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646 related items for PubMed ID: 20560144

  • 1. Thermodynamic and kinetic consequences of substituting glycine at different positions in a Pro-Hyp-Gly repeat collagen model peptide.
    Chen YS, Chen CC, Horng JC.
    Biopolymers; 2011; 96(1):60-8. PubMed ID: 20560144
    [Abstract] [Full Text] [Related]

  • 2. Effect of the -Gly-3(S)-hydroxyprolyl-4(R)-hydroxyprolyl- tripeptide unit on the stability of collagen model peptides.
    Mizuno K, Peyton DH, Hayashi T, Engel J, Bächinger HP.
    FEBS J; 2008 Dec; 275(23):5830-40. PubMed ID: 19021759
    [Abstract] [Full Text] [Related]

  • 3. The folding mechanism of collagen-like model peptides explored through detailed molecular simulations.
    Stultz CM.
    Protein Sci; 2006 Sep; 15(9):2166-77. PubMed ID: 16943446
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  • 4. Amino acid sequence environment modulates the disruption by osteogenesis imperfecta glycine substitutions in collagen-like peptides.
    Yang W, Battineni ML, Brodsky B.
    Biochemistry; 1997 Jun 10; 36(23):6930-5. PubMed ID: 9188687
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  • 5. Triple-helix propensity of hydroxyproline and fluoroproline: comparison of host-guest and repeating tripeptide collagen models.
    Persikov AV, Ramshaw JA, Kirkpatrick A, Brodsky B.
    J Am Chem Soc; 2003 Sep 24; 125(38):11500-1. PubMed ID: 13129344
    [Abstract] [Full Text] [Related]

  • 6. Stabilization of triple-helical structures of collagen peptides containing a Hyp-Thr-Gly, Hyp-Val-Gly, or Hyp-Ser-Gly sequence.
    Okuyama K, Miyama K, Morimoto T, Masakiyo K, Mizuno K, Bächinger HP.
    Biopolymers; 2011 Sep 24; 95(9):628-40. PubMed ID: 21442606
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  • 11. Stability related bias in residues replacing glycines within the collagen triple helix (Gly-Xaa-Yaa) in inherited connective tissue disorders.
    Persikov AV, Pillitteri RJ, Amin P, Schwarze U, Byers PH, Brodsky B.
    Hum Mutat; 2004 Oct 24; 24(4):330-7. PubMed ID: 15365990
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  • 12. Conformational effects of Gly-X-Gly interruptions in the collagen triple helix.
    Bella J, Liu J, Kramer R, Brodsky B, Berman HM.
    J Mol Biol; 2006 Sep 15; 362(2):298-311. PubMed ID: 16919298
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  • 13. Stability junction at a common mutation site in the collagenous domain of the mannose binding lectin.
    Mohs A, Li Y, Doss-Pepe E, Baum J, Brodsky B.
    Biochemistry; 2005 Feb 15; 44(6):1793-9. PubMed ID: 15697204
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  • 14. NMR and CD spectroscopy show that imino acid restriction of the unfolded state leads to efficient folding.
    Xu Y, Hyde T, Wang X, Bhate M, Brodsky B, Baum J.
    Biochemistry; 2003 Jul 29; 42(29):8696-703. PubMed ID: 12873129
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  • 15. Collagen-like triple helix formation of synthetic (Pro-Pro-Gly)10 analogues: (4(S)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly)10, (4(R)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly)10 and (4(S)-fluoroprolyl-4(R)-fluoroprolyl-Gly)10.
    Doi M, Nishi Y, Uchiyama S, Nishiuchi Y, Nishio H, Nakazawa T, Ohkubo T, Kobayashi Y.
    J Pept Sci; 2005 Oct 29; 11(10):609-16. PubMed ID: 15880478
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  • 16. Severity of osteogenesis imperfecta and structure of a collagen-like peptide modeling a lethal mutation site.
    Radmer RJ, Klein TE.
    Biochemistry; 2004 May 11; 43(18):5314-23. PubMed ID: 15122897
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  • 17. Collagen model peptides: Sequence dependence of triple-helix stability.
    Persikov AV, Ramshaw JA, Brodsky B.
    Biopolymers; 2000 May 11; 55(6):436-50. PubMed ID: 11304671
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  • 19. Folding and conformational consequences of glycine to alanine replacements at different positions in a collagen model peptide.
    Bhate M, Wang X, Baum J, Brodsky B.
    Biochemistry; 2002 May 21; 41(20):6539-47. PubMed ID: 12009919
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  • 20. A host-guest set of triple-helical peptides: stability of Gly-X-Y triplets containing common nonpolar residues.
    Shah NK, Ramshaw JA, Kirkpatrick A, Shah C, Brodsky B.
    Biochemistry; 1996 Aug 13; 35(32):10262-8. PubMed ID: 8756681
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