The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F 1 F o ‐ ATP synthase-Reference-Cited by-同舟云学术

The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F 1 F o ‐ ATP synthase

Published:2014-06-18 Issue:15 Volume:33 Page:1624-1638
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:EMBO J

Author:

Lytovchenko Oleksandr¹,Naumenko Nataliia¹,Oeljeklaus Silke²³,Schmidt Bernhard¹,Malsburg Karina⁴,Deckers Markus¹,Warscheid Bettina²³,Laan Martin³⁴,Rehling Peter¹⁵

Affiliation:

1. Department of Cellular Biochemistry University Medical Center Göttingen Göttingen Germany

2. Department of Biochemistry and Functional Proteomics Faculty for Biology University of Freiburg Freiburg Germany

3. BIOSS Centre for Biological Signalling Studies University of Freiburg Freiburg Germany

4. Institute for Biochemistry and Molecular Biology ZBMZ University of Freiburg Freiburg Germany

5. Max Planck Institute for Biophysical Chemistry Göttingen Germany

Publisher

EMBO

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Link

https://onlinelibrary.wiley.com/doi/pdf/10.15252/embj.201488076

Reference74 articles.

1. Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase.

2. Methods to Determine the Status of Mitochondrial ATP Synthase Assembly

3. MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization

4. Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits

5. The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane

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