(Q50943720)

25 March 2018

title

Assembly of human mitochondrial ATP synthase through two separate intermediates, F1-c-ring and b-e-g complex. (English)

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author name string

Makoto Fujikawa

1

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Kanako Sugawara

2

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Tsutomu Tanabe

3

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Masasuke Yoshida

4

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25 March 2018

language of work or name

English

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publication date

19 August 2015

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25 March 2018

published in

FEBS Letters

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volume

589

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issue

19 Pt B

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page(s)

2707-2712

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Rotary ATPases--dynamic molecular machines

cites work

1 reference

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A functionally active human F1F0 ATPase can be purified by immunocapture from heart tissue and fibroblast cell lines. Subunit structure and activity studies

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Identification of two proteins associated with mammalian ATP synthase

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Knockdown of DAPIT (diabetes-associated protein in insulin-sensitive tissue) results in loss of ATP synthase in mitochondria

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Population of ATP synthase molecules in mitochondria is limited by available 6.8-kDa proteolipid protein (MLQ).

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High resolution clear native electrophoresis for in-gel functional assays and fluorescence studies of membrane protein complexes.

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria

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Impaired ATP synthase assembly associated with a mutation in the human ATP synthase subunit 6 gene

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The structure of the membrane extrinsic region of bovine ATP synthase

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Assembly and oligomerization of human ATP synthase lacking mitochondrial subunits a and A6L.

21 January 2018

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Modular assembly of yeast mitochondrial ATP synthase

21 January 2018

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Subunit δ is the key player for assembly of the H(+)-translocating unit of Escherichia coli F(O)F1 ATP synthase

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Subcomplexes of human ATP synthase mark mitochondrial biosynthesis disorders

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21 January 2018

Identifiers

DOI

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25 March 2018

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25 March 2018