Literature DB >> 7265217

Temperature-sensitive mutants blocked in the folding or subunit of the bacteriophage P22 tail spike protein. II. Active mutant proteins matured at 30 degrees C.

D P Goldenberg, J King.   

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Year:  1981        PMID: 7265217     DOI: 10.1016/0022-2836(81)90307-7

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


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  20 in total

1.  C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer.

Authors:  Matthew J Gage; Anne Skaja Robinson
Journal:  Protein Sci       Date:  2003-12       Impact factor: 6.725

2.  Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike.

Authors:  Brian G Lefebvre; Noelle K Comolli; Matthew J Gage; Anne Skaja Robinson
Journal:  Protein Sci       Date:  2004-05-07       Impact factor: 6.725

3.  Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike.

Authors:  Scott Betts; Cameron Haase-Pettingell; Kristen Cook; Jonathan King
Journal:  Protein Sci       Date:  2004-09       Impact factor: 6.725

4.  Three amino acids that are critical to formation and stability of the P22 tailspike trimer.

Authors:  Matthew J Gage; Jennifer L Zak; Anne Skaja Robinson
Journal:  Protein Sci       Date:  2005-08-04       Impact factor: 6.725

5.  Intragenic suppressors of folding defects in the P22 tailspike protein.

Authors:  B Fane; J King
Journal:  Genetics       Date:  1991-02       Impact factor: 4.562

6.  Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands.

Authors:  V N Uversky; V P Kutyshenko; V V Rogov; K S Vassilenko; A T Gudkov
Journal:  Protein Sci       Date:  1996-09       Impact factor: 6.725

7.  Isolation of suppressors of temperature-sensitive folding mutations.

Authors:  R Villafane; A Fleming; C Haase-Pettingell
Journal:  J Bacteriol       Date:  1994-01       Impact factor: 3.490

8.  Mechanism of phage P22 tailspike protein folding mutations.

Authors:  M Danner; R Seckler
Journal:  Protein Sci       Date:  1993-11       Impact factor: 6.725

9.  Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.

Authors:  S Miller; B Schuler; R Seckler
Journal:  Protein Sci       Date:  1998-10       Impact factor: 6.725

10.  Protein folding failure sets high-temperature limit on growth of phage P22 in Salmonella enterica serovar Typhimurium.

Authors:  Welkin H Pope; Cameron Haase-Pettingell; Jonathan King
Journal:  Appl Environ Microbiol       Date:  2004-08       Impact factor: 4.792

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