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Journal of Molecular Biology, ISSN 0022-2836, 08/2010, Volume 401, Issue 2, pp. 182 - 193
Rhomboids are a family of intramembrane serine proteases that are conserved in bacteria, archaea, and eukaryotes. They are required for numerous fundamental... 
rhomboid protease | Mgm1 | substrate recognition | mitochondria | intramembrane proteolysis | Mitochondria | Rhomboid protease | Intramembrane proteolysis | Substrate recognition | SIGNAL | REQUIREMENTS | INNER MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SACCHAROMYCES-CEREVISIAE | YEAST | SUBSTRATE-SPECIFICITY | GENE | PROTEINS | M-AAA PROTEASE | MORPHOLOGY | Species Specificity | Saccharomyces cerevisiae - genetics | Humans | Molecular Sequence Data | Substrate Specificity | Mitochondrial Proteins - genetics | GTP-Binding Proteins - genetics | Metalloproteases - metabolism | Saccharomyces cerevisiae - metabolism | Mitochondrial Proteins - metabolism | Conserved Sequence | Membrane Proteins - metabolism | Recombinant Proteins - metabolism | Serine Proteases - metabolism | Amino Acid Sequence | Mutagenesis, Site-Directed | GTP-Binding Proteins - chemistry | Mutant Proteins - genetics | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Recombinant Proteins - genetics | Binding Sites - genetics | Saccharomyces cerevisiae Proteins - genetics | Sequence Homology, Amino Acid | Models, Biological | Mutant Proteins - chemistry | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Processing, Post-Translational | Serine Endopeptidases - metabolism | GTP-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Proteases | Proteolysis | Amino acids | Mitochondrial DNA | Biosynthesis | Membrane proteins | Promiscuity | Life Sciences | Cellular Biology
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2010, Volume 404, Issue 3, pp. 456 - 477
Journal Article
Journal Article
Journal Article
FEBS Letters, ISSN 0014-5793, 2004, Volume 574, Issue 1, pp. 161 - 166
Journal Article