These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

187 related articles for article (PubMed ID: 11797014)

  • 1. Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability.
    Jaswal SS; Sohl JL; Davis JH; Agard DA
    Nature; 2002 Jan; 415(6869):343-6. PubMed ID: 11797014
    [TBL] [Abstract][Full Text] [Related]  

  • 2. The folding landscape of an alpha-lytic protease variant reveals the role of a conserved beta-hairpin in the development of kinetic stability.
    Truhlar SM; Agard DA
    Proteins; 2005 Oct; 61(1):105-14. PubMed ID: 16044461
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Interdependent folding of the N- and C-terminal domains defines the cooperative folding of alpha-lytic protease.
    Cunningham EL; Agard DA
    Biochemistry; 2003 Nov; 42(45):13212-9. PubMed ID: 14609332
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Unfolded conformations of alpha-lytic protease are more stable than its native state.
    Sohl JL; Jaswal SS; Agard DA
    Nature; 1998 Oct; 395(6704):817-9. PubMed ID: 9796818
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases.
    Jaswal SS; Truhlar SM; Dill KA; Agard DA
    J Mol Biol; 2005 Mar; 347(2):355-66. PubMed ID: 15740746
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Two energetically disparate folding pathways of alpha-lytic protease share a single transition state.
    Derman AI; Agard DA
    Nat Struct Biol; 2000 May; 7(5):394-7. PubMed ID: 10802737
    [TBL] [Abstract][Full Text] [Related]  

  • 7. The folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stability.
    Truhlar SM; Cunningham EL; Agard DA
    Protein Sci; 2004 Feb; 13(2):381-90. PubMed ID: 14718653
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Structure of alpha-lytic protease complexed with its pro region.
    Sauter NK; Mau T; Rader SD; Agard DA
    Nat Struct Biol; 1998 Nov; 5(11):945-50. PubMed ID: 9808037
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Disabling the folding catalyst is the last critical step in alpha-lytic protease folding.
    Cunningham EL; Agard DA
    Protein Sci; 2004 Feb; 13(2):325-31. PubMed ID: 14739318
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Structural and mechanistic exploration of acid resistance: kinetic stability facilitates evolution of extremophilic behavior.
    Kelch BA; Eagen KP; Erciyas FP; Humphris EL; Thomason AR; Mitsuiki S; Agard DA
    J Mol Biol; 2007 May; 368(3):870-83. PubMed ID: 17382344
    [TBL] [Abstract][Full Text] [Related]  

  • 11. On the unfolding of alpha-lytic protease and the role of the pro region.
    Inuzuka Y; Lazaridis T
    Proteins; 2000 Oct; 41(1):21-32. PubMed ID: 10944390
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Kinetic stability as a mechanism for protease longevity.
    Cunningham EL; Jaswal SS; Sohl JL; Agard DA
    Proc Natl Acad Sci U S A; 1999 Sep; 96(20):11008-14. PubMed ID: 10500115
    [TBL] [Abstract][Full Text] [Related]  

  • 13. alpha-lytic protease precursor: characterization of a structured folding intermediate.
    Anderson DE; Peters RJ; Wilk B; Agard DA
    Biochemistry; 1999 Apr; 38(15):4728-35. PubMed ID: 10200160
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Positive selection dictates the choice between kinetic and thermodynamic protein folding and stability in subtilases.
    Subbian E; Yabuta Y; Shinde U
    Biochemistry; 2004 Nov; 43(45):14348-60. PubMed ID: 15533039
    [TBL] [Abstract][Full Text] [Related]  

  • 15. The pro region N-terminal domain provides specific interactions required for catalysis of alpha-lytic protease folding.
    Cunningham EL; Mau T; Truhlar SM; Agard DA
    Biochemistry; 2002 Jul; 41(28):8860-7. PubMed ID: 12102628
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Exploring the Evolutionary History of Kinetic Stability in the α-Lytic Protease Family.
    Nixon CF; Lim SA; Sailer ZR; Zheludev IN; Gee CL; Kelch BA; Harms MJ; Marqusee S
    Biochemistry; 2021 Jan; 60(3):170-181. PubMed ID: 33433210
    [TBL] [Abstract][Full Text] [Related]  

  • 17. The prosegment catalyzes pepsin folding to a kinetically trapped native state.
    Dee DR; Yada RY
    Biochemistry; 2010 Jan; 49(2):365-71. PubMed ID: 20000477
    [TBL] [Abstract][Full Text] [Related]  

  • 18. The 0.83 A resolution crystal structure of alpha-lytic protease reveals the detailed structure of the active site and identifies a source of conformational strain.
    Fuhrmann CN; Kelch BA; Ota N; Agard DA
    J Mol Biol; 2004 May; 338(5):999-1013. PubMed ID: 15111063
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Pro region C-terminus:protease active site interactions are critical in catalyzing the folding of alpha-lytic protease.
    Peters RJ; Shiau AK; Sohl JL; Anderson DE; Tang G; Silen JL; Agard DA
    Biochemistry; 1998 Sep; 37(35):12058-67. PubMed ID: 9724517
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Unfolding simulations reveal the mechanism of extreme unfolding cooperativity in the kinetically stable alpha-lytic protease.
    Salimi NL; Ho B; Agard DA
    PLoS Comput Biol; 2010 Feb; 6(2):e1000689. PubMed ID: 20195497
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 10.