The structure of urease activation complexes examined by flexibility analysis, mutagenesis, and small-angle X-ray scattering
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Interplay of metal ions and ureaseEvolution of Macromolecular Docking Techniques: The Case Study of Nickel and Iron Metabolism in Pathogenic BacteriaCrystal structure of a truncated urease accessory protein UreF from Helicobacter pyloriAssembly of Preactivation Complex for Urease Maturation in Helicobacter pylori: CRYSTAL STRUCTURE OF UreF-UreH PROTEIN COMPLEXStructure of UreG/UreF/UreH complex reveals how urease accessory proteins facilitate maturation of Helicobacter pylori ureaseThe crystal structure of Sporosarcina pasteurii urease in a complex with citrate provides new hints for inhibitor designFluoride inhibition of Sporosarcina pasteurii urease: structure and thermodynamicsMutational and Computational Evidence That a Nickel-Transfer Tunnel in UreD Is Used for Activation of Klebsiella aerogenes Urease.Structure of Rv1848 (UreA), the Mycobacterium tuberculosis urease gamma subunitMutagenesis of Klebsiella aerogenes UreG to probe nickel binding and interactions with other urease-related proteins.Analysis of a soluble (UreD:UreF:UreG)2 accessory protein complex and its interactions with Klebsiella aerogenes urease by mass spectrometry.Function of UreB in Klebsiella aerogenes urease.Klebsiella aerogenes UreF: identification of the UreG binding site and role in enhancing the fidelity of urease activation.Biosynthesis of the urease metallocenterNickel binding properties of Helicobacter pylori UreF, an accessory protein in the nickel-based activation of urease.Functional and phylogenetic analysis of ureD in Shiga toxin-producing Escherichia coli.Helicobacter pylori UreE, a urease accessory protein: specific Ni(2+)- and Zn(2+)-binding properties and interaction with its cognate UreG.Structural insights into how GTP-dependent conformational changes in a metallochaperone UreG facilitate urease maturation.A Structural Model of the Urease Activation Complex Derived from Ion Mobility-Mass Spectrometry and Integrative Modeling.His-rich sequences – is plagiarism from nature a good idea?Evidence-based docking of the urease activation complex
P2860
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P2860
The structure of urease activation complexes examined by flexibility analysis, mutagenesis, and small-angle X-ray scattering
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 18 September 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
The structure of urease activa ...... d small-angle X-ray scattering
@en
The structure of urease activa ...... small-angle X-ray scattering.
@nl
type
label
The structure of urease activa ...... d small-angle X-ray scattering
@en
The structure of urease activa ...... small-angle X-ray scattering.
@nl
prefLabel
The structure of urease activa ...... d small-angle X-ray scattering
@en
The structure of urease activa ...... small-angle X-ray scattering.
@nl
P2093
P2860
P1476
The structure of urease activa ...... d small-angle X-ray scattering
@en
P2093
Leslie A Kuhn
Sai Chetan K Sukuru
Soledad Quiroz-Valenzuela
P2860
P356
10.1016/J.ABB.2008.09.004
P407
P577
2008-09-18T00:00:00Z