Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB.
about
Structural Basis for GTP-Dependent Dimerization of Hydrogenase Maturation Factor HypBStructure of UreG/UreF/UreH complex reveals how urease accessory proteins facilitate maturation of Helicobacter pylori ureaseMetal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPasesThe relationship between folding and activity in UreG, an intrinsically disordered enzyme.Interaction between hydrogenase maturation factors HypA and HypB is required for [NiFe]-hydrogenase maturation.YeiR: a metal-binding GTPase from Escherichia coli involved in metal homeostasisMetal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins.High-affinity metal binding by the Escherichia coli [NiFe]-hydrogenase accessory protein HypB is selectively modulated by SlyD.Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase.Escherichia coli SlyD, more than a Ni(II) reservoir.The metal selectivity of a short peptide maquette imitating the high-affinity metal-binding site of E. coli HypB.
P2860
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P2860
Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB.
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2011 nî lūn-bûn
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2011年の論文
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2011年学术文章
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2011年学术文章
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2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
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2011年學術文章
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2011年學術文章
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name
Relationship between the GTPas ...... on activities of E. coli HypB.
@en
Relationship between the GTPas ...... on activities of E. coli HypB.
@nl
type
label
Relationship between the GTPas ...... on activities of E. coli HypB.
@en
Relationship between the GTPas ...... on activities of E. coli HypB.
@nl
prefLabel
Relationship between the GTPas ...... on activities of E. coli HypB.
@en
Relationship between the GTPas ...... on activities of E. coli HypB.
@nl
P2093
P2860
P1476
Relationship between the GTPas ...... on activities of E. coli HypB.
@en
P2093
Harini Kaluarachchi
Thanh T Ngu
P2860
P2888
P304
P356
10.1007/S00775-011-0782-Y
P577
2011-05-05T00:00:00Z