Purification, characterization, and primary structure of Clostridium perfringens lambda-toxin, a thermolysin-like metalloprotease.
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Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteinsClostridium perfringens epsilon toxin: a malevolent molecule for animals and man?Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin familyClostridium perfringensepsilon toxin H149A mutant as a platform for receptor binding studiesNeurotoxicity of Clostridium perfringens epsilon-toxin for the rat hippocampus via the glutamatergic system.Microbial metalloproteinases mediate sensing of invading pathogens and activate innate immune responses in the lepidopteran model host Galleria mellonellaCharacterization of virulence plasmid diversity among Clostridium perfringens type B isolates.Clostridium perfringens epsilon toxin mutant Y30A-Y196A as a recombinant vaccine candidate against enterotoxemiaStructural and functional characterization of mature forms of metalloprotease E495 from Arctic sea-ice bacterium Pseudoalteromonas sp. SM495.Necrotic enteritis-derived Clostridium perfringens strain with three closely related independently conjugative toxin and antibiotic resistance plasmids.Comparison of virulence plasmids among Clostridium perfringens type E isolatesVirulence plasmid diversity in Clostridium perfringens type D isolatesClostridium perfringens iota-toxin requires activation of both binding and enzymatic components for cytopathic activityPathogenic Leptospira Secreted Proteases Target the Membrane Attack Complex: A Potential Role for Thermolysin in Complement Inhibition.Identification of a lambda toxin-negative Clostridium perfringens strain that processes and activates epsilon prototoxin intracellularly.Promoter upstream bent DNA activates the transcription of the Clostridium perfringens phospholipase C gene in a low temperature-dependent manner.
P2860
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P2860
Purification, characterization, and primary structure of Clostridium perfringens lambda-toxin, a thermolysin-like metalloprotease.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Purification, characterization ...... rmolysin-like metalloprotease.
@en
Purification, characterization ...... rmolysin-like metalloprotease.
@nl
type
label
Purification, characterization ...... rmolysin-like metalloprotease.
@en
Purification, characterization ...... rmolysin-like metalloprotease.
@nl
prefLabel
Purification, characterization ...... rmolysin-like metalloprotease.
@en
Purification, characterization ...... rmolysin-like metalloprotease.
@nl
P2093
P2860
P1476
Purification, characterization ...... rmolysin-like metalloprotease.
@en
P2093
Katayama S
Matsushita C
Matsushita O
P2860
P304
P407
P577
1996-01-01T00:00:00Z