Functional and biochemical characterization of the baculovirus caspase inhibitor MaviP35
about
The N Terminus of the Vaccinia Virus Protein F1L Is an Intrinsically Unstructured Region That Is Not Involved in Apoptosis Regulation.Caspase inhibitors of the P35 family are more active when purified from yeast than bacteria.SfDronc, an initiator caspase involved in apoptosis in the fall armyworm Spodoptera frugiperda.Yeast techniques for modeling drugs targeting Bcl-2 and caspase family members.Analysis of the minimal specificity of caspase-2 and identification of Ac-VDTTD-AFC as a caspase-2-selective peptide substrate.Vaccinia virus encodes a novel inhibitor of apoptosis that associates with the apoptosome.Anti-proliferative and pro-apoptotic effects induced by simultaneous inactivation of HER1 and HER2 through endogenous polyclonal antibodies.
P2860
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P2860
Functional and biochemical characterization of the baculovirus caspase inhibitor MaviP35
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Functional and biochemical characterization of the baculovirus caspase inhibitor MaviP35
@ast
Functional and biochemical characterization of the baculovirus caspase inhibitor MaviP35
@en
type
label
Functional and biochemical characterization of the baculovirus caspase inhibitor MaviP35
@ast
Functional and biochemical characterization of the baculovirus caspase inhibitor MaviP35
@en
prefLabel
Functional and biochemical characterization of the baculovirus caspase inhibitor MaviP35
@ast
Functional and biochemical characterization of the baculovirus caspase inhibitor MaviP35
@en
P2093
P2860
P356
P1476
Functional and biochemical characterization of the baculovirus caspase inhibitor MaviP35
@en
P2093
D Pantaki-Eimany
P2860
P356
10.1038/CDDIS.2011.127
P577
2011-12-15T00:00:00Z