Structure of Rhodococcus equivirulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs
about
Structural characterisation of the virulence-associated protein VapG from the horse pathogen Rhodococcus equi.Transcriptome reprogramming by plasmid-encoded transcriptional regulators is required for host niche adaption of a macrophage pathogenThe Rhodococcus equi virulence protein VapA disrupts endolysosome function and stimulates lysosome biogenesis.Higher-Order Structure in Bacterial VapBC Toxin-Antitoxin Complexes.VapA of Rhodococcus equi binds phosphatidic acid.Resonance assignments of a VapC family toxin from Clostridium thermocellum.
P2860
Structure of Rhodococcus equivirulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs
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2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հուլիսին հրատարակված գիտական հոդված
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年论文
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name
Structure of Rhodococcus equiv ...... isting of two Greek-key motifs
@ast
Structure of Rhodococcus equiv ...... isting of two Greek-key motifs
@en
Structure of Rhodococcus equiv ...... isting of two Greek-key motifs
@nl
type
label
Structure of Rhodococcus equiv ...... isting of two Greek-key motifs
@ast
Structure of Rhodococcus equiv ...... isting of two Greek-key motifs
@en
Structure of Rhodococcus equiv ...... isting of two Greek-key motifs
@nl
prefLabel
Structure of Rhodococcus equiv ...... isting of two Greek-key motifs
@ast
Structure of Rhodococcus equiv ...... isting of two Greek-key motifs
@en
Structure of Rhodococcus equiv ...... isting of two Greek-key motifs
@nl
P2093
P2860
P1476
Structure of Rhodococcus equiv ...... isting of two Greek-key motifs
@en
P2093
Albert Haas
Christina Geerds
Hartmut H Niemann
Jens Wohlmann
P2860
P304
P356
10.1107/S2053230X14009911
P577
2014-07-01T00:00:00Z