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Skeletal muscle is an important organ for development and metabolism and its metabolic disor⁃ ders will induce a series of muscle diseases. As an important regulator of the muscle contraction process, Ca
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Interferon inducible transmembrane proteins (IFITM) were identified by small interference RNA(siRNA) screening method n 1980s. Its antiviral effect and mechanism have become a research hotspot in recent years. Recent studies have shown that IFITM could block the entry of viruses by multiple pathways. It could restrict the endosomal pathway in influenza A viral replication cycle after viral host binding but prior to viral RNA release. In the endosomal pathway, IFITM nhibited the viral RNA release to cytoplasm by decreasing the expression of clathrin, disturbing the acidified function of vacuolar(v)-ATPase, and disrupting intracellular cholesterol homeostasis. Some reports showed that IFITM could restrict the hemifusion between infectious cells and uninfectious cells. Moreover, IFITM could also nduce the memory CD8 + T cells to selectively maintaining the expression of themselves, thus enhancing the survival of cells.
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The exact positioning of the membrane in transmembrane (TM) proteins plays important functional roles. Yet, the structures of TM proteins in protein data bank (pdb) have no information about the explicit position of the membrane. Using a simple hydrophobic lipid-protein mismatch energy function and a flexible lipid/water boundary, the position of lipid bilayer for representative TM proteins in pdb have been annotated. A web server called MAPS (Membrane Annotation of Protein Structures; available at: http://www.boseinst.ernet.in/gautam/maps) has been set up that allows the user to interactively analyze membrane-protein orientations of any uploaded pdb structure with user-defined membrane flexibility parameters.