@article {17510022,
	title = {Structural analyses of a hypothetical minimal metabolism},
	journal = {Philos Trans R Soc Lond B Biol Sci},
	volume = {362},
	number = {1486},
	year = {2007},
	note = {Gabaldon, Toni Pereto, Juli Montero, Francisco Gil, Rosario Latorre, Amparo Moya, Andres Research Support, Non-U.S. Gov{\textquoteright}t England Philosophical transactions of the Royal Society of London. Series B, Biological sciences Philos Trans R Soc Lond B Biol Sci. 2007 Oct 29;362(1486):1751-62.},
	pages = {1751-62},
	abstract = {By integrating data from comparative genomics and large-scale deletion studies, we previously proposed a minimal gene set comprising 206 protein-coding genes. To evaluate the consistency of the metabolism encoded by such a minimal genome, we have carried out a series of computational analyses. Firstly, the topology of the minimal metabolism was compared with that of the reconstructed networks from natural bacterial genomes. Secondly, the robustness of the metabolic network was evaluated by simulated mutagenesis and, finally, the stoichiometric consistency was assessed by automatically deriving the steady-state solutions from the reaction set. The results indicated that the proposed minimal metabolism presents stoichiometric consistency and that it is organized as a complex power-law network with topological parameters falling within the expected range for a natural metabolism of its size. The robustness analyses revealed that most random mutations do not alter the topology of the network significantly, but do cause significant damage by preventing the synthesis of several compounds or compromising the stoichiometric consistency of the metabolism. The implications that these results have on the origins of metabolic complexity and the theoretical design of an artificial minimal cell are discussed.},
	keywords = {*Cell Physiological Phenomena Cells/*metabolism Cluster Analysis *Computer Simulation *Metabolic Networks and Pathways *Models, Biological Models, Statistical},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=17510022},
	author = {Gabald{\'o}n, T. and Peret{\'o}, J. and Montero, F. and Gil, R. and Latorre, A. and Moya, A.}
}
@article {15576054,
	title = {Shaping the mitochondrial proteome},
	journal = {Biochim Biophys Acta},
	volume = {1659},
	number = {2-3},
	year = {2004},
	note = {Gabaldon, Toni Huynen, Martijn A Research Support, Non-U.S. Gov{\textquoteright}t Review Netherlands Biochimica et biophysica acta Biochim Biophys Acta. 2004 Dec 6;1659(2-3):212-20.},
	pages = {212-20},
	abstract = {Mitochondria are eukaryotic organelles that originated from a single bacterial endosymbiosis some 2 billion years ago. The transition from the ancestral endosymbiont to the modern mitochondrion has been accompanied by major changes in its protein content, the so-called proteome. These changes included complete loss of some bacterial pathways, amelioration of others and gain of completely new complexes of eukaryotic origin such as the ATP/ADP translocase and most of the mitochondrial protein import machinery. This renewal of proteins has been so extensive that only 14-16\% of modern mitochondrial proteome has an origin that can be traced back to the bacterial endosymbiont. The rest consists of proteins of diverse origin that were eventually recruited to function in the organelle. This shaping of the proteome content reflects the transformation of mitochondria into a highly specialized organelle that, besides ATP production, comprises a variety of functions within the eukaryotic metabolism. Here we review recent advances in the fields of comparative genomics and proteomics that are throwing light on the origin and evolution of the mitochondrial proteome.},
	keywords = {Animals Biological Transport Energy Metabolism Eukaryotic Cells/physiology *Evolution Humans Mitochondria/*physiology Phylogeny Proteome/*physiology},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=15576054},
	author = {Gabald{\'o}n, T. and M. A. Huynen}
}
