Backbone NMR resonance assignments for the C terminal domain of the Streptococcus mutans adhesin P1
Author:
Funder
NIH/NIDCR
NSF
NIH
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
https://link.springer.com/content/pdf/10.1007/s12104-023-10158-y.pdf
Reference16 articles.
1. Abranches J, Zeng L, Kajfasz JK et al (2018) Biology of oral streptococci. Microbiol Spectr 6:5–6
2. Barran-Berdon AL, Ocampo S, Haider M et al (2020) Enhanced purification coupled with biophysical analyses shows cross-β structure as a core building block for Streptococcus mutans functional amyloids. Sci Rep 10:1–11
3. Besingi RN, Wenderska IB, Senadheera DB et al (2017) Functional amyloids in streptococcus mutans, their use as targets of biofilm inhibition and initial characterization of SMU_63c. Microbiology (United Kingdom) 163:488–501. https://doi.org/10.1099/mic.0.000443
4. Brady LJ, Maddocks SE, Larson MR et al (2010) The changing faces of Streptococcus antigen I/II polypeptide family adhesins. Mol Microbiol 77:276–286
5. Hafsa NE, Arndt D, Wishart DS (2015) CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts. Nucleic Acids Res 43:W370–W377
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