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Biophysical and biochemical nature of amorphous protein oligomers determines the strength of immune response and the generation of T‐cell memory.
- Published in:
- FEBS Journal, 2023, v. 290, n. 19, p. 4712, doi. 10.1111/febs.16884
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- Article
Blocking PSD95‐PDZ3's amyloidogenesis through point mutations that inhibit high‐temperature reversible oligomerization (RO).
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- FEBS Journal, 2022, v. 289, n. 11, p. 3205, doi. 10.1111/febs.16339
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- Article
Non-Glycosylated SARS-CoV-2 Omicron BA.5 Receptor Binding Domain (RBD) with a Native-like Conformation Induces a Robust Immune Response with Potent Neutralization in a Mouse Model.
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- Molecules, 2024, v. 29, n. 11, p. 2676, doi. 10.3390/molecules29112676
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- Article
E. coli production of a multi-disulfide bonded SARS-CoV-2 Omicron BA.5 RBD exhibiting native-like biochemical and biophysical properties.
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- Biophysics & Physicobiology, 2023, v. 20, n. 4, p. 1, doi. 10.2142/biophysico.bppb-v20.0036
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Antisera Produced Using an E. coli -Expressed SARS-CoV-2 RBD and Complemented with a Minimal Dose of Mammalian-Cell-Expressed S1 Subunit of the Spike Protein Exhibits Improved Neutralization.
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- International Journal of Molecular Sciences, 2023, v. 24, n. 13, p. 10583, doi. 10.3390/ijms241310583
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- Article
The Immunogenicity of DENV1–4 ED3s Strongly Differ despite Their Almost Identical Three-Dimensional Structures and High Sequence Similarities.
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- International Journal of Molecular Sciences, 2023, v. 24, n. 3, p. 2393, doi. 10.3390/ijms24032393
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- Article
An Escherichia coli Expressed Multi-Disulfide Bonded SARS-CoV-2 RBD Shows Native-like Biophysical Properties and Elicits Neutralizing Antisera in a Mouse Model.
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- International Journal of Molecular Sciences, 2022, v. 23, n. 24, p. 15744, doi. 10.3390/ijms232415744
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- Article
A Multi-Disulfide Receptor-Binding Domain (RBD) of the SARS-CoV-2 Spike Protein Expressed in E. coli Using a SEP-Tag Produces Antisera Interacting with the Mammalian Cell Expressed Spike (S1) Protein.
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- International Journal of Molecular Sciences, 2022, v. 23, n. 3, p. 1703, doi. 10.3390/ijms23031703
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- Article