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161 related items for PubMed ID: 21454493
1. 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]
2. 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 20; 19(4):775-85. PubMed ID: 20162611 [Abstract] [Full Text] [Related]
3. 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 [Abstract] [Full Text] [Related]
4. 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 [Abstract] [Full Text] [Related]
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 Jan 21; 5(6):378-85. PubMed ID: 25482084 [Abstract] [Full Text] [Related]
6. Mechanism of stabilization of a bacterial collagen triple helix in the absence of hydroxyproline. Mohs A, Silva T, Yoshida T, Amin R, Lukomski S, Inouye M, Brodsky B. J Biol Chem; 2007 Oct 12; 282(41):29757-65. PubMed ID: 17693404 [Abstract] [Full Text] [Related]
7. 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 12; 18(6):1241-51. PubMed ID: 19472339 [Abstract] [Full Text] [Related]
8. 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]
9. 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 [Abstract] [Full Text] [Related]
10. An engineered alpha1 integrin-binding collagenous sequence. Seo N, Russell BH, Rivera JJ, Liang X, Xu X, Afshar-Kharghan V, Höök M. J Biol Chem; 2010 Oct 01; 285(40):31046-54. PubMed ID: 20675378 [Abstract] [Full Text] [Related]
11. 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 01; 69(Pt 9):1023-5. PubMed ID: 23989154 [Abstract] [Full Text] [Related]
12. 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 01; 61(2):351-67. PubMed ID: 16856940 [Abstract] [Full Text] [Related]
14. 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]
15. 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 [Abstract] [Full Text] [Related]
16. 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 [Abstract] [Full Text] [Related]
17. Folding of collagen IV. Dölz R, Engel J, Kühn K. Eur J Biochem; 1988 Dec 15; 178(2):357-66. PubMed ID: 2850175 [Abstract] [Full Text] [Related]
18. 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 [Abstract] [Full Text] [Related]
19. Alpha-helical coiled-coil oligomerization domains are almost ubiquitous in the collagen superfamily. McAlinden A, Smith TA, Sandell LJ, Ficheux D, Parry DA, Hulmes DJ. J Biol Chem; 2003 Oct 24; 278(43):42200-7. PubMed ID: 12920133 [Abstract] [Full Text] [Related]