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Johannes Schimpf (1986-)

Wissenschaftler

Name	Johannes Schimpf
Zeit	1986- (Lebensdaten)
Ort	Sokuluk (Geburtsort) Deutschland
Geschlecht	männlich
Beruf	Wissenschaftler (charakteristischer Beruf)
Beziehung	Biochemie (Studienfach)
Weitere Angaben	Diss. 2020, Universität Freiburg, Fakultät für Chemie und Pharmazie
Quelle	FreiDok plus
Datensatztyp	Person
GND-Nummer	1200249372
Datensatz-ID	1200249372
Beteiligt an alle anzeigen Exploring ND-011992, a quinazoline-type inhibitor targeting quinone reductases and quinol oxidases Mutations in respiratory complex I promote antibiotic persistence through alterations in intracellular acidity and protein synthesis A quinol anion as catalytic intermediate coupling proton translocation with electron transfer in E. coli respiratory complex I Biochemical consequences of two clinically relevant ND-gene mutations in Escherichia coli respiratory complex I Mass photometry of membrane proteins Quantifying the heterogeneity of macromolecular machines by mass photometry Towards the structure of complex I and bo3 oxidase from Escherichia coli and exploring its aerobic respiratory chain Reduction of the off-pathway iron-sulphur cluster N1a of Escherichia coli respiratory complex I restrains NAD+ dissociation Reduction of the off-pathway iron-sulphur cluster N1a of Escherichia coli respiratory complex I restrains NAD+ dissociation

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Katalog der Deutschen Nationalbibliothek

Johannes Schimpf (1986-)

Exploring ND-011992, a quinazoline-type inhibitor targeting quinone reductases and quinol oxidases

Mutations in respiratory complex I promote antibiotic persistence through alterations in intracellular acidity and protein synthesis

A quinol anion as catalytic intermediate coupling proton translocation with electron transfer in E. coli respiratory complex I

Biochemical consequences of two clinically relevant ND-gene mutations in Escherichia coli respiratory complex I

Mass photometry of membrane proteins

Quantifying the heterogeneity of macromolecular machines by mass photometry

Towards the structure of complex I and bo3 oxidase from Escherichia coli and exploring its aerobic respiratory chain

Reduction of the off-pathway iron-sulphur cluster N1a of Escherichia coli respiratory complex I restrains NAD+ dissociation

Reduction of the off-pathway iron-sulphur cluster N1a of Escherichia coli respiratory complex I restrains NAD+ dissociation