Expression of fully active ammodytoxin A, a potent presynaptically neurotoxic phospholipase A2, in Escherichia coli.
about
Vipera ammodytes bites treated with antivenom ViperaTAb: a case series with pharmacokinetic evaluation.Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.Engineering the disulphide bond patterns of secretory phospholipases A2 into porcine pancreatic isozyme. The effects on folding, stability and enzymatic properties.An aromatic, but not a basic, residue is involved in the toxicity of group-II phospholipase A2 neurotoxins.A new phospholipase A2 isolated from the sea anemone Urticina crassicornis - its primary structure and phylogenetic classification.
P2860
Expression of fully active ammodytoxin A, a potent presynaptically neurotoxic phospholipase A2, in Escherichia coli.
description
1993 nî lūn-bûn
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1993年の論文
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1993年学术文章
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1993年学术文章
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1993年学术文章
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name
Expression of fully active amm ...... ipase A2, in Escherichia coli.
@en
Expression of fully active amm ...... ipase A2, in Escherichia coli.
@nl
type
label
Expression of fully active amm ...... ipase A2, in Escherichia coli.
@en
Expression of fully active amm ...... ipase A2, in Escherichia coli.
@nl
prefLabel
Expression of fully active amm ...... ipase A2, in Escherichia coli.
@en
Expression of fully active amm ...... ipase A2, in Escherichia coli.
@nl
P2093
P2860
P1433
P1476
Expression of fully active amm ...... ipase A2, in Escherichia coli.
@en
P2093
P2860
P356
10.1016/0014-5793(93)81679-T
P407
P577
1993-11-01T00:00:00Z