The assembly factor P17 from bacteriophage PRD1 interacts with positively charged lipid membranes
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1432-1327.2000.01708.x/fullpdf
Reference30 articles.
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2. Overexpression, purification, and characterization of Escherichia coli bacteriophage PRD1 DNA polymerase. In vitro synthesis of full-length PRD1 DNA with purified proteins;Savilahti;J. Biol. Chem.,1991
3. DNA packaging orders the membrane of bacteriophage PRD1;Butcher;EMBO J.,1995
4. Bacteriophage PRD1 contains a labile receptor-binding structure at each vertex;Rydman;J. Mol. Biol.,1998
5. New mutant class, made by targeted mutagenesis, of phage PRD1 reveals that protein P5 connects the receptor binding protein to the vertex;Bamford;J. Virol.,2000
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1. Non-structural proteins P17 and P33 are involved in the assembly of the internal membrane-containing virus PRD1;Virology;2015-08
2. Comparison of Lipid-Containing Bacterial and Archaeal Viruses;Advances in Virus Research;2015
3. Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli;Virus Research;2014-01
4. Lipid-Containing Viruses: Bacteriophage PRD1 Assembly;Viral Molecular Machines;2011-11-08
5. Hsp70 stabilizes lysosomes and reverts Niemann–Pick disease-associated lysosomal pathology;Nature;2010-01-27
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