About: Christopher Horst Lillig

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

researcher, ORCID id # 0000-0003-2509-5117

Attributes	Values
rdf:type	Item
description	ikertzailea (eu) 연구원 (ko) 研究者 (ja) wetenschapper (nl) дослідник (uk) эрдэмтэн (mn) वैज्ञानिक (hi) изилдөөчү (ky) researcher, ORCID id # 0000-0003-2509-5117 (en)
rdfs:label	Christopher Horst Lillig (en) Christopher Horst Lillig (es) Christopher Horst Lillig (fr) Christopher Horst Lillig (nl) Christopher Horst Lillig (ast)
skos:prefLabel	Christopher Horst Lillig (en) Christopher Horst Lillig (es) Christopher Horst Lillig (fr) Christopher Horst Lillig (nl) Christopher Horst Lillig (ast)
name	Christopher Horst Lillig (en) Christopher Horst Lillig (es) Christopher Horst Lillig (fr) Christopher Horst Lillig (nl) Christopher Horst Lillig (ast)
Scopus author ID	wds:Q58231655-98CC3E95-2790-4AC2-9FC5-F78D632A2D87
Scopus author ID	55666065700
given name	wds:Q58231655-C1710224-E043-4763-83F7-BCB8F2317C7C
given name	Christopher
instance of	wds:Q58231655-62162C43-4CC8-4511-8F6D-D229A3AD5ECB
instance of	Homo sapiens
Loop ID	wds:Q58231655-4DA412BF-257C-4CE0-BCF8-BBE4CCAA0A7E
Loop ID	92598
occupation	wds:Q58231655-FDC11A76-C80B-4596-A6C2-784FB513F2A1
employer	wds:Q58231655-04B5BCFC-319C-4C84-A53E-979D55C73BDB wds:Q58231655-36C000B2-4CDE-4539-94EE-F922DB1D739F
sex or gender	wds:Q58231655-C7D1BF60-2DCF-4C1F-A21A-2F82EFB6E733
VIAF ID	wds:Q58231655-A216A991-CFE0-4CFE-ACE3-27E8CB73DF40
GND ID	wds:q58231655-19adb184-48d4-18f5-cd37-abff2ee1d356
IdRef ID	wds:q58231655-a735ac20-42a1-2d67-ad69-d0a18188cb40
educated at	wds:Q58231655-A2ABA656-6A32-49C6-AAB2-F02EED41584A
family name	wds:q58231655-689b7b6a-4ce0-682e-f99a-47abc679f4d5
WorldCat Identities ID (superseded)	wds:Q58231655-80DCC85B-815E-47FF-97C9-3E2989783BE3
VIAF ID	http://viaf.org/viaf/913875
GND ID	https://d-nb.info/gnd/123165911
IdRef ID	http://www.idref.fr/261025724/id
occupation	researcher
employer	Karolinska Institutet University of Marburg
sex or gender	male
VIAF ID	913875
GND ID	123165911
IdRef ID	261025724
educated at	University of Greifswald
family name	Lillig
WorldCat Identities ID (superseded)	viaf-913875
ORCID iD	wds:Q58231655-96292C74-5EA8-4FD6-BFF1-0599B17A6E25
ORCID iD	https://orcid.org/0000-0003-2509-5117
ORCID iD	0000-0003-2509-5117
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58231655
is author of	Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling Vertebrate-specific glutaredoxin is essential for brain development Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor Glutaredoxin systems. The reducing activity of glutaredoxin 3 toward cytoplasmic substrate proteins is restricted by methionine 43. Cold Atmospheric Plasma Treatment Induces Anti-Proliferative Effects in Prostate Cancer Cells by Redox and Apoptotic Signaling Pathways How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2? Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence Thioredoxin and related molecules--from biology to health and disease Functional and morphological changes in endocrine pancreas following cola drink consumption in rats Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster Glutaredoxins in thiol/disulfide exchange. Redox regulation by glutathione needs enzymes Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase Linkage of inflammation and oxidative stress via release of glutathionylated peroxiredoxin-2, which acts as a danger signal Redox proteomics of the inflammatory secretome identifies a common set of redoxins and other glutathionylated proteins released in inflammation, influenza virus infection and oxidative stress Redox atlas of the mouse. Immunohistochemical detection of glutaredoxin-, peroxiredoxin-, and thioredoxin-family proteins in various tissues of the laboratory mouse Segment-specific overexpression of redoxins after renal ischemia and reperfusion: protective roles of glutaredoxin 2, peroxiredoxin 3, and peroxiredoxin 6. Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: effects on structure and activity. A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase. Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3. Redox regulation of 3'-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins Identification, expression pattern, and characterization of mouse glutaredoxin 2 isoforms. Thioredoxins and glutaredoxins as facilitators of protein folding. Expression pattern of human glutaredoxin 2 isoforms: identification and characterization of two testis/cancer cell-specific isoforms Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron homeostasis and hemoglobin maturation The multidomain thioredoxin-monothiol glutaredoxins represent a distinct functional group Dual role of astrocytes in perinatal asphyxia injury and neuroprotection. The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity. Enzymatic control of cysteinyl thiol switches in proteins Cellular functions of glutathione Cysteine Oxidation Targets Peroxiredoxins 1 and 2 for Exosomal Release through a Novel Mechanism of Redox-Dependent Secretion Iron-sulfur glutaredoxin 2 protects oligodendrocytes against damage induced by nitric oxide release from activated microglia. Glutathione, Glutaredoxins, and Iron. Special issue on selenoprotein expression and function Redox regulation of differentiation and de-differentiation

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