TheEscherichia colimetal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3

The Helicobacter pylori GroES Cochaperonin HspA Functions as a Specialized Nickel Chaperone and Sequestration Protein through Its Unique C-Terminal Extension

(2010) K. Schauer et al.   JOURNAL OF BACTERIOLOGY

Crystal Structure Determination and Functional Characterization of the Metallochaperone SlyD from Thermus thermophilus

(2010) Christian Löw et al.   JOURNAL OF MOLECULAR BIOLOGY

The interaction of theEscherichia coliprotein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity

(2009) Luigi Martino et al.   FEBS Journal

NMR Solution Structure of SlyD from Escherichia coli: Spatial Separation of Prolyl Isomerase and Chaperone Function

(2009) Ulrich Weininger et al.   JOURNAL OF MOLECULAR BIOLOGY

The Ni(II)-Binding Properties of the Metallochaperone SlyD

(2009) Harini Kaluarachchi et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

In VivoInteractome ofHelicobacter pyloriUrease Revealed by Tandem Affinity Purification

(2008) Kerstin Stingl et al.   MOLECULAR & CELLULAR PROTEOMICS