Nucleotide sequence of bacteriophage fd DNA.Beck E., Sommer R., Auerswald E.A., Kurz C., Zink B., Osterburg G., Schaller H., Sugimoto K., Sugisaki H.[...], Takanami M.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]Strain478 / HeidelbergCategorySequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNucleic Acids Res. 5:4495-4503 (1978)Cited in9
Adsorption protein of the bacteriophage fd: isolation, molecular properties, and location in the virus.Goldsmith M.E., Konigsberg W.H.View abstractCited forPROTEIN SEQUENCE OF 19-27CategorySequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 16:2686-2694 (1977)Cited in1
The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli.Riechmann L., Holliger P.View abstractCited forINTERACTION WITH HOST TOLACategoryInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 90:351-360 (1997)Cited in1
Delineating the site of interaction on the pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli.Deng L.W., Perham R.N.View abstractCited forFUNCTIONCategoryFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 319:603-614 (2002)Cited in1
The filamentous phages fd and IF1 use different mechanisms to infect Escherichia coli.Lorenz S.H., Jakob R.P., Weininger U., Balbach J., Dobbek H., Schmid F.X.View abstractCited forFUNCTIONCategoryFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 405:989-1003 (2011)Cited in21
A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd.Holliger P., Riechmann L.View abstractCited forSTRUCTURE BY NMR OF 20-85CategoryStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCStructure 5:265-275 (1997)Cited in1
Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 A: evidence for conformational lability.Holliger P., Riechmann L., Williams R.L.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-235, DISULFIDE BONDSCategoriesPTM / Processing, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 288:649-657 (1999)Cited in1