Results 21 to 30 of about 62,951 (328)

Electron Transport Chain Is Biochemically Linked to Pilus Assembly Required for Polymicrobial Interactions and Biofilm Formation in the Gram-Positive Actinobacterium Actinomyces oris

open access: yesmBio, 2017
The Gram-positive actinobacteria Actinomyces spp. are key colonizers in the development of oral biofilms due to the inherent ability of Actinomyces to adhere to receptor polysaccharides on the surface of oral streptococci and host cells.
Belkys C. Sanchez   +4 more
doaj   +1 more source

Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space [PDF]

open access: yes, 2017
Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways.
Cardenas-Rodriguez, Mauricio   +1 more
core   +1 more source

ER-Mitochondria contact sites : a new regulator of cellular calcium flux comes into play [PDF]

open access: yes, 2016
Endoplasmic reticulum (ER)-mitochondria membrane contacts are hotspots for calcium signaling. In this issue, Raturi et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201512077) show that the thioredoxin TMX1 inhibits the calcium pump SERCA2b at ...
Anelli   +22 more
core   +2 more sources

Review

open access: yes, 2020
The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium ...
Agh R   +13 more
core   +1 more source

Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases [PDF]

open access: yes, 2014
Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as protein disulfide isomerase and a mechanism to form disulfides de novo.
Appenzeller-Herzog   +22 more
core   +1 more source

Synthèse bibliographique: la divinyl éther synthase de plantes [PDF]

open access: yesBiotechnologie, Agronomie, Société et Environnement, 2001
Divinyl ether synthase in plants: a review. Divinyl ether synthase, an enzyme of the lipoxygenase pathway transforms, in potato tubers, 9-hydroperoxides of fatty acids into colneleic and colnelenic acid, two divinyl ethers of fatty acids.
Fauconnier M.L.   +4 more
doaj  

Protein Engineering for Nicotinamide Coenzyme Specificity in Oxidoreductases: Attempts and Challenges

open access: yesFrontiers in Microbiology, 2018
Oxidoreductases are ubiquitous enzymes that catalyze an extensive range of chemical reactions with great specificity, efficiency, and selectivity. Most oxidoreductases are nicotinamide cofactor-dependent enzymes with a strong preference for NADP or NAD ...
Andrea M. Chánique   +2 more
doaj   +1 more source

How are proteins reduced in the endoplasmic reticulum? [PDF]

open access: yes, 2018
The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for protein folding, degradation, chaperone function, and the ER stress response. Our understanding of this process is generally poor but progress has been made.
Bulleid, Neil   +2 more
core   +2 more sources

Intracellular proteome expression during 4-n-nonylphenol biodegradation by the filamentous fungus Metarhizium robertsii [PDF]

open access: yes, 2014
4-n-nonylphenol (4-n-NP) is an endocrine disrupting compound (EDC); pollutants that cause serious disturbances in the environment. This study shows the degradation pathway and initial proteome analysis in cultures of a fungus that actively degrades 4-n-
Dzitko , Katarzyna   +5 more
core   +1 more source

Electrodes modified with lipid membranes to study quinone oxidoreductases

open access: yes, 2009
Quinone oxidoreductases are a class of membrane enzymes that catalyse the oxidation or reduction of membrane-bound quinols/quinones. The conversion of quinone/quinol by these enzymes is difficult to study because of the hydrophobic nature of the enzymes ...
Jeuken, LJC, Weiss, SA
core   +1 more source

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