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Journal Abstract Search

207 related items for PubMed ID: 20162611

  • 1. 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; 19(4):775-85. PubMed ID: 20162611
    [Abstract] [Full Text] [Related]

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  • 3. Designed coiled coils promote folding of a recombinant bacterial collagen.
    Yoshizumi A, Fletcher JM, Yu Z, Persikov AV, Bartlett GJ, Boyle AL, Vincent TL, Woolfson DN, Brodsky B.
    J Biol Chem; 2011 May 20; 286(20):17512-20. PubMed ID: 21454493
    [Abstract] [Full Text] [Related]

  • 4. 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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  • 5. 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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  • 6. Expanding the family of collagen proteins: recombinant bacterial collagens of varying composition form triple-helices of similar stability.
    Xu C, Yu Z, Inouye M, Brodsky B, Mirochnitchenko O.
    Biomacromolecules; 2010 Feb 08; 11(2):348-56. PubMed ID: 20025291
    [Abstract] [Full Text] [Related]

  • 7. The crucial role of trimerization domains in collagen folding.
    Boudko SP, Engel J, Bächinger HP.
    Int J Biochem Cell Biol; 2012 Jan 08; 44(1):21-32. PubMed ID: 22001560
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  • 8. 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 Jan 08; 5(6):378-85. PubMed ID: 25482084
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  • 9. Self-association of streptococcus pyogenes collagen-like constructs into higher order structures.
    Yoshizumi A, Yu Z, Silva T, Thiagarajan G, Ramshaw JA, Inouye M, Brodsky B.
    Protein Sci; 2009 Jun 08; 18(6):1241-51. PubMed ID: 19472339
    [Abstract] [Full Text] [Related]

  • 10. The crystal structure of the streptococcal collagen-like protein 2 globular domain from invasive M3-type group A Streptococcus shows significant similarity to immunomodulatory HIV protein gp41.
    Squeglia F, Bachert B, De Simone A, Lukomski S, Berisio R.
    J Biol Chem; 2014 Feb 21; 289(8):5122-33. PubMed ID: 24356966
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  • 11. Binding of the low-density lipoprotein by streptococcal collagen-like protein Scl1 of Streptococcus pyogenes.
    Han R, Caswell CC, Lukomska E, Keene DR, Pawlowski M, Bujnicki JM, Kim JK, Lukomski S.
    Mol Microbiol; 2006 Jul 21; 61(2):351-67. PubMed ID: 16856940
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  • 12. A streptococcal collagen-like protein interacts with the alpha2beta1 integrin and induces intracellular signaling.
    Humtsoe JO, Kim JK, Xu Y, Keene DR, Höök M, Lukomski S, Wary KK.
    J Biol Chem; 2005 Apr 08; 280(14):13848-57. PubMed ID: 15647274
    [Abstract] [Full Text] [Related]

  • 13. Bacterial collagen-like proteins that form triple-helical structures.
    Yu Z, An B, Ramshaw JA, Brodsky B.
    J Struct Biol; 2014 Jun 08; 186(3):451-61. PubMed ID: 24434612
    [Abstract] [Full Text] [Related]

  • 14. 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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  • 16. Streptococcal Scl1 and Scl2 proteins form collagen-like triple helices.
    Xu Y, Keene DR, Bujnicki JM, Höök M, Lukomski S.
    J Biol Chem; 2002 Jul 26; 277(30):27312-8. PubMed ID: 11976327
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  • 17. Folding of collagen IV.
    Dölz R, Engel J, Kühn K.
    Eur J Biochem; 1988 Dec 15; 178(2):357-66. PubMed ID: 2850175
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  • 18. Collagen triple helix formation can be nucleated at either end.
    Frank S, Boudko S, Mizuno K, Schulthess T, Engel J, Bächinger HP.
    J Biol Chem; 2003 Mar 07; 278(10):7747-50. PubMed ID: 12540847
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  • 19. Surface-exposed loops and an acidic patch in the Scl1 protein of group A Streptococcus enable Scl1 binding to wound-associated fibronectin.
    McNitt DH, Choi SJ, Keene DR, Van De Water L, Squeglia F, Berisio R, Lukomski S.
    J Biol Chem; 2018 May 18; 293(20):7796-7810. PubMed ID: 29615492
    [Abstract] [Full Text] [Related]

  • 20. Trimerization of the amino propeptide of type IIA procollagen using a 14-amino acid sequence derived from the coiled-coil neck domain of surfactant protein D.
    McAlinden A, Crouch EC, Bann JG, Zhang P, Sandell LJ.
    J Biol Chem; 2002 Oct 25; 277(43):41274-81. PubMed ID: 12194968
    [Abstract] [Full Text] [Related]

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