Results 1 to 10 of about 3,189 (173)

The dithiol mechanism of class I glutaredoxins promotes specificity for glutathione as a reducing agent [PDF]

open access: yesRedox Biology
Class I glutaredoxins reversibly reduce glutathione- and nonglutathione disulfides with the help of reduced glutathione (GSH) using either a monothiol mechanism or a dithiol mechanism.
Lukas Lang   +3 more
doaj   +2 more sources

Making HEDS or tails of glutaredoxin catalysis: Direct reduction of bis(2-hydroxyethyl) disulfide as a non-glutathione disulfide substrate [PDF]

open access: yesRedox Biology
The bis(2-hydroxyethyl) disulfide (HEDS) steady-state assay is the most commonly used assay to measure the activity and kinetic parameters of glutaredoxins.
Lukas Lang   +3 more
doaj   +2 more sources

Oxidative Stress, Glutaredoxins, and Their Therapeutic Potential in Posterior Capsular Opacification [PDF]

open access: yesAntioxidants
Posterior capsular opacification (PCO) is the most common long-term complication of cataract surgery. Traditionally, the pathogenesis of PCO involves the residual lens epithelial cells (LECs), which undergo transdifferentiation into a myofibroblast ...
Chenshuang Li, Weijia Yan, Hong Yan
doaj   +2 more sources

Redox signals and oxidative stress in the control of mitochondrial protein import. [PDF]

open access: yesProtein Sci
Abstract Mitochondrial protein import is essential for organelle biogenesis and cellular homeostasis. It operates in an environment that is intrinsically shaped by redox chemistry. Mitochondria are major sources of reactive oxygen species (ROS), which arise as by‐products of oxidative phosphorylation. Cells therefore maintain sophisticated ROS‐handling
Hasberg L   +3 more
europepmc   +2 more sources

The Monothiol Glutaredoxin Grx4 Influences Iron Homeostasis and Virulence in Ustilago maydis [PDF]

open access: yesJournal of Fungi, 2023
The corn smut fungus, Ustilago maydis, is an excellent model for studying biotrophic plant-pathogen interactions, including nutritional adaptation to the host environment.
Sean W. McCotter   +4 more
doaj   +2 more sources

CEP peptide and cytokinin pathways converge on CEPD glutaredoxins to inhibit root growth [PDF]

open access: yesNature Communications, 2023
C-terminally encoded peptide (CEP) and cytokinin (CK) hormones modulate plant root architecture in response to environmental cues. The results show that CEP and CK pathways utilise CEPD glutaredoxins in separate organs to curb primary root growth.
Michael Taleski   +5 more
doaj   +2 more sources

New insights on thioredoxins (Trxs) and glutaredoxins (Grxs) by in silico amino acid sequence, phylogenetic and comparative structural analyses in organisms of three domains of life

open access: yesHeliyon, 2022
Thioredoxins (Trxs) and Glutaredoxins (Grxs) regulate several cellular processes by controlling the redox state of their target proteins. Trxs and Grxs belong to thioredoxin superfamily and possess characteristic Trx/Grx fold.
Shailendra P Singh, Soumila Mondal
exaly   +3 more sources

Glutaredoxins: roles in iron homeostasis [PDF]

open access: yesTrends in Biochemical Sciences, 2010
Glutaredoxins, proteins traditionally involved in redox reactions, are also required for iron-sulfur cluster assembly and haem biosynthesis. These new roles are probably related to the ability of some glutaredoxins to bind labile [2Fe-2S] clusters and to transfer them rapidly and efficiently to acceptor proteins.
Nicolas Rouhier   +2 more
exaly   +5 more sources

Sketching microprotein portraits. [PDF]

open access: yesProtein Sci
Abstract The illustrations of intricate molecular machineries inside cells created by David Goodsell continue to inspire the scientific community. Here, we aim to extend his artworks to include microproteins, a newly recognized class of small proteins with less than 100 amino acids, encoded by small open reading frames.
Diaz G   +6 more
europepmc   +2 more sources

Redox Modulation Matters: Emerging Functions for Glutaredoxins in Plant Development and Stress Responses

open access: yesPlants, 2014
Glutaredoxins (GRXs) are small ubiquitous glutathione (GSH)-dependent oxidoreductases that catalyze the reversible reduction of protein disulfide bridges or protein-GSH mixed disulfide bonds via a dithiol or monothiol mechanism, respectively. Three major
Shutian Li
exaly   +3 more sources

Home - About - Disclaimer - Privacy