Title |
Molecular mechanism of the camptothecin resistance of Glu710Gly topoisomerase IB mutant analyzed in vitro and in silico
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Published in |
Molecular Cancer, September 2013
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DOI | 10.1186/1476-4598-12-100 |
Pubmed ID | |
Authors |
Cinzia Tesauro, Blasco Morozzo della Rocca, Alessio Ottaviani, Andrea Coletta, Laura Zuccaro, Barbara Arnò, Ilda D'Annessa, Paola Fiorani, Alessandro Desideri |
Abstract |
DNA topoisomerases are key enzymes that modulate the topological state of DNA through the breaking and rejoining of DNA strands. Human topoisomerase IB can be inhibited by several compounds that act through different mechanisms, including clinically used drugs, such as the derivatives of the natural compound camptothecin that reversibly bind the covalent topoisomerase-DNA complex, slowing down the religation of the cleaved DNA strand, thus inducing cell death. Three enzyme mutations, which confer resistance to irinotecan in an adenocarcinoma cell line, were recently identified but the molecular mechanism of resistance was unclear. |
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Unknown | 1 | 100% |
Demographic breakdown
Type | Count | As % |
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
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India | 1 | 3% |
Denmark | 1 | 3% |
Unknown | 35 | 95% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 11 | 30% |
Student > Ph. D. Student | 9 | 24% |
Student > Master | 4 | 11% |
Student > Bachelor | 4 | 11% |
Student > Doctoral Student | 3 | 8% |
Other | 4 | 11% |
Unknown | 2 | 5% |
Readers by discipline | Count | As % |
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Pharmacology, Toxicology and Pharmaceutical Science | 1 | 3% |
Other | 2 | 5% |
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