Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.
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Evolution of Macromolecular Docking Techniques: The Case Study of Nickel and Iron Metabolism in Pathogenic BacteriaStructure of UreG/UreF/UreH complex reveals how urease accessory proteins facilitate maturation of Helicobacter pylori ureaseSelectivity of Ni(II) and Zn(II) binding to Sporosarcina pasteurii UreE, a metallochaperone in the urease assembly: a calorimetric and crystallographic studyCommon themes and unique proteins for the uptake and trafficking of nickel, a metal essential for the virulence of Helicobacter pyloriNickel trafficking system responsible for urease maturation in Helicobacter pylori.Nickel binding properties of Helicobacter pylori UreF, an accessory protein in the nickel-based activation of urease.Metallochaperones and metalloregulation in bacteria.
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P2860
Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.
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2013 nî lūn-bûn
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2013年の論文
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2013年学术文章
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name
Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.
@en
Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.
@nl
type
label
Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.
@en
Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.
@nl
prefLabel
Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.
@en
Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.
@nl
P2860
P1476
Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.
@en
P2093
Francesco Biagi
P2860
P2888
P304
P356
10.1007/S00775-013-1002-8
P577
2013-05-10T00:00:00Z