A Conformational Unfolding Reaction Activates Phage fd for the Infection of Escherichia coli
- 1 October 2007
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 373 (2) , 452-461
- https://doi.org/10.1016/j.jmb.2007.07.060
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signalingJournal of Molecular Recognition, 2005
- Natively unfolded proteinsCurrent Opinion in Structural Biology, 2005
- Protein unfolding in the cellTrends in Biochemical Sciences, 2004
- Unfolded Proteins and Protein Folding Studied by NMRChemical Reviews, 2004
- The Mechanism of Bacterial Infection by Filamentous Phages Involves Molecular Interactions between TolA and Phage Protein 3 DomainsJournal of Bacteriology, 2003
- Delineating the Site of Interaction on the pIII Protein of Filamentous Bacteriophage fd with the F-pilus of Escherichia coliJournal of Molecular Biology, 2002
- Interdomain interactions within the gene 3 protein of filamentous phageFEBS Letters, 1999
- Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 Å: evidence for conformational lability 1 1Edited by J. M. ThorntonJournal of Molecular Biology, 1999
- Interaction of the Globular Domains of pIII Protein of Filamentous Bacteriophage fd with the F-Pilus ofEscherichia coliVirology, 1999
- The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3pNature Structural & Molecular Biology, 1998