National Repository of Grey Literature 3 records found  Search took 0.01 seconds. 
Rhomboid family intramembrane proteases in prokaryotes: mechanism, substrate repertoires and biological functions in the Gram-positive bacterium Bacillus subtilis.
Began, Jakub
Rhomboid proteases are a class of serine intramembrane proteases, a large family of enzymes that catalyze the proteolytic cleavage of membrane proteins within their transmembrane regions, in the hydrophobic environment of cellular lipid membranes. Rhomboid proteases were discovered in 2001 in Drosophila. In their pioneering study, Lee et al. identified the essential role of Rhomboid-1 protein (Rhom-1), which proteolytically activates the epidermal growth factor (EGF) receptor signaling pathway, in the early stages of fly eye development. Members of the rhomboid superfamily - active proteases (rhomboids) as well as their catalytically-dead counterparts (rhomboid-like proteins, including iRhoms and Derlins) - are widely conserved, implying their biological significance. Rhomboids are present in all kingdoms of life from archea to humans, while proteolytically inactive rhomboid-like proteins are present in eukaryotes only. Rhomboid superfamily proteins play roles in a wide range of processes, as diverse as signaling in metazoan development, mitochondrial biogenesis in yeast, host- cell invasion by protozoan parasites, protein quality control in the endoplasmic reticulum (ER) or bacterial quorum sensing. Rhomboids are the best understood intramembrane proteases from a structural and mechanistic points...
Rhomboid family intramembrane proteases in prokaryotes: mechanism, substrate repertoires and biological functions in the Gram-positive bacterium Bacillus subtilis.
Began, Jakub
Rhomboid proteases are a class of serine intramembrane proteases, a large family of enzymes that catalyze the proteolytic cleavage of membrane proteins within their transmembrane regions, in the hydrophobic environment of cellular lipid membranes. Rhomboid proteases were discovered in 2001 in Drosophila. In their pioneering study, Lee et al. identified the essential role of Rhomboid-1 protein (Rhom-1), which proteolytically activates the epidermal growth factor (EGF) receptor signaling pathway, in the early stages of fly eye development. Members of the rhomboid superfamily - active proteases (rhomboids) as well as their catalytically-dead counterparts (rhomboid-like proteins, including iRhoms and Derlins) - are widely conserved, implying their biological significance. Rhomboids are present in all kingdoms of life from archea to humans, while proteolytically inactive rhomboid-like proteins are present in eukaryotes only. Rhomboid superfamily proteins play roles in a wide range of processes, as diverse as signaling in metazoan development, mitochondrial biogenesis in yeast, host- cell invasion by protozoan parasites, protein quality control in the endoplasmic reticulum (ER) or bacterial quorum sensing. Rhomboids are the best understood intramembrane proteases from a structural and mechanistic points...
Rhomboid family intramembrane proteases in prokaryotes: mechanism, substrate repertoires and biological functions in the Gram-positive bacterium Bacillus subtilis.
Began, Jakub ; Stříšovský, Kvido (advisor) ; Bařinka, Cyril (referee) ; Krásný, Libor (referee)
Rhomboid proteases are a class of serine intramembrane proteases, a large family of enzymes that catalyze the proteolytic cleavage of membrane proteins within their transmembrane regions, in the hydrophobic environment of cellular lipid membranes. Rhomboid proteases were discovered in 2001 in Drosophila. In their pioneering study, Lee et al. identified the essential role of Rhomboid-1 protein (Rhom-1), which proteolytically activates the epidermal growth factor (EGF) receptor signaling pathway, in the early stages of fly eye development. Members of the rhomboid superfamily - active proteases (rhomboids) as well as their catalytically-dead counterparts (rhomboid-like proteins, including iRhoms and Derlins) - are widely conserved, implying their biological significance. Rhomboids are present in all kingdoms of life from archea to humans, while proteolytically inactive rhomboid-like proteins are present in eukaryotes only. Rhomboid superfamily proteins play roles in a wide range of processes, as diverse as signaling in metazoan development, mitochondrial biogenesis in yeast, host- cell invasion by protozoan parasites, protein quality control in the endoplasmic reticulum (ER) or bacterial quorum sensing. Rhomboids are the best understood intramembrane proteases from a structural and mechanistic points...

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