular membranes — and actin dynamics is key in their formation and movement.
An oligomer of the Sec61 trimeric complex is thought to form the protein - conducting channel for protein transport across the endoplasmic reticulum.
Moreover, a funnel - shaped pore in the Sec61 oligomer aligned with the exit of a tunnel traversing the large ribosomal subunit, strongly suggesting that both structures function together in the translocation of proteins across the endoplasmic reticulum membrane.
Part of the answer lies in quality control for newly - minted proteins, which takes place in the sub-cellular compartments of the «endoplasmic reticulum», or ER.
The problem with making blood stem cells proliferate outside the body is that the artificial growth gives rise to an accumulation of abnormal proteins in a part of the cell called the endoplasmic reticulum, ER.
An international group of researchers led by Professor Christoph Hess from the Department of Biomedicine at the University of Basel and University Hospital Basel have now found a structure that accounts for the rapid immunologic memory of particular immune cells (CD8 + memory T cells): these important memory cells form multiple connections between mitochondria — the powerhouses of cells — and the endoplasmic reticulum, the site of protein production.
Lead author Dr Chris Bakal, leader of the Dynamical Cell Systems Team at The Institute of Cancer Research, London, said: «The endoplasmic reticulum is the factory of our cells, creating the proteins and lipids needed for our cells to grow and proliferate.
A protein in the TOR signalling pathway, called SREBP, controls the flow of messages to the endoplasmic reticulum telling it to expand — and could allow cancer cells to produce enough proteins and lipids to fuel their non-stop growth.
Domains that contained dilysine endoplasmic reticulum retrieval signals bound the α -, β ′ -, and ϵ - COP subunits of coatomer, whereas other p24 domains bound the β -, γ -, and ζ - COP subunits and required a phenylalanine - containing motif.
The researchers focused on the mitochondria - associated membrane (MAM), which is a contacting site of mitochondria and endoplasmic reticulum (ER).
Transit of a CD8 - p24 chimera from the endoplasmic reticulum through the Golgi complex was slowed when the phenylalanine motif was mutated, suggesting that this motif may function as an anterograde transport signal.
It turns out that neuropathic pain is triggered when the body experiences endoplasmic reticulum (ER) stress, a condition in which the production and transport of protein exceeds the cells» capacities, say researchers from the University of California, Davis.
After detecting a harmful buildup of unfolded proteins, the endoplasmic reticulum sends a signal to the nucleus that activates genes that work to fix the problem.
Starting in the late 1980s, their labs revealed steps in how the endoplasmic reticulum, the cell's factory for processing secreted and membrane proteins, deals with proteins whose linear sequence of amino acids hasn't folded into a proper 3D shape.
The findings reveal a causal chain of events whereby the decreased levels of wolframin protein destabilize the endoplasmic reticulum (causing endoplasmic reticulum stress), thereby reducing calcium release.
Specifically, under stress, caused by uncontrolled ingestion of fats for example, the endoplasmic reticulum — a cell organelle associated with protein synthesis and folding and lipid metabolism — stops its activity in order to re-establish cell equilibrium.
They counted each of the contact points between two cellular organelles — the endoplasmic reticulum (ER) and mitochondria — and demonstrated for the first time that the number of these connections, called MAMs, markedly increase during obesity.
In both yeast and humans, proteins are produced in the endoplasmic reticulum, decorated with a complex of mannose and other sugars, and eventually shipped to the Golgi apparatus for further processing.
Lung fibrosis is thought to also come about when the endoplasmic reticulum (ER) in the cells of the lung becomes stressed and can no longer properly fold and unfold proteins.
In addition, gastrocnemius muscles from IL - 15Rα — KO mice expressed higher levels of mRNA for the sarcoplasmic endoplasmic reticulum calcium ATPase - II (SERCA2) and lower mRNA expression and protein content of the calcium - binding protein calsequestrin (Figure 5, F and G).
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