Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Erschienen in
-
In: Microbial Cell 5.2018, No. 4, S. 198-207, doi:10.15698/mic2018.04.625
- Ereignis
-
Veröffentlichung
- (wo)
-
Frankfurt am Main
- (wer)
-
Universitätsbibliothek Johann Christian Senckenberg
- (wann)
-
2018
- Urheber
- URN
-
urn:nbn:de:hebis:30:3-525542
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
25.03.2025, 13:46 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
- Rampello, Nadia Giusi
- Stenger, Maria
- Westermann, Benedikt
- Osiewacz, Heinz D.
- Universitätsbibliothek Johann Christian Senckenberg
Entstanden
- 2018
Ähnliche Objekte (12)
Structure of a complete ATP synthase dimer reveals the molecular basis of inner mitochondrial membrane morphology
Variants in mitochondrial ATP synthase cause variable neurologic phenotypes
The mitochondrial Hsp70 controls the assembly of the F1FO-ATP synthase
BNIP3 regulates bioenergetics in cardiomyocytes by interaction with mitochondrial ATP synthase
Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase
Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase
Characterization of a highly diverged mitochondrial ATP synthase Fo subunit in Trypanosoma brucei
Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows
Visualizing mitochondrial FoF1-ATP synthase as the target of the immunomodulatory drug Bz-423
![Kinetische Untersuchungen zum Kopplungsmechanismus an der H+-ATP-Synthase [H-ATP-Synthase] von Chloroplasten](/assets/placeholder/searchResultMediaNoDigitisedMedia.png)
Kinetische Untersuchungen zum Kopplungsmechanismus an der H+-ATP-Synthase [H-ATP-Synthase] von Chloroplasten
Das molekulare Drehlager der ATP-Synthase
Die ATP-Synthase aus Wolinella succinogenes
Structure of a complete ATP synthase dimer reveals the molecular basis of inner mitochondrial membrane morphology
Variants in mitochondrial ATP synthase cause variable neurologic phenotypes
The mitochondrial Hsp70 controls the assembly of the F1FO-ATP synthase
BNIP3 regulates bioenergetics in cardiomyocytes by interaction with mitochondrial ATP synthase
Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase
Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase
Characterization of a highly diverged mitochondrial ATP synthase Fo subunit in Trypanosoma brucei
Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows
Visualizing mitochondrial FoF1-ATP synthase as the target of the immunomodulatory drug Bz-423
Kinetische Untersuchungen zum Kopplungsmechanismus an der H+-ATP-Synthase [H-ATP-Synthase] von Chloroplasten
Das molekulare Drehlager der ATP-Synthase
Die ATP-Synthase aus Wolinella succinogenes
Structure of a complete ATP synthase dimer reveals the molecular basis of inner mitochondrial membrane morphology
Variants in mitochondrial ATP synthase cause variable neurologic phenotypes
The mitochondrial Hsp70 controls the assembly of the F1FO-ATP synthase
BNIP3 regulates bioenergetics in cardiomyocytes by interaction with mitochondrial ATP synthase
Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase
Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase
Characterization of a highly diverged mitochondrial ATP synthase Fo subunit in Trypanosoma brucei
Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows
Visualizing mitochondrial FoF1-ATP synthase as the target of the immunomodulatory drug Bz-423
Kinetische Untersuchungen zum Kopplungsmechanismus an der H+-ATP-Synthase [H-ATP-Synthase] von Chloroplasten
Das molekulare Drehlager der ATP-Synthase