Glutaredoxin 1 promotes intestinal epithelial cell copper toxicity in inflammatory bowel disease [PDF]
Redox BiologyProtein S-glutathionylation (PSSG), a redox-sensitive post-translational modification, regulates protein conformation and activity, potentially resulting in cell death.
Tiantian Zhang +11 more
doaj +2 more sources
Human glutaredoxin-1 can transfer copper to isolated metal binding domains of the P1B-type ATPase, ATP7B. [PDF]
Sci Rep, 2020 Intracellular copper (Cu) in eukaryotic organisms is regulated by homeostatic systems, which rely on the activities of soluble metallochaperones that participate in Cu exchange through highly tuned protein-protein interactions. Recently, the human enzyme
Maghool S +4 more
europepmc +2 more sources
The SP/NK1R System-Mediated ROS Generation in GBM Cells through Inhibiting Glutaredoxin Protein
Neurology Research International, 2021 Altered redox balance is among the main contributing factors developing glioblastoma multiforme (GBM), a highly aggressive grade IV brain tumor. Neuropeptide substance P (SP) plays a key role in modifying the cellular redox environment by activating the ...
Negeen Mehrabani +4 more
doaj +2 more sources
Temporal changes in glutaredoxin 1 and protein s-glutathionylation in allergic airway inflammation. [PDF]
PLoS ONE, 2015 Asthma is a chronic inflammatory disorder of the airways, involving oxidative stress. Upon oxidative stress, glutathione covalently binds to protein thiols to protect them against irreversible oxidation.
Kanako Maki +5 more
doaj +2 more sources
Monothiol and dithiol glutaredoxin-1 from <i>Clostridium oremlandii</i>: identification of domain-swapped structures by NMR, X-ray crystallography and HDX mass spectrometry. [PDF]
IUCrJ, 2020 Structures of monothiol and dithiol glutaredoxin-1 from C. oremlandii are reported. Monothiol glutaredoxin-1 formed domain-swapped structures, one of which was in a hetero-oligomer complex.
Lee K +12 more
europepmc +2 more sources
Deciphering the functional roles of glutaredoxin 1 in chub mackerel (
Comparative Immunology ReportsGlutaredoxins (Grxs) are crucial components of the cellular antioxidant defense system, maintaining redox homeostasis and protecting against oxidative stress.
W.P.S.N. Wijeweera +8 more
doaj +2 more sources
Fish & Shellfish Immunology, 2012 Glutaredoxin (abbreviated as Grx) is an important ubiquitous disulfide reductase, which can protect organisms against oxidative stresses. In the present study, a monothiol glutaredoxin gene (named as VpGrx1) and a dithiol glutaredoxin gene (named as VpGrx2) were identified from Venerupis philippinarum.
Changkao, Mu +4 more
openaire +3 more sources
Making HEDS or tails of glutaredoxin catalysis: Direct reduction of bis(2-hydroxyethyl) disulfide as a non-glutathione disulfide substrate [PDF]
Redox BiologyThe 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
The lineage-specific, intrinsically disordered N-terminal extension of monothiol glutaredoxin 1 from trypanosomes contains a regulatory region [PDF]
Scientific Reports, 2018 Glutaredoxins (Grx) are small proteins conserved throughout all the kingdoms of life that are engaged in a wide variety of biological processes and share a common thioredoxin-fold.
Mattia Sturlese +9 more
doaj +2 more sources
Mechanism of 1-Cys type methionine sulfoxide reductase A regeneration by glutaredoxin
Biochemical and Biophysical Research Communications, 2015 Glutaredoxin (Grx), a major redox regulator, can act as a reductant of methionine sulfoxide reductase A (MsrA). However, the biochemical mechanisms involved in MsrA activity regeneration by Grx remain largely unknown. In this study, we investigated the regeneration mechanism of 1-Cys type Clostridium oremlandii MsrA (cMsrA) lacking a resolving Cys ...
Moon-Jung, Kim +5 more
openaire +3 more sources