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161 related items for PubMed ID: 21454494

  • 1. Dissecting a bacterial collagen domain from Streptococcus pyogenes: sequence and length-dependent variations in triple helix stability and folding.
    Yu Z, Brodsky B, Inouye M.
    J Biol Chem; 2011 May 27; 286(21):18960-8. PubMed ID: 21454494
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  • 2. Location of glycine mutations within a bacterial collagen protein affects degree of disruption of triple-helix folding and conformation.
    Cheng H, Rashid S, Yu Z, Yoshizumi A, Hwang E, Brodsky B.
    J Biol Chem; 2011 Jan 21; 286(3):2041-6. PubMed ID: 21071452
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  • 4. Noncollagenous region of the streptococcal collagen-like protein is a trimerization domain that supports refolding of adjacent homologous and heterologous collagenous domains.
    Yu Z, Mirochnitchenko O, Xu C, Yoshizumi A, Brodsky B, Inouye M.
    Protein Sci; 2010 Apr 21; 19(4):775-85. PubMed ID: 20162611
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  • 5. Preparation and characterization of monomers to tetramers of a collagen-like domain from Streptococcus pyogenes.
    Peng YY, Stoichevska V, Howell L, Madsen S, Werkmeister JA, Dumsday GJ, Ramshaw JA.
    Bioengineered; 2014 Apr 21; 5(6):378-85. PubMed ID: 25482084
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  • 10. Bacterial collagen-like proteins that form triple-helical structures.
    Yu Z, An B, Ramshaw JA, Brodsky B.
    J Struct Biol; 2014 Jun 21; 186(3):451-61. PubMed ID: 24434612
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  • 12. The crucial role of trimerization domains in collagen folding.
    Boudko SP, Engel J, Bächinger HP.
    Int J Biochem Cell Biol; 2012 Jan 21; 44(1):21-32. PubMed ID: 22001560
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  • 14. Vascular Ehlers-Danlos syndrome mutations in type III collagen differently stall the triple helical folding.
    Mizuno K, Boudko S, Engel J, Bächinger HP.
    J Biol Chem; 2013 Jun 28; 288(26):19166-76. PubMed ID: 23645670
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  • 16. The influence of specific binding of collagen-silk chimeras to silk biomaterials on hMSC behavior.
    An B, DesRochers TM, Qin G, Xia X, Thiagarajan G, Brodsky B, Kaplan DL.
    Biomaterials; 2013 Jan 28; 34(2):402-12. PubMed ID: 23088839
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  • 17. Crystallization and preliminary X-ray crystallographic analysis of the variable domain of Scl2.3, a streptococcal collagen-like protein from invasive M3-type Streptococcus pyogenes.
    Squeglia F, Bachert B, Romano M, Lukomski S, Berisio R.
    Acta Crystallogr Sect F Struct Biol Cryst Commun; 2013 Sep 28; 69(Pt 9):1023-5. PubMed ID: 23989154
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  • 18. Folding delay and structural perturbations caused by type IV collagen natural interruptions and nearby Gly missense mutations.
    Hwang ES, Brodsky B.
    J Biol Chem; 2012 Feb 03; 287(6):4368-75. PubMed ID: 22179614
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  • 19. Transformation of the mechanism of triple-helix peptide folding in the absence of a C-terminal nucleation domain and its implications for mutations in collagen disorders.
    Buevich AV, Silva T, Brodsky B, Baum J.
    J Biol Chem; 2004 Nov 05; 279(45):46890-5. PubMed ID: 15299012
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  • 20. The peptides acetyl-(Gly-3(S)Hyp-4(R)Hyp)10-NH2 and acetyl-(Gly-Pro-3(S)Hyp)10-NH2 do not form a collagen triple helix.
    Mizuno K, Hayashi T, Peyton DH, Bachinger HP.
    J Biol Chem; 2004 Jan 02; 279(1):282-7. PubMed ID: 14576161
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