Titlebook: Aminopeptidases in Biology and Disease; Nigel M. Hooper,Uwe Lendeckel Book 2004 Springer Science+Business Media New York 2004 biology.neur

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Virtuelle Mobilit?t‘ im ?Raum ohne Grenzen‘tack by other known aminopeptidases. Structurally, the enzyme is a member of the “pita-bread fold” family. It occurs in mammalian tissues in both cytosolic and glycosylphosphatidylinositol-anchored membrane-bound forms generated from two separate genes. The interest in the scientific community for t

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Internationale ?akademische‘ Mobilit?ty sequenced genome of . predicts that there are ～19,000 genes, of which ～ 2% are proteases. The aminopeptidase family of . is relatively large and the use of RNAi and gene deletion mutants has shown that some family members have roles in embryogenesis, the germ line and growth. Expression pattern an

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Hans-Jürgen Bieling,Tobias Haas,Julia LuxThe CD13/aminopeptidase N cell surface peptidase was originally identified as a marker for tumors of the hematopoietic system. Recent evidence however extends the role of CD13/APN to solid tumors as well where it is postulated to regulate angiogenesis and tumor metastasis.

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Methionine Aminopeptidase,ential modification. Indirect evidence suggests that removal of initiator Met by MetAP is important for the normal function of many proteins involved in DNA repair, signal transduction, cell transformation, secretory vesicle trafficking, and viral capsid assembly and infection. Currently, much effor

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Placental Leucine Aminopeptidase,-regulated membrane aminopeptidase (IRAP). P-LAP is translocated from the cytosol to the plasma membrane by oxytocin stimulation in vascular endothelial cells and by vasopressin in renal cells, which is similar to the finding that insulin stimulates IRAP translocation in adipocytes. P-LAP has a wide