Ligand Depletion in vivo Modulates the Dynamic Range of Cooperative Signal Transduction (original) (raw)

Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site

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Preventing Misfolding of the Prion Protein by Trimethylamine N -Oxide †

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assembly of Klebsiella aerogenes urease. UreG is required for in vivo metallocenter suggesting that a nucleotide-binding site in UreD-UreF-UreG complex, and evidence Characterization of UreG, identification of a

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Linked Folding and Anion Binding of the Bacillus subtilis Ribonuclease P Protein †

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Probing Protein-Protein Interactions: The Ribose-Binding Protein in Bacterial Transport and Chemotaxis

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Timothy Lohman

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The effect of the osmolyte trimethylamine N-oxide on the stability of the prion protein at low pH

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Characterization of UreG, identification of a UreD-UreF-UreG complex, and evidence suggesting that a nucleotide-binding site in UreG is required for in vivo metallocenter assembly of Klebsiella aerogenes urease

Robert Hausinger

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