Titlebook: Intramembrane-Cleaving Proteases (I-CLiPs); Nigel M. Hooper,Uwe Lendeckel Book 2007 Springer Science+Business Media B.V. 2007 Alzheimer‘s.

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Rhomboid Intramembrane Serine Proteases,llular role of rhomboid proteins to broad biological processes, including host-cell invasion by malaria parasites, which is the first implication of these enzymes as possible therapeutic targets in human disease

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uthors recognised as leaders in their fields.Easy to read de.In recent years a growing number of proteases have been identified that catalyse peptide bond hydrolysis in the plane of the cellular membrane. These so-called ‘intramembrane-cleaving proteases’ (I-CLiPs) are involved in a diverse range of

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The Site-2 Protease at Ten,in a membrane-spanning helix. S2P was the first intramembrane-cleaving protease to be recognized but more has been learned about other such proteins. Fundamental questions about the role and function of S2P remain unanswered. S2P plays a crucial role in mammalian lipid metabolism and the unfolded pr

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GXGD-Type Intramembrane Proteases,, which share their respective active site motifs with their classical counterparts, the aspartate protease I-CLiPs acquired a novel characteristic GxGD active site motif during evolution. These so-called GxGD-type proteases include the presenilin (PS), signal peptide peptidase (SPP), SPP-like prote

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Proteases of the Rhomboid Family in the Yeast Saccharomyces Cerevisiae,a wide range of cellular functions and developmental processes by intramembrane proteolysis. In yeast, two members of the rhomboid family are known, Rbd2 and Pcp1. Rbd2 is associated with the Golgi apparatus, but its function and its substrates are still unknown. The rhomboid protease Pcp1, located