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Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

169 related items for PubMed ID: 10074339

  • 1.
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  • 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
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  • 3. 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 23; 34(20):6815-26. PubMed ID: 7756313
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  • 4. Scaffolding mutants identifying domains required for P22 procapsid assembly and maturation.
    Greene B, King J.
    Virology; 1996 Nov 01; 225(1):82-96. PubMed ID: 8918536
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  • 5. GroEL binds a late folding intermediate of phage P22 coat protein.
    de Beus MD, Doyle SM, Teschke CM.
    Cell Stress Chaperones; 2000 Jul 01; 5(3):163-72. PubMed ID: 11005374
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  • 8. Structural transitions in the scaffolding and coat proteins of P22 virus during assembly and disassembly.
    Tuma R, Prevelige PE, Thomas GJ.
    Biochemistry; 1996 Apr 09; 35(14):4619-27. PubMed ID: 8605213
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  • 9. 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 09; 65(5):1300-10. PubMed ID: 17680786
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  • 11. Molecular genetics of bacteriophage P22 scaffolding protein's functional domains.
    Weigele PR, Sampson L, Winn-Stapley D, Casjens SR.
    J Mol Biol; 2005 May 13; 348(4):831-44. PubMed ID: 15843016
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  • 12. GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat protein.
    Nakonechny WS, Teschke CM.
    J Biol Chem; 1998 Oct 16; 273(42):27236-44. PubMed ID: 9765246
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  • 17. Structural roles of subunit cysteines in the folding and assembly of the DNA packaging machine (portal) of bacteriophage P22.
    Rodríguez-Casado A, Thomas GJ.
    Biochemistry; 2003 Apr 01; 42(12):3437-45. PubMed ID: 12653547
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  • 19. Alleviation of a defect in protein folding by increasing the rate of subunit assembly.
    Aramli LA, Teschke CM.
    J Biol Chem; 2001 Jul 06; 276(27):25372-7. PubMed ID: 11304542
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