NMR Solution Structure of SlyD from Escherichia coli: Spatial Separation of Prolyl Isomerase and Chaperone Function-Reference-Cited by-同舟云学术

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

Published:2009-03 Issue:2 Volume:387 Page:295-305
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Weininger Ulrich,Haupt Caroline,Schweimer Kristian,Graubner Wenke,Kovermann Michael,Brüser Thomas,Scholz Christian,Schaarschmidt Peter,Zoldak Gabriel,Schmid Franz X.,Balbach Jochen

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference42 articles.

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4. SlyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis–trans-isomerases;Roof;J. Biol. Chem.,1994

5. SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities;Scholz;Biochemistry,2006

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