Read e-book online ABC Transporters and Multidrug Resistance (Wiley Series in PDF

By Ahcene Boumendjel, Jean Boutonnat, Jacques Robert

ISBN-10: 0470227346

ISBN-13: 9780470227343

A complete assessment of the most up-tp-date clinical examine on ABC transporters and multidrug resistanceATP-binding cassette transporter genes (ABC transporters) are identified to play a very important function within the improvement of multidrug resistance (MDR). MDR is the facility of pathologic cells, akin to tumors, to resist chemical substances designed to focus on and wreck such cells. In MDR, sufferers who're on medicine finally strengthen resistance not to simply the drug they're taking, yet to numerous varieties of drugs.ABC Transporters and Multidrug Resistance bargains a necessary source for pharmaceutical researchers who're operating to find medications to counteract multidrug resistance in ailments akin to melanoma. in a single accomplished quantity, this publication incorporates a selection of the most up-tp-date wisdom at the involvement of ABC transporters in drug delivery and resistance.This accomplished quantity presents an summary at the description of the constitution, the genome, basic tissue expression, physiological element, and mechanism of motion of the ABC protein. The specialist members discover the expression, detection, and implications of ABC proteins in hematological malignancies and good tumors and ABC proteins and pathogenic microorganisms. This quantity additionally explains MDR modulation via inhibition of ABC transporters and the layout of inhibitors and mechanism of motion. moreover, the ebook bargains crucial details at the organic and scientific point of multidrug resistance.

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Extra info for ABC Transporters and Multidrug Resistance (Wiley Series in Drug Discovery and Development)

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In a second step, nucleotide binding and/or ATP hydrolysis causes conformational changes of the transporter, which subsequently can extract substrates from the inner leaf and pump them directly to the external aqueous medium (146, 147). This model is strengthened by data demonstrating unidirectional transport of fluorescent P-gp substrates from the cytoplasmic leaflet of the plasma membrane to the external aqueous environment (148). In the “flippase” model, P-gp encounters drugs in the inner leaflet of the plasma membrane and flips them to the outer leaflet from which they diffuse into the extracellular medium (149).

69. 70. 71. 72. 73. 74. 75. 76. 77. 78. 79. THE P-GLYCOPROTEIN 170 asymmetric configuration in the nucleotide-bound state. J Biol Chem 280: 2857–2862. Vandevuer S, Van Bambeke F, Tulkens PM, and Prévost M. 2006. Predicting the three-dimensional structure of human P-glycoprotein in absence of ATP by computational techniques embodying crosslinking data: Insight into the mechanism of ligand migration and binding sites. Proteins 63: 466–478. Lee JY, Urbatsch IL, Senior AE, and Wilkens S. 2008. Nucleotide-induced structural changes in P-glycoprotein observed by electron microscopy.

Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein. FASEB J 21: 3937–3948. 63. Rosenberg MF, Kamis AB, Callaghan R, Higgins CF, and Ford RC. 2003. Threedimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding. J Biol Chem 278: 8294–8299. 64. Rosenberg MF, Callaghan R, Modok S, Higgins CF, and Ford RC. 2005. Threedimensional structure of P-glycoprotein: The transmembrane regions adopt an 40 65.

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ABC Transporters and Multidrug Resistance (Wiley Series in Drug Discovery and Development) by Ahcene Boumendjel, Jean Boutonnat, Jacques Robert

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