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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5
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|
pubmed:dateCreated |
2010-4-6
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|
pubmed:abstractText |
The cytochrome P450 lanosterol 14alpha-demethylase (Erg11p) encoded by ERG11 gene is the primary target for azole antifungals. Changes in azole affinity of this enzyme caused by amino acid substitutions have been reported as a mechanism of azole antifungal resistance. This study aimed to investigate the relationship between amino acid substitutions in Erg11p from fluconazole resistant Candida albicans (C. albicans) isolates and their cross-resistance to azoles.
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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pubmed:month |
Mar
|
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pubmed:issn |
0366-6999
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
123
|
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pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
544-8
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pubmed:dateRevised |
2010-9-14
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pubmed:meshHeading |
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pubmed:year |
2010
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|
pubmed:articleTitle |
Relationship between antifungal resistance of fluconazole resistant Candida albicans and mutations in ERG11 gene.
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|
pubmed:affiliation |
Department of Dermatology, Peking University First Hospital; Research Center for Medical Mycology, Peking University, Beijing 100034, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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