Equilibrium folding of pro-HlyA from Escherichia coli reveals a stable calcium ion dependent folding intermediate

Author:

Thomas Sabrina,Bakkes Patrick J.,Smits Sander H.J.,Schmitt Lutz

Funder

Jürgen Manchot Graduate School “Molecules of Infection”

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference63 articles.

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2. The type 1 secretion pathway — the hemolysin system and beyond;Thomas;Biochim. Biophys. Acta,2014

3. RTX toxin structure and function: a story of numerous anomalies and few analogies in toxin biology;Welch;Curr. Top. Microbiol. Immunol.,2001

4. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif;Baumann;EMBO J.,1993

5. Cloning and functional characterization of the plasmid-encoded hemolysin determinant of Escherichia coli;Goebel;J. Bacteriol.,1982

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