| pubmed-article:14754408 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14754408 | lifeskim:mentions | umls-concept:C0013227 | lld:lifeskim |
| pubmed-article:14754408 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:14754408 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:14754408 | lifeskim:mentions | umls-concept:C0242643 | lld:lifeskim |
| pubmed-article:14754408 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:14754408 | lifeskim:mentions | umls-concept:C1709060 | lld:lifeskim |
| pubmed-article:14754408 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:14754408 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:14754408 | pubmed:dateCreated | 2004-2-2 | lld:pubmed |
| pubmed-article:14754408 | pubmed:abstractText | A major problem in cancer treatment is the development of resistance to multiple chemotherapeutic agents in tumor cells. A major mechanism of this multidrug resistance (MDR) is overexpression of the MDR1 product P-glycoprotein, known to bind to and transport a wide variety of agents. This review concentrates on the progress made toward understanding the role of this protein in MDR, identifying and characterizing the drug binding sites of P-glycoprotein, and modulating MDR by P-glycoprotein-specific inhibitors. Since our initial discovery that P-glycoprotein binds to vinblastine photoaffinity analogs, many P-glycoprotein-specific photoaffinity analogs have been developed and used to identify the particular domains of P-glycoprotein capable of interacting with these analogs and other P-glycoprotein substrates. Furthermore, significant advances have been made in delineating the drug binding sites of this protein by studying mutant P-glycoprotein. Photoaffinity labeling experiments and the use of site-directed antibodies to several domains of this protein have allowed the localization of the general binding domains of some of the cytotoxic agents and MDR modulators on P-glycoprotein. Moreover, site-directed mutagenesis studies have identified the amino acids critical for the binding of some of these agents to P-glycoprotein. Furthermore, equilibrium binding assays using plasma membranes from MDR cells and radioactive drugs have aided our understanding of the modes of drug interactions with P-glycoprotein. Based on the available data, a topological model of P-glycoprotein and the approximate locations of its drug binding sites, as well as a proposed classification of multiple drug binding sites of this protein, is presented in this review. | lld:pubmed |
| pubmed-article:14754408 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754408 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754408 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754408 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14754408 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754408 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14754408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754408 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14754408 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:14754408 | pubmed:issn | 1568-0118 | lld:pubmed |
| pubmed-article:14754408 | pubmed:author | pubmed-author:SafaAhmad RAR | lld:pubmed |
| pubmed-article:14754408 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14754408 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:14754408 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14754408 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14754408 | pubmed:pagination | 1-17 | lld:pubmed |
| pubmed-article:14754408 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:14754408 | pubmed:meshHeading | pubmed-meshheading:14754408... | lld:pubmed |
| pubmed-article:14754408 | pubmed:meshHeading | pubmed-meshheading:14754408... | lld:pubmed |
| pubmed-article:14754408 | pubmed:meshHeading | pubmed-meshheading:14754408... | lld:pubmed |
| pubmed-article:14754408 | pubmed:meshHeading | pubmed-meshheading:14754408... | lld:pubmed |
| pubmed-article:14754408 | pubmed:meshHeading | pubmed-meshheading:14754408... | lld:pubmed |
| pubmed-article:14754408 | pubmed:meshHeading | pubmed-meshheading:14754408... | lld:pubmed |
| pubmed-article:14754408 | pubmed:meshHeading | pubmed-meshheading:14754408... | lld:pubmed |
| pubmed-article:14754408 | pubmed:meshHeading | pubmed-meshheading:14754408... | lld:pubmed |
| pubmed-article:14754408 | pubmed:meshHeading | pubmed-meshheading:14754408... | lld:pubmed |
| pubmed-article:14754408 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14754408 | pubmed:articleTitle | Identification and characterization of the binding sites of P-glycoprotein for multidrug resistance-related drugs and modulators. | lld:pubmed |
| pubmed-article:14754408 | pubmed:affiliation | Department of Pharmacology and Toxicology and Indiana University Cancer Center, West Walnut Street, Indianapolis, IN 46202, USA. asafa@iupui.edu | lld:pubmed |
| pubmed-article:14754408 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14754408 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14754408 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:14754408 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14754408 | lld:pubmed |
