Results 101 to 110 of about 8,975 (219)

Subdivision of the bacterioferritin comigratory protein family of bacterial peroxiredoxins based on catalytic activity. [PDF]

open access: yes, 2013
© American Chemical Society,2010. Post-print version of article deposited in accordance with SHERPA RoMEO guidelinesPeroxiredoxins are ubiquitous proteins that catalyze the reduction of hydroperoxides, thus conferring resistance to oxidative stress ...
Brown, Alan R   +7 more
core   +1 more source

An unexplored role for Peroxiredoxin in exercise-induced redox signalling?

open access: yesRedox Biology, 2016
Peroxiredoxin (PRDX) is a ubiquitous oxidoreductase protein with a conserved ionised thiol that permits catalysis of hydrogen peroxide (H2O2) up to a million times faster than any thiol-containing signalling protein.
Alex J. Wadley   +2 more
doaj   +1 more source

Role of glutathionylation in infection and inflammation [PDF]

open access: yes, 2019
Glutathionylation, that is, the formation of mixed disulfides between protein cysteines and glutathione (GSH) cysteines, is a reversible post-translational modification catalyzed by dierent cellular oxidoreductases, by which the redox state of the cell
Baldelli, S.   +5 more
core   +1 more source

The physiological concentration of ferrous iron (II) alters the inhibitory effect of hydrogen peroxide on CD45, LAR and PTP1B phosphatases [PDF]

open access: yes, 2015
Hydrogen peroxide is an important regulator of protein tyrosine phosphatase activity via reversible oxidation. However, the role of iron in this reaction has not been yet elucidated. Here we compare the influence of hydrogen peroxide and the ferrous iron
Alicja Kuban-Jankowska   +5 more
core   +1 more source

The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress [PDF]

open access: yes, 2017
Mycothiol (MSH) is the major low molecular weight (LMW) thiol in Actinomycetes and functions in post-translational thiol-modification by protein S-mycothiolation as emerging thiol-protection and redox-regulatory mechanism.
Adrian, Lorenz   +14 more
core   +1 more source

Protein S-glutathionlyation links energy metabolism to redox signaling in mitochondria

open access: yesRedox Biology, 2016
At its core mitochondrial function relies on redox reactions. Electrons stripped from nutrients are used to form NADH and NADPH, electron carriers that are similar in structure but support different functions.
Ryan J. Mailloux, Jason R. Treberg
doaj   +1 more source

Safety evaluation of substituted thiophenes used as flavoring ingredients. [PDF]

open access: yes, 2016
This publication is the second in a series by the Expert Panel of the Flavor and Extract Manufacturers Association summarizing the conclusions of its third systematic re-evaluation of the safety of flavorings previously considered to be generally ...
Bastaki, M   +11 more
core   +1 more source

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