Structure of the cytosolic domain of TOM5, a mitochondrial import protein
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(00)01160-1/fullpdf
Reference15 articles.
1. Tom5 functionally links mitochondrial preprotein receptors to the general import pore
2. Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis
3. Just follow the acid chain
4. N-Terminal Half of a Mitochondrial Presequence Peptide Takes a Helical Conformation When Bound to Dodecylphosphocholine Micelles: A Proton Nuclear Magnetic Resonance Study
5. 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle
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1. Molecular architecture of the active mitochondrial protein gate;Science;2015-09-25
2. Evidence of Evolutionary Constraints That Influences the Sequence Composition and Diversity of Mitochondrial Matrix Targeting Signals;PLoS ONE;2013-06-25
3. Structure, topology and function of the translocase of the outer membrane of mitochondria;Plant Physiology and Biochemistry;2008-03
4. TOM and SAM Machineries in Mitochondrial Protein Import and Outer Membrane Biogenesis;Molecular Machines Involved in Protein Transport across Cellular Membranes;2007
5. Role of Tom5 in Maintaining the Structural Stability of the TOM Complex of Mitochondria;Journal of Biological Chemistry;2005-04
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