232 related articles for article (PubMed ID: 17680786)
1. Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching.
Parent KN; Suhanovsky MM; Teschke CM
Mol Microbiol; 2007 Sep; 65(5):1300-10. PubMed ID: 17680786
[TBL] [Abstract][Full Text] [Related]
2. A second-site suppressor of a folding defect functions via interactions with a chaperone network to improve folding and assembly in vivo.
Parent KN; Ranaghan MJ; Teschke CM
Mol Microbiol; 2004 Nov; 54(4):1036-50. PubMed ID: 15522085
[TBL] [Abstract][Full Text] [Related]
3. GroEL/S substrate specificity based on substrate unfolding propensity.
Parent KN; Teschke CM
Cell Stress Chaperones; 2007; 12(1):20-32. PubMed ID: 17441504
[TBL] [Abstract][Full Text] [Related]
4. A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly.
D'Lima NG; Teschke CM
J Virol; 2015 Oct; 89(20):10569-79. PubMed ID: 26269173
[TBL] [Abstract][Full Text] [Related]
5. Cryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins.
Parent KN; Sinkovits RS; Suhanovsky MM; Teschke CM; Egelman EH; Baker TS
Phys Biol; 2010 Dec; 7(4):045004. PubMed ID: 21149969
[TBL] [Abstract][Full Text] [Related]
6. A concerted mechanism for the suppression of a folding defect through interactions with chaperones.
Doyle SM; Anderson E; Parent KN; Teschke CM
J Biol Chem; 2004 Apr; 279(17):17473-82. PubMed ID: 14764588
[TBL] [Abstract][Full Text] [Related]
7. Aggregation and assembly of phage P22 temperature-sensitive coat protein mutants in vitro mimic the in vivo phenotype.
Teschke CM
Biochemistry; 1999 Mar; 38(10):2873-81. PubMed ID: 10074339
[TBL] [Abstract][Full Text] [Related]
8. The role of the coat protein A-domain in p22 bacteriophage maturation.
Morris DS; Prevelige PE
Viruses; 2014 Jul; 6(7):2708-22. PubMed ID: 25025835
[TBL] [Abstract][Full Text] [Related]
9. Bacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus.
Suhanovsky MM; Teschke CM
Virology; 2011 Sep; 417(2):418-29. PubMed ID: 21784500
[TBL] [Abstract][Full Text] [Related]
10. Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching.
Suhanovsky MM; Parent KN; Dunn SE; Baker TS; Teschke CM
Mol Microbiol; 2010 Sep; 77(6):1568-82. PubMed ID: 20659287
[TBL] [Abstract][Full Text] [Related]
11. 'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants.
Teschke CM; Parent KN
Virology; 2010 Jun; 401(2):119-30. PubMed ID: 20236676
[TBL] [Abstract][Full Text] [Related]
12. Interactions between coat and scaffolding proteins of phage P22 are altered in vitro by amino acid substitutions in coat protein that cause a cold-sensitive phenotype.
Teschke CM; Fong DG
Biochemistry; 1996 Nov; 35(47):14831-40. PubMed ID: 8942646
[TBL] [Abstract][Full Text] [Related]
13. Quantitative analysis of multi-component spherical virus assembly: scaffolding protein contributes to the global stability of phage P22 procapsids.
Parent KN; Zlotnick A; Teschke CM
J Mol Biol; 2006 Jun; 359(4):1097-106. PubMed ID: 16697406
[TBL] [Abstract][Full Text] [Related]
14. Phage P22 procapsids equilibrate with free coat protein subunits.
Parent KN; Suhanovsky MM; Teschke CM
J Mol Biol; 2007 Jan; 365(2):513-22. PubMed ID: 17067636
[TBL] [Abstract][Full Text] [Related]
15. In vitro folding of phage P22 coat protein with amino acid substitutions that confer in vivo temperature sensitivity.
Teschke CM; King J
Biochemistry; 1995 May; 34(20):6815-26. PubMed ID: 7756313
[TBL] [Abstract][Full Text] [Related]
16. Folding defects caused by single amino acid substitutions in a subunit are not alleviated by assembly.
Capen CM; Teschke CM
Biochemistry; 2000 Feb; 39(5):1142-51. PubMed ID: 10653661
[TBL] [Abstract][Full Text] [Related]
17. Identification of subunit-subunit interactions in bacteriophage P22 procapsids by chemical cross-linking and mass spectrometry.
Kang S; Hawkridge AM; Johnson KL; Muddiman DC; Prevelige PE
J Proteome Res; 2006 Feb; 5(2):370-7. PubMed ID: 16457603
[TBL] [Abstract][Full Text] [Related]
18. Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein.
Aramli LA; Teschke CM
J Biol Chem; 1999 Aug; 274(32):22217-24. PubMed ID: 10428787
[TBL] [Abstract][Full Text] [Related]
19. Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties.
Anderson E; Teschke CM
Virology; 2003 Aug; 313(1):184-97. PubMed ID: 12951032
[TBL] [Abstract][Full Text] [Related]
20. Rapid unfolding of a domain populates an aggregation-prone intermediate that can be recognized by GroEL.
Doyle SM; Anderson E; Zhu D; Braswell EH; Teschke CM
J Mol Biol; 2003 Sep; 332(4):937-51. PubMed ID: 12972263
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
