Backbone NMR resonance assignments for the VP1u N-terminal receptor-binding domain of the human parvovirus pathogen B19
Author:
Funder
National Science Foundation Cooperative Agreement and the State of Florida
NIH
Publisher
Springer Science and Business Media LLC
Link
https://link.springer.com/content/pdf/10.1007/s12104-024-10181-7.pdf
Reference17 articles.
1. Bircher C, Bieri J, Assaraf R, Leisi R, Ros C (2022) A conserved receptor-binding domain in the VP1u of Primate Erythroparvoviruses determines the marked tropism for erythroid cells. Viruses 14(2):420. https://doi.org/10.3390/v14020420
2. Deiss V, Tratschin JD, Weitz M, Siegl G (1990) Cloning of the Human Parvovirus B19 Genome and Structural Analysis of its palindromic termini. Virology 175(1):247–254. https://doi.org/10.1016/0042-6822(90)90205-6
3. 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(W1):W370–377. https://doi.org/10.1093/nar/gkv494
4. Heegaard ED, Kevin E, Brown (2002) Human Parvovirus B19. Clin Microbiol Rev 15(3):485–505. https://doi.org/10.1128/CMR.15.3.485-505.2002
5. Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O, Tunyasuvunakool K et al (2021) Highly Accurate protein structure prediction with AlphaFold. Nature 596(7873):583–589. https://doi.org/10.1038/s41586-021-03819-2
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