Results 31 to 40 of about 389,979 (247)

Salmonella Populations inside Host Cells

open access: yesFrontiers in Cellular and Infection Microbiology, 2017
Bacteria of the Salmonella genus cause diseases ranging from gastroenteritis to life-threatening typhoid fever and are among the most successful intracellular pathogens known.
Sónia Castanheira   +1 more
doaj   +1 more source

Dissecting the Role of SAL1 in Metabolizing the Stress Signaling Molecule 3′-Phosphoadenosine 5′-Phosphate in Different Cell Compartments

open access: yesFrontiers in Molecular Biosciences, 2022
Plants possess the most highly compartmentalized eukaryotic cells. To coordinate their intracellular functions, plastids and the mitochondria are dependent on the flow of information to and from the nuclei, known as retrograde and anterograde signals ...
Natallia Ashykhmina   +8 more
doaj   +1 more source

Cytosolic Sensing of Viruses [PDF]

open access: yesImmunity, 2013
Cells are equipped with mechanisms that allow them to rapidly detect and respond to viruses. These defense mechanisms rely partly on receptors that monitor the cytosol for the presence of atypical nucleic acids associated with virus infection. RIG-I-like receptors detect RNA molecules that are absent from the uninfected host.
Goubau, Delphine   +2 more
openaire   +2 more sources

PINK1 import regulation; a fine system to convey mitochondrial stress to the cytosol

open access: yesBMC Biology, 2018
Insights from inherited forms of parkinsonism suggest that insufficient mitophagy may be one etiology of the disease. PINK1/Parkin-dependent mitophagy, which helps maintain a healthy mitochondrial network, is initiated by activation of the PINK1 kinase ...
Shiori Sekine, R. Youle
semanticscholar   +1 more source

The activity of NADH-, NADPH- and Fd-dependent glutamate synthase in the plastids and cytosol of Pisum arvense L. root cells

open access: yesActa Societatis Botanicorum Poloniae, 2014
Three forms of glutamate synthase (NADH-GOGAT, NADPH-GOGAT and Fd-(ferredoxin) GOGAT) were found in the plastids and cytosol of Pisum arvense root cells.
Genowefa Kubik-Dobosz
doaj   +1 more source

Folding-competent and folding-defective forms of Ricin A chain have different fates following retrotranslocation from the endoplasmic reticulum [PDF]

open access: yes, 2010
We report that a toxic polypeptide retaining the potential to refold upon dislocation from the endoplasmic reticulum (ER) to the cytosol (ricin A chain; RTA) and a misfolded version that cannot (termed RTAΔ), follow ER-associated degradation (ERAD ...
Ladds, Graham   +26 more
core   +1 more source

Overexpression of the transcription factor Yap1 modifies intracellular redox conditions and enhances recombinant protein secretion

open access: yesMicrobial Cell, 2014
Oxidative folding of secretory proteins in the endoplasmic reticulum (ER) is a redox active process, which also impacts the redox conditions in the cytosol. As the transcription factor Yap1 is involved in the transcriptional response to oxidative stress,
Marizela Delic   +6 more
doaj   +1 more source

Regulation of Antigen Export to the Cytosol During Cross-Presentation

open access: yesFrontiers in Immunology, 2019
Cross-priming refers to the induction of primary cytotoxic CD8+ T cell responses to antigens that are not expressed in antigen presenting cells (APCs) responsible for T cell priming.
Marine Gros, S. Amigorena
semanticscholar   +1 more source

Heat-Induced Oxidation of the Nuclei and Cytosol

open access: yesFrontiers in Plant Science, 2021
The concept that heat stress (HS) causes a large accumulation of reactive oxygen species (ROS) is widely accepted. However, the intracellular compartmentation of ROS accumulation has been poorly characterized.
Richa Babbar   +4 more
doaj   +1 more source

Properties of triiodothyronine-binding proteins in liver cytosol of rat [PDF]

open access: yes, 1983
The electrophoretic mobility and the sedimentation coefficient were determined in partially purified preparations of both rat liver cytosol and serum triiodothyronine (T3)-binding proteins.
S. Bédard, J. -G. Lehoux, D. Bellabarba
core   +1 more source

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