E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
about
Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli.The TPR domain of BepA is required for productive interaction with substrate proteins and the β-barrel assembly machinery complex.Distinctive Roles for Periplasmic Proteases in the Maintenance of Essential Outer Membrane Protein Assembly.Controlling molecular self-assembly: from amyloid oligomerization and therapy to novel biomaterials and technological applications in nanomedicine.
P2860
E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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2012年学术文章
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2012年学术文章
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name
E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
@en
E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
@nl
type
label
E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
@en
E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
@nl
prefLabel
E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
@en
E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
@nl
P2093
P2860
P356
P1433
P1476
E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
@en
P2093
Albert Sickmann
Christiane Lütticke
Markus Kaiser
Patrick Hauske
Urs Lewandrowski
P2860
P304
P356
10.1039/C2MB05506F
P577
2012-04-11T00:00:00Z