Structural insight into the TRIAP 1/ PRELI ‐like domain family of mitochondrial phospholipid transfer complexes-Reference-Cited by-同舟云学术

Structural insight into the TRIAP 1/ PRELI ‐like domain family of mitochondrial phospholipid transfer complexes

Published:2015-06-13 Issue:7 Volume:16 Page:824-835
ISSN:1469-221X
Container-title:EMBO reports
language:en
Short-container-title:EMBO Rep

Author:

Miliara Xeni¹,Garnett James A¹²,Tatsuta Takashi³,Abid Ali Ferdos¹,Baldie Heather¹,Pérez‐Dorado Inmaculada¹,Simpson Peter¹,Yague Ernesto⁴,Langer Thomas³,Matthews Stephen¹

Affiliation:

1. Department of Life Sciences Imperial College London London UK

2. School of Biological and Chemical Sciences Joseph Priestley Building Queen Mary University of London London UK

3. Institute for Genetics, Cologne Excellence Cluster on Cellular Stress Responses in Aging‐Associated Diseases (CECAD) Center for Molecular Medicine (CMMC) University of Cologne Cologne Germany

4. Department of Surgery and Cancer Imperial College London Hammersmith Hospital Campus London UK

Publisher

EMBO

Subject

Genetics,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.15252/embr.201540229

Reference42 articles.

1. Mitochondrial protein import: from transport pathways to an integrated network

2. The MIA pathway: A tight bond between protein transport and oxidative folding in mitochondria

3. Novel Mitochondrial Intermembrane Space Proteins as Substrates of the MIA Import Pathway

4. Making heads or tails of phospholipids in mitochondria

5. Ups1p, a conserved intermembrane space protein, regulates mitochondrial shape and alternative topogenesis of Mgm1p

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