The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors (Q27732575)

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E J Dodson

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B F Anderson

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C J Marshall

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P A Sullivan

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J F Cutfield

The emerging fungal threat

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publication date

15 November 1995

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published in

Structure

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volume

3

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issue

11

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page(s)

1261-71

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cites work

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

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The structure and function of the aspartic proteinases

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Crystallization of Inhibited Aspartic Proteinase from Candida albicans

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Application of a fluorogenic substrate in the assay of proteolytic activity and in the discovery of a potent inhibitor of Candida albicans aspartic proteinase

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Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain

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Domain flexibility in aspartic proteinases

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The γ Turn, a Possible Folded Conformation of the Polypeptide Chain. Comparison with the β Turn

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A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica

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Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin

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Identifiers

DOI

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Fatcat ID

release_aspgayflkrbsph4fet7uwirbde

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/aspgayflkrbsph4fet7uwirbde

24 November 2022