Transmembrane compound

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  • Volume 3 of the book series Biomathematical and Biomechanical Modeling of the Circulatory and Ventilatory Systems aims at presenting major sets of signaling receptors mainly located at the plasma membrane, 1 in a modeling framework rather than biological perspective. Collecting signaling effectors, their main interactions, and major properties are the first tasks required for any modeling of cell signaling processes. The major objective is to comprehend the complexity of natural phenomena to model these events. In other words, to yield the maximal amount of known information (i.e.

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  • Human P-glycoprotein (P-gp), which conveys multidrug resistance, is an ATP-dependent drug efflux pump that transports a wide variety of struc-turally unrelated compounds out of cells. P-gp possesses a ‘linker region’ of75 amino acids that connects two homologous halves, each of which contain a transmembrane domain followed by a nucleotide-binding domain.

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  • The human multidrug resistance-associated protein (MRP1) is an ATP-dependent efflux pump that transports anionic conjugates, and hydrophobic compounds in a glutathione dependent manner. Similar to the other, well-characterized multidrug transporter P-gp, MRP1 comprises two nucleotide-binding domains (NBDs) in addition to transmembrane domains. However, whereas the NBDs of P-gp have been shown to be functionally equivalent, those of MRP1 differ significantly.

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  • Human UDP-glucuronosyltransferase 1A (UGT1A) isoforms are endoplas-mic reticulum (ER)-resident type I membrane proteins responsible for the detoxification of a broad range of toxic phenolic compounds. These pro-teins contain a C-terminal stop transfer sequence with a transmembrane domain (TMD), which anchors the protein into the membrane, followed by a short cytosolic tail (CT).

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