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185 related items for PubMed ID: 12206509

  • 1. Comparison of the average structures, from molecular dynamics, of complexes of GTPase activating protein (GAP) with oncogenic and wild-type ras-p21: identification of potential effector domains.
    Chen JM, Friedman FK, Brandt-Rauf PW, Pincus MR, Chie L.
    J Protein Chem; 2002 Jul; 21(5):349-59. PubMed ID: 12206509
    [Abstract] [Full Text] [Related]

  • 2. Inhibition of ras-induced oocyte maturation by peptides from ras-p21 and GTPase activating protein (GAP) identified as being effector domains from molecular dynamics calculations.
    Friedman FK, Chie L, Chung D, Robinson R, Brandt-Rauf P, Yamaizumi Z, Pincus MR.
    J Protein Chem; 2002 Jul; 21(5):361-6. PubMed ID: 12206510
    [Abstract] [Full Text] [Related]

  • 3. Specificity of inhibition of ras-p21 signal transduction by peptides from GTPase activating protein (GAP) and the son-of sevenless (SOS) ras-specific guanine nucleotide exchange protein.
    Chie L, Chung D, Pincus MR.
    Protein J; 2005 May; 24(4):253-8. PubMed ID: 16283548
    [Abstract] [Full Text] [Related]

  • 4. Structural effects of the binding of GTP to the wild-type and oncogenic forms of the ras-gene-encoded p21 proteins.
    Monaco R, Chen JM, Friedman FK, Brandt-Rauf P, Chung D, Pincus MR.
    J Protein Chem; 1995 Nov; 14(8):721-9. PubMed ID: 8747433
    [Abstract] [Full Text] [Related]

  • 5. Identification, using molecular dynamics, of an effector domain of the ras-binding domain of the raf-p74 protein that is uniquely involved in oncogenic ras-p21 signaling.
    Chen JM, Rijhwani K, Friedman FK, Hyde MJ, Pincus MR.
    J Protein Chem; 2000 Oct; 19(7):545-51. PubMed ID: 11233167
    [Abstract] [Full Text] [Related]

  • 6. Comparison of molecular dynamics averaged structures for complexes of normal and oncogenic ras-p21 with SOS nucleotide exchange protein, containing computed conformations for three crystallographically undefined domains, suggests a potential role of these domains in ras signaling.
    Duncan T, Chen JM, Friedman FK, Hyde M, Chie L, Pincus MR.
    Protein J; 2004 Apr; 23(3):217-28. PubMed ID: 15200053
    [Abstract] [Full Text] [Related]

  • 7. Oncogenic amino acid substitutions in the inhibitory rap-1A protein cause it to adopt a ras-p21-like conformation as computed using molecular dynamics.
    Chen JM, Brandt-Rauf PW, Pincus MR.
    J Biomol Struct Dyn; 1996 Jun; 13(6):925-33. PubMed ID: 8832375
    [Abstract] [Full Text] [Related]

  • 8. Molecular dynamics analysis of the structures of ras-guanine nucleotide exchange protein (SOS) bound to wild-type and oncogenic ras-p21. Identification of effector domains of SOS.
    Chen JM, Friedman FK, Hyde MJ, Monaco R, Pincus MR.
    J Protein Chem; 1999 Nov; 18(8):867-74. PubMed ID: 10839623
    [Abstract] [Full Text] [Related]

  • 9. Development of new anti-cancer peptides from conformational energy analysis of the oncogenic ras-p21 protein and its complexes with target proteins.
    Pincus MR.
    Front Biosci; 2004 Sep 01; 9():3486-509. PubMed ID: 15353372
    [Abstract] [Full Text] [Related]

  • 10. Revisiting the structural flexibility of the complex p21(ras)-GTP: the catalytic conformation of the molecular switch II.
    Soares TA, Miller JH, Straatsma TP.
    Proteins; 2001 Dec 01; 45(4):297-312. PubMed ID: 11746677
    [Abstract] [Full Text] [Related]

  • 11. Comparison of the computed three-dimensional structures of oncogenic forms (bound to GDP) of the ras-gene-encoded p21 protein with the structure of the normal (non-transforming) wild-type protein.
    Monaco R, Chen JM, Chung D, Brandt-Rauf P, Pincus MR.
    J Protein Chem; 1995 Aug 01; 14(6):457-66. PubMed ID: 8593186
    [Abstract] [Full Text] [Related]

  • 12. Comparison of the low energy conformations of an oncogenic and a non-oncogenic p21 protein, neither of which binds GTP or GDP.
    Liwo A, Gibson KD, Scheraga HA, Brandt-Rauf PW, Monaco R, Pincus MR.
    J Protein Chem; 1994 Feb 01; 13(2):237-51. PubMed ID: 8060496
    [Abstract] [Full Text] [Related]

  • 13. Guanine-nucleotide binding activity, interaction with GTPase-activating protein and solution conformation of the human c-Ha-Ras protein catalytic domain are retained upon deletion of C-terminal 18 amino acid residues.
    Fujita-Yoshigaki J, Ito Y, Yamasaki K, Muto Y, Miyazawa T, Nishimura S, Yokoyama S.
    J Protein Chem; 1992 Dec 01; 11(6):731-9. PubMed ID: 1466766
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