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Journal Abstract Search

634 related items for PubMed ID: 19099423

  • 1. The partially folded homodimeric intermediate of Escherichia coli aspartate aminotransferase contains a "molten interface" structure.
    Deu E, Dhoot J, Kirsch JF.
    Biochemistry; 2009 Jan 20; 48(2):433-41. PubMed ID: 19099423
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  • 3. The unfolding pathway for Apo Escherichia coli aspartate aminotransferase is dependent on the choice of denaturant.
    Deu E, Kirsch JF.
    Biochemistry; 2007 May 15; 46(19):5810-8. PubMed ID: 17425331
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  • 4. Thermodynamic analysis of unfolding and dissociation in lactose repressor protein.
    Barry JK, Matthews KS.
    Biochemistry; 1999 May 18; 38(20):6520-8. PubMed ID: 10350470
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  • 5. Stability and unfolding of reduced Escherichia coli glutaredoxin 2: a monomeric structural homologue of the glutathione transferase family.
    Gildenhuys S, Wallace LA, Dirr HW.
    Biochemistry; 2008 Oct 07; 47(40):10801-8. PubMed ID: 18788752
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  • 6. Pro-sequence and Ca2+-binding: implications for folding and maturation of Ntn-hydrolase penicillin amidase from E. coli.
    Ignatova Z, Wischnewski F, Notbohm H, Kasche V.
    J Mol Biol; 2005 May 13; 348(4):999-1014. PubMed ID: 15843029
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  • 7. Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate.
    Grimsley JK, Scholtz JM, Pace CN, Wild JR.
    Biochemistry; 1997 Nov 25; 36(47):14366-74. PubMed ID: 9398154
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  • 8. Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562.
    Garcia P, Bruix M, Rico M, Ciofi-Baffoni S, Banci L, Ramachandra Shastry MC, Roder H, de Lumley Woodyear T, Johnson CM, Fersht AR, Barker PD.
    J Mol Biol; 2005 Feb 11; 346(1):331-44. PubMed ID: 15663948
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  • 9. Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase.
    Birolo L, Malashkevich VN, Capitani G, De Luca F, Moretta A, Jansonius JN, Marino G.
    Biochemistry; 1999 Jan 19; 38(3):905-13. PubMed ID: 9893985
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  • 11. Accumulation of partly folded states in the equilibrium unfolding of ervatamin A: spectroscopic description of the native, intermediate, and unfolded states.
    Nallamsetty S, Dubey VK, Pande M, Ambasht PK, Jagannadham MV.
    Biochimie; 2007 Nov 19; 89(11):1416-24. PubMed ID: 17658212
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  • 14. A new folding intermediate of apomyoglobin from Aplysia limacina: stepwise formation of a molten globule.
    Staniforth RA, Giannini S, Bigotti MG, Cutruzzolà F, Travaglini-Allocatelli C, Brunori M.
    J Mol Biol; 2000 Apr 14; 297(5):1231-44. PubMed ID: 10764586
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  • 16. Urea-induced unfolding and conformational stability of 3-isopropylmalate dehydrogenase from the Thermophile thermus thermophilus and its mesophilic counterpart from Escherichia coli.
    Motono C, Yamagishi A, Oshima T.
    Biochemistry; 1999 Jan 26; 38(4):1332-7. PubMed ID: 9930995
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  • 17. Energetics of MazG unfolding in correlation with its structural features.
    Drobnak I, Korencic A, Loris R, Marianovsky I, Glaser G, Jamnik A, Vesnaver G, Lah J.
    J Mol Biol; 2009 Sep 11; 392(1):63-74. PubMed ID: 19523960
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  • 19. Domain folding and flexibility of Escherichia coli FtsZ determined by tryptophan site-directed mutagenesis.
    Díaz-Espinoza R, Garcés AP, Arbildua JJ, Montecinos F, Brunet JE, Lagos R, Monasterio O.
    Protein Sci; 2007 Aug 11; 16(8):1543-56. PubMed ID: 17656575
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  • 20. Structural stability and domain organization of colicin E1.
    Griko YV, Zakharov SD, Cramer WA.
    J Mol Biol; 2000 Sep 29; 302(4):941-53. PubMed ID: 10993734
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