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Antje Beling (1976-)

Ärztin

Name	Antje Beling
Time	1976- (Date of birth and death)
Place	Deutschland
Gender	weiblich
Academic degree	Prof. Dr. med.
Profession	Ärztin (characteristic profession)
Variant	Antje Voigt (früherer Name)
Related	Charité - Universitätsmedizin Berlin. Institut für Biochemie Innere Medizin (Thema) Immunologie (Thema) Ubiquitin (Thema) Enteroviren (Thema) Myokarditis (Thema)
Further information	Berlin, Univ.-Medizin, Habil.-Schr., 2012
Source	Homepage: https://biochemie.charite.de/forschung/kardiale_infektionsbiologie_und_immunologie/team (Stand: 16.06.2020)
Record type	Person
GND-Identifier	129314749
Record ID	129314749
Involved in show all Combination of FOLFOXIRI Drugs with Oncolytic Coxsackie B3 Virus PD-H Synergistically Induces Oncolysis in the Refractory Colorectal Cancer Cell Line Colo320 Elucidation of Molecular Mechanisms of the Pathogenesis of Rare Proteasome associated Mendelian Disorders ISG15 blocks cardiac glycolysis and ensures sufficient mitochondrial energy production during Coxsackievirus B3 infection Mitigated viral myocarditis in A/J mice by the immunoproteasome inhibitor ONX 0914 depends on inhibition of systemic inflammatory responses in CoxsackievirusB3 infection Protein modification with ISG15 blocks coxsackievirus pathology by antiviral and metabolic reprogramming The in vivo ISGylome links ISG15 to metabolic pathways and autophagy upon Listeria monocytogenes infection The immunoproteasome‐specific inhibitor ONX 0914 reverses susceptibility to acute viral myocarditis Cysteine-reactive free ISG15 generates IL-1β–producing CD8α+dendritic cells at the site of infection = Cysteine-reactive free ISG15 generates IL-1[beta]–producing CD8[alpha]+dendritic cells at the site of infection The immunoproteasome controls the availability of the cardioprotective pattern recognition molecule Pentraxin3 Die Bedeutung des Immunoproteasoms in der Pathogenese der murinen Coxsackievirus-B3-Myokarditis Prozessierung des Pp89-MCMV-MHC-Klasse-I-Epitops durch das Proteasom Prozessierung des Pp89-MCMV-MHC-Klasse-I-Epitops durch das Proteasom

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Katalog der Deutschen Nationalbibliothek

Antje Beling (1976-)

Combination of FOLFOXIRI Drugs with Oncolytic Coxsackie B3 Virus PD-H Synergistically Induces Oncolysis in the Refractory Colorectal Cancer Cell Line Colo320

Elucidation of Molecular Mechanisms of the Pathogenesis of Rare Proteasome associated Mendelian Disorders

ISG15 blocks cardiac glycolysis and ensures sufficient mitochondrial energy production during Coxsackievirus B3 infection

Mitigated viral myocarditis in A/J mice by the immunoproteasome inhibitor ONX 0914 depends on inhibition of systemic inflammatory responses in CoxsackievirusB3 infection

Protein modification with ISG15 blocks coxsackievirus pathology by antiviral and metabolic reprogramming

The in vivo ISGylome links ISG15 to metabolic pathways and autophagy upon Listeria monocytogenes infection

The immunoproteasome‐specific inhibitor ONX 0914 reverses susceptibility to acute viral myocarditis

Cysteine-reactive free ISG15 generates IL-1β–producing CD8α+dendritic cells at the site of infection = Cysteine-reactive free ISG15 generates IL-1[beta]–producing CD8[alpha]+dendritic cells at the site of infection

The immunoproteasome controls the availability of the cardioprotective pattern recognition molecule Pentraxin3

Die Bedeutung des Immunoproteasoms in der Pathogenese der murinen Coxsackievirus-B3-Myokarditis

Prozessierung des Pp89-MCMV-MHC-Klasse-I-Epitops durch das Proteasom

Prozessierung des Pp89-MCMV-MHC-Klasse-I-Epitops durch das Proteasom