The interaction of theEscherichia coliprotein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity-Reference-Cited by-同舟云学术

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

Published:2009-08 Issue:16 Volume:276 Page:4529-4544
ISSN:1742-464X
Container-title:FEBS Journal
language:en
Short-container-title:

Author:

Martino Luigi,He Yangzi,Hands-Taylor Katherine L. D.,Valentine Elizabeth R.,Kelly Geoff,Giancola Concetta,Conte Maria R.

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2009.07159.x/fullpdf

Reference58 articles.

1. Deletion and fusion analysis of the phage phi X174 lysis gene E;Maratea;Gene,1985

2. An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif;Wulfing;J Biol Chem,1994

3. Phi X174 lysis requires slyD, a host gene which is related to the FKBP family of peptidyl-prolyl cis-trans isomerases;Roof;FEMS Microbiol Rev,1995

4. Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography;Bolanos-Garcia;Biochim Biophys Acta,2006

5. 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

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