Conserved motifs reveal details of ancestry and structure in the small TIM chaperones of the mitochondrial intermembrane space.

@article{Gentle2007ConservedMR,
  title={Conserved motifs reveal details of ancestry and structure in the small TIM chaperones of the mitochondrial intermembrane space.},
  author={I. Gentle and A. Perry and F. Alcock and V. Likic and P. Dole{\vz}al and Ee Ting Ng and A. Purcell and Malcolm McConnville and Thomas Naderer and Anne-Laure Chanez and Fabien Charrière and Caroline Aschinger and A. Schneider and K. Tokatlidis and T. Lithgow},
  journal={Molecular biology and evolution},
  year={2007},
  volume={24 5},
  pages={
          1149-60
        }
}
The mitochondrial inner and outer membranes are composed of a variety of integral membrane proteins, assembled into the membranes posttranslationally. The small translocase of the inner mitochondrial membranes (TIMs) are a group of approximately 10 kDa proteins that function as chaperones to ferry the imported proteins across the mitochondrial intermembrane space to the outer and inner membranes. In yeast, there are 5 small TIM proteins: Tim8, Tim9, Tim10, Tim12, and Tim13, with equivalent… Expand
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The Structural Basis of the TIM10 Chaperone Assembly*
The Tim8-Tim13 Complex of Neurospora crassa Functions in the Assembly of Proteins into Both Mitochondrial Membranes*
Assembly of Tim9 and Tim10 into a Functional Chaperone*
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