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 / HeidelbergCategoriesSequencesSourceUniProtKB 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 19-27CategoriesSequencesSourceUniProtKB 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 TOLACategoriesInteractionSourceUniProtKB 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 forFUNCTIONCategoriesFunctionSourceUniProtKB 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 forFUNCTIONCategoriesFunctionSourceUniProtKB 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 20-85CategoriesStructureSourceUniProtKB 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
Elimination of a cis-proline-containing loop and turn optimization stabilizes a protein and accelerates its folding.Jakob R.P., Zierer B.K., Weininger U., Hofmann S.D., Lorenz S.H., Balbach J., Dobbek H., Schmid F.X.View abstractCategoriesStructureSourcePDB: 3KNQPubMedEurope PMCJ Mol Biol 399:331-346 (2010)Mapped to1
Changing the determinants of protein stability from covalent to non- covalent interactions by in vitro evolution: a structural and energetic analysis.Kather I., Jakob R., Dobbek H., Schmid F.X.View abstractCategoriesStructureSourcePDB: 3DGSPubMedEurope PMCJ Mol Biol 381:1040-1054 (2008)Mapped to1