- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
Rheinisch-Westfälische Technische Hochschule Aachen, Dissertation, 2020
- Ereignis
-
Veröffentlichung
- (wo)
-
Aachen
- (wer)
-
Universitätsbibliothek der RWTH Aachen
- (wann)
-
2020
- Urheber
- Beteiligte Personen und Organisationen
-
Gordeliy, Valentin
Dencher, Norbert
Bamberg, Ernst
Engelhard, Martin
- DOI
-
10.18154/RWTH-2021-00849
- URN
-
urn:nbn:de:101:1-2021080406535964218630
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
25.03.2025, 13:41 MEZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Vlasov, Alexey
- Gordeliy, Valentin
- Dencher, Norbert
- Bamberg, Ernst
- Engelhard, Martin
- Universitätsbibliothek der RWTH Aachen
Entstanden
- 2020
Ähnliche Objekte (12)
Biochemical and structural analysis of F-type ATP synthases and its subcomplexes
Biochemical and structural analysis of F-type ATP synthases and its subcomplexes
Computational studies of F-type ATP synthases
The proton conducting F0-part of bacterial ATP synthases
Unusual features of the c-ring of F1FO ATP synthases
Bacterial F-type ATP synthases follow a well-choreographed assembly pathway
Inhibition of F1Fo ATP synthases by bacterial virulence factors and photoswitchable azopolyphenols
The chloroplast ATP synthase upon oxidative stress : critical targets of reactive oxygen species
Complete Ion-Coordination Structure in the Rotor Ring of Na+ -Dependent F-ATP Synthases
Chloroplast Reactions
Structural and biochemical characterization of the chloroplast signal recognition particle
Structural features of chloroplast trigger factor determined at 2.6 Å resolution
Biochemical and structural analysis of F-type ATP synthases and its subcomplexes
Biochemical and structural analysis of F-type ATP synthases and its subcomplexes
Computational studies of F-type ATP synthases
The proton conducting F0-part of bacterial ATP synthases
Unusual features of the c-ring of F1FO ATP synthases
Bacterial F-type ATP synthases follow a well-choreographed assembly pathway
Inhibition of F1Fo ATP synthases by bacterial virulence factors and photoswitchable azopolyphenols
The chloroplast ATP synthase upon oxidative stress : critical targets of reactive oxygen species
Complete Ion-Coordination Structure in the Rotor Ring of Na+ -Dependent F-ATP Synthases
Chloroplast Reactions
Structural and biochemical characterization of the chloroplast signal recognition particle
Structural features of chloroplast trigger factor determined at 2.6 Å resolution
Biochemical and structural analysis of F-type ATP synthases and its subcomplexes
Biochemical and structural analysis of F-type ATP synthases and its subcomplexes
Computational studies of F-type ATP synthases
The proton conducting F0-part of bacterial ATP synthases
Unusual features of the c-ring of F1FO ATP synthases
Bacterial F-type ATP synthases follow a well-choreographed assembly pathway
Inhibition of F1Fo ATP synthases by bacterial virulence factors and photoswitchable azopolyphenols
The chloroplast ATP synthase upon oxidative stress : critical targets of reactive oxygen species
Complete Ion-Coordination Structure in the Rotor Ring of Na+ -Dependent F-ATP Synthases
Chloroplast Reactions
Structural and biochemical characterization of the chloroplast signal recognition particle