Insights into the selective inhibition of Candida albicans secreted aspartyl protease: a docking analysis study (Q42165805)

17 October 2017

Insights into the selective inhibition of Candida albicans secreted aspartyl protease: a docking analysis study (English)

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17 October 2017

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S K Pranav Kumar

1

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PubMed ID

11836127

17 October 2017

Vithal M Kulkarni

series ordinal

2

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PubMed ID

11836127

17 October 2017

language of work or name

English

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publication date

1 April 2002

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Bioorganic & Medicinal Chemistry

17 October 2017

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17 October 2017

10

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17 October 2017

4

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17 October 2017

1153-1170

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Recent progress and current problems in treatment of invasive fungal infections in neutropenic patients

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Nosocomial fungal infections: a classification for hospital-acquired fungal infections and mycoses arising from endogenous flora or reactivation

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Candida proteinases and candidosis

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The structure and function of the aspartic proteinases

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Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica

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Candida albicans secreted aspartyl proteinases: isoenzyme pattern is determined by cell type, and levels are determined by environmental factors.

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Expression of seven members of the gene family encoding secretory aspartyl proteinases in Candida albicans

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The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors

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Selectivity analysis of 5-(arylthio)-2,4-diaminoquinazolines as inhibitors of Candida albicans dihydrofolate reductase by molecular dynamics simulations

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Identifiers

DOI

1 reference

17 October 2017

1 reference

PubMed ID

11836127