about
Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulenceCysteine Oxidation Targets Peroxiredoxins 1 and 2 for Exosomal Release through a Novel Mechanism of Redox-Dependent SecretionThioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signalingIdentification of potential protein dithiol-disulfide substrates of mammalian Grx2Functional and morphological changes in endocrine pancreas following cola drink consumption in ratsNeuronal Damage Induced by Perinatal Asphyxia Is Attenuated by Postinjury Glutaredoxin-2 AdministrationLinkage of inflammation and oxidative stress via release of glutathionylated peroxiredoxin-2, which acts as a danger signal.Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3.How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?Identification of a dithiol-disulfide switch in collapsin response mediator protein 2 (CRMP2) that is toggled in a model of neuronal differentiationRedox proteomics of the inflammatory secretome identifies a common set of redoxins and other glutathionylated proteins released in inflammation, influenza virus infection and oxidative stress.Cold Atmospheric Plasma Treatment Induces Anti-Proliferative Effects in Prostate Cancer Cells by Redox and Apoptotic Signaling Pathways.The reducing activity of glutaredoxin 3 toward cytoplasmic substrate proteins is restricted by methionine 43.Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron homeostasis and hemoglobin maturation.Thioredoxins and glutaredoxins as facilitators of protein folding.Glutaredoxin systems.Oxidative Stress and Microcirculatory Flow Abnormalities in the Ventricles during Atrial Fibrillation.Glutaredoxins in thiol/disulfide exchange.Dual role of astrocytes in perinatal asphyxia injury and neuroprotection.Redox regulation of cytoskeletal dynamics during differentiation and de-differentiation.Enzymatic control of cysteinyl thiol switches in proteins.Molecular dynamics simulations and in vitro analysis of the CRMP2 thiol switch.Glutathione, Glutaredoxins, and Iron.The amino terminal subdomain of glycoprotein Gc of Schmallenberg virus: disulfide bonding and structural determinants of neutralization.Thioredoxin 1 and glutaredoxin 2 contribute to maintain the phenotype and integrity of neurons following perinatal asphyxia.Lights on iron-sulfur clusters.Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur clusterRedox regulation by glutathione needs enzymes.Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: effects on structure and activity.Segment-specific overexpression of redoxins after renal ischemia and reperfusion: protective roles of glutaredoxin 2, peroxiredoxin 3, and peroxiredoxin 6.Identification, expression pattern, and characterization of mouse glutaredoxin 2 isoforms.A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase.Shortened isoforms of the androgen receptor are regulated by the cytoprotective heat-shock protein HSPB1 and the tumor-suppressive microRNA miR-1 in prostate cancer cells.Effects of cytotoxic cis- and trans-diammine monochlorido platinum(II) complexes on selenium-dependent redox enzymes and DNA.The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity.New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductaseThe multidomain thioredoxin-monothiol glutaredoxins represent a distinct functional groupRedox atlas of the mouse. Immunohistochemical detection of glutaredoxin-, peroxiredoxin-, and thioredoxin-family proteins in various tissues of the laboratory mouseSpecial issue on selenoprotein expression and functionRedoxins in peripheral neurons after sciatic nerve injury
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description
researcher, ORCID id # 0000-0003-2509-5117
@en
wetenschapper
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name
Christopher Horst Lillig
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Christopher Horst Lillig
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Christopher Horst Lillig
@es
Christopher Horst Lillig
@nl
type
label
Christopher Horst Lillig
@ast
Christopher Horst Lillig
@en
Christopher Horst Lillig
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Christopher Horst Lillig
@nl
prefLabel
Christopher Horst Lillig
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Christopher Horst Lillig
@en
Christopher Horst Lillig
@es
Christopher Horst Lillig
@nl
P214
P106
P1153
55666065700
P21
P214
P31
P496
0000-0003-2509-5117
P735
P7859
viaf-913875