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1
Role of the bacteriophage P22 tail in the early stages of infection.
J Virol. 1976 Apr;18(1):361-4. doi: 10.1128/JVI.18.1.361-364.1976.
2
A model for the adsorption of phage P22 to Salmonella typhimurium.
J Gen Virol. 1978 Sep;40(3):669-73. doi: 10.1099/0022-1317-40-3-669.
3
Sonic fragility of the head-tail bond of bacteriophage P22.
J Virol. 1976 Feb;17(2):675-7. doi: 10.1128/JVI.17.2.675-677.1976.
4
Time-resolved DNA release from an O-antigen-specific bacteriophage with a contractile tail.
J Biol Chem. 2019 Aug 2;294(31):11751-11761. doi: 10.1074/jbc.RA119.008133. Epub 2019 Jun 12.
5
Adsorption of phage P22 to Salmonella typhimurium.
J Gen Virol. 1977 Feb;34(2):207-21. doi: 10.1099/0022-1317-34-2-207.
6
Smooth specific phage adsorption: endorhamnosidase activity of tail parts of P22.
Biochem Biophys Res Commun. 1973 Nov 16;55(2):403-9. doi: 10.1016/0006-291x(73)91101-7.
8
Structure and functions of the bacteriophage P22 tail protein.
J Virol. 1980 Apr;34(1):234-43. doi: 10.1128/JVI.34.1.234-243.1980.
9
Salmonella phage glycanases: substrate specificity of the phage P22 endo-rhamnosidase.
J Gen Virol. 1979 Jun;43(3):503-11. doi: 10.1099/0022-1317-43-3-503.
10
Effect of P22-mediated receptor release and of phage DNA injection on cell viability of Salmonella typhimurium.
J Gen Virol. 1986 Nov;67 ( Pt 11):2561-4. doi: 10.1099/0022-1317-67-11-2561.

引用本文的文献

1
Structural dynamics of bacteriophage P22 infection initiation revealed by cryo-electron tomography.
Nat Microbiol. 2019 Jun;4(6):1049-1056. doi: 10.1038/s41564-019-0403-z. Epub 2019 Mar 18.
2
Exploring the atomic structure and conformational flexibility of a 320 Å long engineered viral fiber using X-ray crystallography.
Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):342-53. doi: 10.1107/S1399004713027685. Epub 2014 Jan 29.

本文引用的文献

1
in vitro MORPHOGENESIS OF PHAGE P22 FROM HEADS AND BASE-PLATE PARTS.
Proc Natl Acad Sci U S A. 1967 Feb;57(2):284-91. doi: 10.1073/pnas.57.2.284.
2
TWO SEQUENTIAL REPRESSIONS OF DNA SYNTHESIS IN THE ESTABLISHMENT OF LYSOGENY BY PHAGE P22 AND ITS MUTANTS.
Proc Natl Acad Sci U S A. 1964 Aug;52(2):356-63. doi: 10.1073/pnas.52.2.356.
4
P22 morphogenesis. I: Catalytic scaffolding protein in capsid assembly.
J Supramol Struct. 1974;2(2-4):202-24. doi: 10.1002/jss.400020215.
5
Smooth specific phage adsorption: endorhamnosidase activity of tail parts of P22.
Biochem Biophys Res Commun. 1973 Nov 16;55(2):403-9. doi: 10.1016/0006-291x(73)91101-7.
6
Binding of bacteriophage P22 tail parts to cells.
J Virol. 1972 Dec;10(6):1152-8. doi: 10.1128/JVI.10.6.1152-1158.1972.
7
Genetics of bacteriophage P22. II. Gene order and gene function.
Virology. 1972 Jul;49(1):268-82. doi: 10.1016/s0042-6822(72)80028-x.
8
Inhibitory effect of bacteriophage P22 infection on host cell deoxyribonuclease activity.
J Virol. 1972 May;9(5):752-7. doi: 10.1128/JVI.9.5.752-757.1972.
10
Sonic fragility of the head-tail bond of bacteriophage P22.
J Virol. 1976 Feb;17(2):675-7. doi: 10.1128/JVI.17.2.675-677.1976.

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