Sentences with word «cytosol»

Against a background of nematode worms, this graphic depicts the stressed mitochondria (lower right, blue and red) accumulating lipid droplets (red balls) in the interior or cytosol of the cell.

For example, although HCV activation was associated with translocation of FOXO3 from cytosol to the nucleus, alcohol produced transcriptional activation without a prominent change in the nuclear - cytosolic ratio.

LLO lacking the PEST - like sequence accumulated in the host - cell cytosol, suggesting that this sequence targets LLO for degradation.

Mutants lacking the PEST - like sequence entered the host cytosol but subsequently permeabilized and killed the host cell.

Taken together, these findings indicate different redox requirements for the glutathione thiol / disulfide redox couple within cytosol and mitochondria of resting cells and reveal distinct regulation of their redox poise in response to inhibition of glutathione biosynthesis.

They are ubiquitously expressed, mostly cytosolic and found in high molecular mass complexes in brain cytosol.

Cleavage - site analysis suggested that the protease plasmin is more active in preterm milk and that cytosol aminopeptidase and carboxypeptidase B2 also break down milk proteins.

The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon.

In guarding the cell against genetic damage, the p53 machinery functions both in the nucleus of the cell and in the cell's gel - like cytosol.

TB bacteria can evade capture by phagolysomes, getting free in the cell's cytosol where a backup mechanism, autophagy, seeks again to deliver them to lysosomes.

Ectopic expression of dPrx5 in mitochondria but not nucleus or cytosol partially extended longevity under normal or oxidative stress conditions while complete restoration of life span occurred when all three forms of dPrx5 were expressed from the wild type dPrx5 transgene.

A number of bacterial toxins have evolved diverse strategies for crossing membrane barriers in order to reach their substrates in the mammalian cytosol.

They tagged fluorescent molecules to curvature - sensing «BAR» proteins that are present in cytosol, and observed how they behaved.

The researchers were surprised to find that knockdown of one specific mitochondrial chaperone, mtHSP70, elicited a unique stress response mediated by fat accumulation, resulting in improved protein folding in the interior or cytosol of the cell.

«The nanocomplex is also very stable in the cell cytosol, is resistant to endonuclease enzymes that might otherwise break it down, and senses mRNA fast.»

The mitochondria are located in the cytosol of the cells, outside of the cell nucleus; the cell's DNA genome is located inside the nuclear membrane.

Bacteria (colorized in blue) are located either in the cytosol or within a membrane - bound vacuole.

The synthesis of these proteins in the cytosol is tightly coupled totheir import into the mitochondria.

Sofar, studies have focused on how the RQC recognizes and clears blocked ribosomes in the cytosol.

The researchers found that when the cells were stressed, they quickly moved mRNAs from the endoplasmic reticulum to the cytosol.

Greber suspects that the nucleus has antiviral defense reactions, akin to the cytosol, and these defense reactions are variable between cells.

«Using this elegant method, we can reveal that not all the incoming viral DNA enters the cell nucleus as originally expected, but a significant fraction remains in the cytosol, the fluids of the cytoplasm,» explains Greber.

They then separated the cells into two groups — those containing mRNAs associated with ribosomes on the endoplasmic reticulum, and those containing mRNAs associated with free - floating ribosomes in the neighboring fluid - filled space known as the cytosol.

p53 activates a mitochondrial protease called Omi, which is then released into the cytosol of the cell when Ras causes mitochondria to fragment.

Subcellular compartments have unique protein compositions, yet protein synthesis only occurs in the cytosol and in mitochondria and chloroplasts.

On top of that, the microscopic needle can be controlled so precisely that scientists are able either to harvest the content of the nucleus or collect the intracellular fluid surrounding the nucleus, the cytosol.

«We were surprised to find that the cells we examined survived even after we had extracted most of their cytosol,» says ETH professor Vorholt.

In order to visualize this signal, the scientists performed experiments with transgenic Arabidopsis plants which were genetically modified to express a protein in the cytosol, the liquid inside the cells, which breaks down and releases light energy after it has bound calcium ions.

The scientists discovered that the prion domain of Sup35 senses the acidic pH of the cytosol and then drives the formation of protein droplets that protect Sup35 from damage.

ATP is transported through further barrel pores across the mitochondrial outer membrane into the cytosol, which fuels life of human cells.

Unlike in the cytosol, where proteins are generally well - mixed by diffusion, proteins in the envelope can segregate asymmetrically.

For proteins in the cytosol, the liquid inside the cell, these random molecular processes include differences in the break - down of proteins, or random partitioning into the two cells that form during cell division.

Mitochondria, also known as the cells» powerhouses, contain roughly 1,000 protein molecules that are transported from the cytosol.

Their preliminary findings indicate that MUS81 - induced movement of DNA to the cytosol also occurs in human cancer cells, including prostate cancer, breast cancer, colorectal cancer, uterine cancer, leukemia, and melanoma cells.

These results suggest that rel - related transcription factors, which are capable of cytosolic to nuclear translocation, may be held in the cytosol by interaction with related cytoplasmic anchor molecules.

It had been thought that misfolded proteins spontaneously clump together in the cytosol, the fluid component of a cell's interior.

With this in vivo model, the research team uncovered evidence of distinct organellar perturbations in redox balance following inhibition of GSH synthesis with buthionine sulfoximine, demonstrating increased mitochondrial oxidation in response to GSH depletion compared to the cytosol.

Time lapse images collected on a Zeiss Axiovert 200M fluorescence microscope in the core imaging facility of IGB allowed real - time monitoring of the redox state in the cytosol and mitochondria of live cells.

The recent development of genetically - encoded fluorescent biosensors specific to glutathione (GSH), the most abundant cellular redox buffer, has facilitated the IGB research group's discovery of distinct alterations of glutathione redox potentials in the cytosol versus mitochondria within the cell.

The leakage of proteins like cytochrome c and other molecules from the space between the inner and outer membranes of the mitochondria into the cytosol activates caspase proteases and sets in motion a series of reactions that lead to the rapid demise of the cell.

When Ca2 + arises in the cytosol, M13 and calmodulin bind to each other and subsequently TEV - C and TEV - N regain proteolytic functions.

The non-invasive force measurement method based on the fluctuation theorem enabled measurement by analyzing the fluctuating behavior of cargo vesicles in the cytosol subject to thermal noise and so on.

Alcohol - treated HCV / Sod2 + / - mice also showed a greater concentration of FOXO3 in the cytosol of the cell compared to the nuclear location found in other types of mice.

Also, through these studies we solidified the mechanistic understanding for how p53 functions in the cytosol, which complements its pro-apoptotic role in the nucleus.»

Furthermore, the project will analyze the dynamics of these complexes between membrane and cytosol, the dynamics of their assembly and disassembly on endosomal and vacuolar subcompartments, and their connection to trafficking pathways like the AP - 3 pathway.

Elisa Vitiello from the University of Grenoble in France speculated on how the EV superfamily of proteins might be behind vampire out - of - the - cytosol cell biology.

Chs4 is prenylated by Ram1 / Ram2 in the cytosol leading to its association with the membranes of the ER.