Results 231 to 240 of about 19,535 (281)

Beyond ROS clearance: Peroxiredoxins in stress signaling and aging.

open access: yesAgeing Research Reviews, 2018
Antioxidants were long predicted to have lifespan-promoting effects, but in general this prediction has not been well supported. While some antioxidants do seem to have a clear effect on longevity, this may not be primarily as a result of their role in ...
G. Detienne   +5 more
semanticscholar   +2 more sources

The biological role of peroxiredoxins in innate immune responses of aquatic invertebrates

Fish and Shellfish Immunology, 2019
Peroxiredoxins (Prxs) are a widespread and greatly transcribed family of antioxidant proteins, which rapidly detoxify peroxynitrite, hydrogen peroxide and organic hydroperoxides.
Muhammad Nadeem Abbas   +2 more
exaly   +2 more sources

Relevance of peroxiredoxins in pathogenic microorganisms

open access: yesApplied Microbiology and Biotechnology, 2021
: The oxidative and nitrosative responses generated by animals and plants are important defenses against infection and establishment of pathogenic microorganisms such as bacteria, fungi, and protozoa.
M. A. de Oliveira   +7 more
semanticscholar   +2 more sources

Peroxiredoxins

Biological Chemistry, 2002
Present knowledge on peroxiredoxins is reviewed with special emphasis on catalytic principles, specificities and biological function. Peroxiredoxins are low efficiency peroxidases using thiols as reductants. They appear to be fairly promiscuous with respect to the hydroperoxide substrate; the specificities for the donor substrate vary considerably ...
Birgit, Hofmann   +2 more
openaire   +2 more sources

Peroxiredoxins in the Lung with Emphasis on Peroxiredoxin VI

2007
All six mammalian peroxiredoxins are expressed in the lung. Peroxiredoxin (Prx) VI is the isoform expressed at the highest level and its lung expression exceeds that for other organs. The predominant location of Prx VI is the cytosol and acidic organelles of Clara cells of the conducting airways and type II epithelial cells and macrophages in the ...
Bruno, Schremmer   +3 more
openaire   +2 more sources

Targeting peroxiredoxins against leukemia

Experimental Cell Research, 2013
Peroxiredoxins (Prx), a family of small non-seleno peroxidases, are important regulators for cellular reactive oxygen species (ROS), which contribute to many signaling pathways and pathogenesis of diseases. Targeting redox homeostasis is being developed as a promising therapeutic strategy for many diseases such as cancers.
Chuan-Xu Liu   +2 more
exaly   +3 more sources

Molecular characterization of novel mitochondrial peroxiredoxins from the Antarctic emerald rockcod and their gene expression in response to environmental warming.

Comparative biochemistry and physiology. Toxicology & pharmacology : CBP, 2019
In the present study we describe the molecular characterization of the two paralogous mitochondrial peroxiredoxins from Trematomus bernacchii, a teleost that plays a pivotal role in the Antarctic food chain.
A. M. Tolomeo   +9 more
semanticscholar   +1 more source

Stress-Induced Peroxiredoxins

2007
Some members of the Prx family are up-regulated in cells under stress conditions. Prx I is the major cytoplasmic Prx and is known as a stress-inducible antioxidant enzyme. Various stress agents or conditions activate Prx I gene expression in vitro and in vivo.
Tetsuro, Ishii, Toru, Yanagawa
openaire   +2 more sources

Structural Survey of the Peroxiredoxins

2007
Peroxiredoxins (Prxs) are ubiquitous proteins that use an active site Cys residue to reduce hydroperoxides. Structural studies since the first Prx structure was determined in 1998 have produced 35 crystal structures of wild type and mutant Prxs with at least one representative structure from each of the five major evolutionary subfamilies of Prxs ...
P Andrew, Karplus, Andrea, Hall
openaire   +2 more sources

The Catalytic Mechanism of Peroxiredoxins

2007
Peroxiredoxins carry out the efficient reduction of a typically broad range of peroxide substrates through an absolutely conserved, activated cysteine residue within a highly conserved active site pocket structure. Though details of reductive recycling after cysteine sulfenic acid formation at the active site vary among members of different Prx classes,
openaire   +2 more sources

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