ZraP is a periplasmic molecular chaperone and a repressor of the zinc-responsive two-component regulator ZraSR

Structure-based de novo prediction of zinc-binding sites in proteins of unknown function

(2011) Wei Zhao et al.   BIOINFORMATICS

Structure of the Periplasmic Stress Response Protein CpxP

(2011) G. L. Thede et al.   JOURNAL OF BACTERIOLOGY

Structural Basis for Two-component System Inhibition and Pilus Sensing by the Auxiliary CpxP Protein

(2011) Xiaohui Zhou et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Dynamics of a starvation-to-surfeit shift: a transcriptomic and modelling analysis of the bacterial response to zinc reveals transient behaviour of the Fur and SoxS regulators

(2011) A. I. Graham et al.   MICROBIOLOGY-SGM

Genetic selection designed to stabilize proteins uncovers a chaperone called Spy

(2011) Shu Quan et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Novel Inducers of the Envelope Stress Response BaeSR in Salmonella Typhimurium: BaeR Is Critically Required for Tungstate Waste Disposal

(2011) Corinne Appia-Ayme et al.   PLoS One

Protein Quality Control in the Bacterial Periplasm

(2010) Melisa Merdanovic et al.   Annual Review of Microbiology

The crystal structureEscherichia coliSpy

(2010) Eunju Kwon et al.   PROTEIN SCIENCE

Severe Zinc Depletion ofEscherichia coli

(2009) Alison I. Graham et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Investigation of the role of the BAM complex and SurA chaperone in outer-membrane protein biogenesis and type III secretion system expression in Salmonella

(2009) Y. Fardini et al.   MICROBIOLOGY-SGM