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Goldenberg, D. P., Smith, D. H., King, J. (1983) Genetic analysis of the folding pathway for the tail spike protein of phage P22. Proceedings of the National Academy of Sciences, 80 (23) 7060-7064 doi:10.1073/pnas.80.23.7060

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Reference TypeJournal (article/letter/editorial)
TitleGenetic analysis of the folding pathway for the tail spike protein of phage P22.
JournalProceedings of the National Academy of Sciences
AuthorsGoldenberg, D. P.Author
Smith, D. H.Author
King, J.Author
Year1983 (December 1)Volume80
Issue23
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.80.23.7060Search in ResearchGate
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Mindat Ref. ID1431639Long-form Identifiermindat:1:5:1431639:1
GUID0
Full ReferenceGoldenberg, D. P., Smith, D. H., King, J. (1983) Genetic analysis of the folding pathway for the tail spike protein of phage P22. Proceedings of the National Academy of Sciences, 80 (23) 7060-7064 doi:10.1073/pnas.80.23.7060
Plain TextGoldenberg, D. P., Smith, D. H., King, J. (1983) Genetic analysis of the folding pathway for the tail spike protein of phage P22. Proceedings of the National Academy of Sciences, 80 (23) 7060-7064 doi:10.1073/pnas.80.23.7060
In(1983, December) Proceedings of the National Academy of Sciences Vol. 80 (23) Proceedings of the National Academy of Sciences

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Yu, M. H., King, J. (1984) Single amino acid substitutions influencing the folding pathway of the phage P22 tail spike endorhamnosidase. Proceedings of the National Academy of Sciences, 81 (21) 6584-6588 doi:10.1073/pnas.81.21.6584
Goldenberg, D., King, J. (1982) Trimeric intermediate in the in vivo folding and subunit assembly of the tail spike endorhamnosidase of bacteriophage P22. Proceedings of the National Academy of Sciences, 79 (11) 3403-3407 doi:10.1073/pnas.79.11.3403
Goldenberg, David P., King, Jonathan (1981) Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein. Journal of Molecular Biology, 145 (4). 633-651 doi:10.1016/0022-2836(81)90307-7
Skolnick, J. (2005) Putting the pathway back into protein folding. Proceedings of the National Academy of Sciences, 102 (7) 2265-2266 doi:10.1073/pnas.0500128102
Smith, Donna H., King, Jonathan (1981) Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein. Journal of Molecular Biology, 145 (4). 653-676 doi:10.1016/0022-2836(81)90308-9
Pukatzki, S., Ma, A. T., Revel, A. T., Sturtevant, D., Mekalanos, J. J. (2007) Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin. Proceedings of the National Academy of Sciences, 104 (39) 15508-15513 doi:10.1073/pnas.0706532104
Watabe, K., Shin, M., Ito, J. (1983) Protein-primed initiation of phage phi 29 DNA replication. Proceedings of the National Academy of Sciences, 80 (14) 4248-4252 doi:10.1073/pnas.80.14.4248
Gauss, P., Doherty, D. H., Gold, L. (1983) Bacterial and phage mutations that reveal helix-unwinding activities required for bacteriophage T4 DNA replication. Proceedings of the National Academy of Sciences, 80 (6) 1669-1673 doi:10.1073/pnas.80.6.1669
Goldenberg, D. P., Berger, J. M., Laheru, D. A., Wooden, S., Zhang, J. X. (1992) Genetic dissection of pancreatic trypsin inhibitor. Proceedings of the National Academy of Sciences, 89 (11) 5083-5087 doi:10.1073/pnas.89.11.5083
Simkovsky, R., King, J. (2006) An elongated spine of buried core residues necessary for in vivo folding of the parallel beta-helix of P22 tailspike adhesin. Proceedings of the National Academy of Sciences, 103 (10) 3575-3580 doi:10.1073/pnas.0509087103
Yaneva, J., Schroth, G. P., van Holde, K. E., Zlatanova, J. (1995) High-affinity binding sites for histone H1 in plasmid DNA. Proceedings of the National Academy of Sciences, 92 (15) 7060-7064 doi:10.1073/pnas.92.15.7060
 
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