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Journal Abstract Search
226 related items for PubMed ID: 15522085
41. GroEL walks the fine line: the subtle balance of substrate and co-chaperonin binding by GroEL. A combinatorial investigation by design, selection and screening. Kawe M, Plückthun A. J Mol Biol; 2006 Mar 24; 357(2):411-26. PubMed ID: 16427651 [Abstract] [Full Text] [Related]
42. Binding-induced stabilization and assembly of the phage P22 tail accessory factor gp4. Olia AS, Al-Bassam J, Winn-Stapley DA, Joss L, Casjens SR, Cingolani G. J Mol Biol; 2006 Oct 20; 363(2):558-76. PubMed ID: 16970964 [Abstract] [Full Text] [Related]
43. Electrostatic interactions drive scaffolding/coat protein binding and procapsid maturation in bacteriophage P22. Parker MH, Prevelige PE. Virology; 1998 Oct 25; 250(2):337-49. PubMed ID: 9792844 [Abstract] [Full Text] [Related]
44. The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein. Bakkes PJ, Faber BW, van Heerikhuizen H, van der Vies SM. Proc Natl Acad Sci U S A; 2005 Jun 07; 102(23):8144-9. PubMed ID: 15919824 [Abstract] [Full Text] [Related]
45. Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Jiang W, Li Z, Zhang Z, Baker ML, Prevelige PE, Chiu W. Nat Struct Biol; 2003 Feb 07; 10(2):131-5. PubMed ID: 12536205 [Abstract] [Full Text] [Related]
46. Protein folding failure sets high-temperature limit on growth of phage P22 in Salmonella enterica serovar Typhimurium. Pope WH, Haase-Pettingell C, King J. Appl Environ Microbiol; 2004 Aug 07; 70(8):4840-7. PubMed ID: 15294822 [Abstract] [Full Text] [Related]
47. Folding defects caused by single amino acid substitutions in a subunit are not alleviated by assembly. Capen CM, Teschke CM. Biochemistry; 2000 Feb 08; 39(5):1142-51. PubMed ID: 10653661 [Abstract] [Full Text] [Related]
48. Folding of the phage P22 coat protein in vitro. Teschke CM, King J. Biochemistry; 1993 Oct 12; 32(40):10839-47. PubMed ID: 8399234 [Abstract] [Full Text] [Related]
49. Electrostatic interactions govern both nucleation and elongation during phage P22 procapsid assembly. Parent KN, Doyle SM, Anderson E, Teschke CM. Virology; 2005 Sep 15; 340(1):33-45. PubMed ID: 16045955 [Abstract] [Full Text] [Related]
50. GroEL can unfold late intermediates populated on the folding pathways of monellin. Patra AK, Udgaonkar JB. J Mol Biol; 2009 Jun 19; 389(4):759-75. PubMed ID: 19393665 [Abstract] [Full Text] [Related]
51. Temperature-sensitive mutations and second-site suppressor substitutions affect folding of the P22 tailspike protein in vitro. Mitraki A, Danner M, King J, Seckler R. J Biol Chem; 1993 Sep 25; 268(27):20071-5. PubMed ID: 8376364 [Abstract] [Full Text] [Related]
52. A tail of protein folding. Villafañe RJ, Baksi K. P R Health Sci J; 1999 Jun 25; 18(2):105-15. PubMed ID: 10461316 [Abstract] [Full Text] [Related]
53. Bacteriophage P22 scaffolding protein forms oligomers in solution. Parker MH, Stafford WF, Prevelige PE. J Mol Biol; 1997 May 09; 268(3):655-65. PubMed ID: 9171289 [Abstract] [Full Text] [Related]
54. Mutations that stabilize folding intermediates of phage P22 tailspike protein: folding in vivo and in vitro, stability, and structural context. Beissinger M, Lee SC, Steinbacher S, Reinemer P, Huber R, Yu MH, Seckler R. J Mol Biol; 1995 May 26; 249(1):185-94. PubMed ID: 7776371 [Abstract] [Full Text] [Related]
59. Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Tang YC, Chang HC, Roeben A, Wischnewski D, Wischnewski N, Kerner MJ, Hartl FU, Hayer-Hartl M. Cell; 2006 Jun 02; 125(5):903-14. PubMed ID: 16751100 [Abstract] [Full Text] [Related]