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1
Q43029878-04FA67B9-53CA-4424-A524-C3C5BC19FA1E
Q43029878-04FA67B9-53CA-4424-A524-C3C5BC19FA1E
BestRank
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http://www.wikidata.org/entity/statement/Q43029878-04FA67B9-53CA-4424-A524-C3C5BC19FA1E
Slow-tight binding inhibition of xylanase by an aspartic protease inhibitor: kinetic parameters and conformational changes that determine the affinity and selectivity of the bifunctional nature of the inhibitor.
P2860
Q43029878-04FA67B9-53CA-4424-A524-C3C5BC19FA1E
BestRank
Statement
http://www.wikidata.org/entity/statement/Q43029878-04FA67B9-53CA-4424-A524-C3C5BC19FA1E
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type
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wasDerivedFrom
465e8da8daf5477982448aae0778e2d8c119734f
P2860
Approaches to labeling and identification of active site residues in glycosidases.