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Q43029878-A0D98CE9-594F-4FB3-A28B-AC19BF9EE11A
Q43029878-A0D98CE9-594F-4FB3-A28B-AC19BF9EE11A
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http://www.wikidata.org/entity/statement/Q43029878-A0D98CE9-594F-4FB3-A28B-AC19BF9EE11A
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-A0D98CE9-594F-4FB3-A28B-AC19BF9EE11A
BestRank
Statement
http://www.wikidata.org/entity/statement/Q43029878-A0D98CE9-594F-4FB3-A28B-AC19BF9EE11A
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wasDerivedFrom
465e8da8daf5477982448aae0778e2d8c119734f
P2860
Crystal structure of the catalytic domain of the beta-1,4-glycanase cex from Cellulomonas fimi