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MitoProteome: mitochondrial protein sequence database and annotation system. Nucleic Acids Res
, 2004
"... MitoProteome is an object-relational mitochondrial protein sequence database and annotation system. The initial release contains 847 human mitochondrial protein sequences, derived from public sequence databases and mass spectrometric analysis of highly puri®ed human heart mitochondria. Each sequence ..."
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MitoProteome is an object-relational mitochondrial protein sequence database and annotation system. The initial release contains 847 human mitochondrial protein sequences, derived from public sequence databases and mass spectrometric analysis of highly puri®ed human heart mitochondria. Each sequence is manually annotated with primary function, subfunction and subcellular location, and extensively annotated in an automated process with data extracted from external databases, including gene information from LocusLink and Ensembl; disease information from OMIM; protein±protein interaction data from MINT and DIP; functional domain information from Pfam; protein ®ngerprints from PRINTS; protein family and family-speci®c signatures from InterPro; structure data from PDB; mutation data from PMD; BLAST homology data from NCBI NR; and proteins found to be related based on LocusLink and SWISS-PROT references and sequence and taxonomy data. By highly automating the processes of maintaining the MitoProteome Protein List and extracting relevant data from external databases, we are able to present a dynamic database, updated frequently to re¯ect changes in public resources. The MitoProteome database is publicly available at
Commentary Controlling muscle mitochondrial content
, 2003
"... Mitochondrial content, a chief determinant of aerobic capacity, varies widely among muscle types and species. Mitochondrial enzyme levels in vertebrate skeletal muscles vary more than 100-fold, from fish white muscle to bird flight muscles. Recent studies have shed light on the transcriptional regul ..."
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Mitochondrial content, a chief determinant of aerobic capacity, varies widely among muscle types and species. Mitochondrial enzyme levels in vertebrate skeletal muscles vary more than 100-fold, from fish white muscle to bird flight muscles. Recent studies have shed light on the transcriptional regulators that control mitochondrial gene expression in muscle fiber differentiation and development, and in the context of pathological conditions such as neuromuscular disease and obesity. While the transcriptional co-activator PGC-1α (peroxisome proliferator-activated receptor gamma co-activator 1) has Summary emerged as a master controller of mitochondrial gene expression, it is important to consider other mechanisms by which coordinated changes in mitochondrial content could arise. These studies, largely using biomedical models, provide important information for comparative biologists interested in the mechanistic basis of interspecies variation in muscle aerobic capacity. Key words: skeletal muscle, oxidative phosphorylation, energy metabolism, peroxisome proliferator-activated receptor (PPAR), PPAR gamma coactivator 1 (PGC-1).
Evolution of nuclearly encoded mitochondrial genes in Metazoa
"... Abstract All Metazoan nuclear genomes underwent a continuous process of both complete and partial genetic material gain and loss. The forces modulating these events are also subject to the strict interaction between nuclear and mitochondrial (mt) genome. In this context we investigate the evolution ..."
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Abstract All Metazoan nuclear genomes underwent a continuous process of both complete and partial genetic material gain and loss. The forces modulating these events are also subject to the strict interaction between nuclear and mitochondrial (mt) genome. In this context we investigate the evolution of nuclear genes encoding proteins which target the mitochondrion, with a particular attention to genes involved in oxidative phosphorylation (OXPHOS), one of the most ancient and conserved functions. To examine thoroughly the evolutionary strategies that preserve OXPHOS and coordinate the two cellular genomes, a comparative analysis has been carried out for 78 OXPHOS gene families in several Metazoa (insects, tunicates, fishes and mammals). We demonstrate that the duplication rate of OXPHOS genes increases passing from invertebrates to vertebrates consistently with the total increase in genome size, but all species are prone to negatively select OXPHOS duplicates compared to the general trend of nuclear gene families. These results are consistent with the Fbalance hypothesis_ and, at least in insects, the expression of duplicate genes is low and strongly testis-biased. D
unknown title
, 2010
"... MitoGenesisDB: an expression data mining tool to explore spatio-temporal dynamics of mitochondrial biogenesis ..."
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MitoGenesisDB: an expression data mining tool to explore spatio-temporal dynamics of mitochondrial biogenesis
unknown title
, 2008
"... Physical and functional characterization of the genetic locus of IBtk, an inhibitor of Bruton’s tyrosine kinase: evidence for three protein isoforms of IBtk ..."
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Physical and functional characterization of the genetic locus of IBtk, an inhibitor of Bruton’s tyrosine kinase: evidence for three protein isoforms of IBtk
TRANSCRIPTOMIC AND PROTEOMIC STUDIES ON LONGEVITY INDUCED BY OVER-EXPRESSION OF HSP22 IN DROSOPHILA MELANOGASTER
"... Thèse présentée à la Faculté des études supérieures de l’Université Laval dans le cadre du programme de doctorat en Biologie Cellulaire et Moléculaire pour l’obtention du grade de Philosophiae Doctor (Ph. D.) ..."
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Thèse présentée à la Faculté des études supérieures de l’Université Laval dans le cadre du programme de doctorat en Biologie Cellulaire et Moléculaire pour l’obtention du grade de Philosophiae Doctor (Ph. D.)
unknown title
, 2008
"... Physical and functional characterization of the genetic locus of IBtk, an inhibitor of Bruton’s tyrosine kinase: evidence for three protein isoforms of IBtk ..."
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Physical and functional characterization of the genetic locus of IBtk, an inhibitor of Bruton’s tyrosine kinase: evidence for three protein isoforms of IBtk
