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Folding of the Ig-Like Domain of the Dengue Virus Envelope Protein Analyzed by High-Hydrostatic-Pressure NMR at a Residue-Level Resolution.
- Published in:
- Biomolecules (2218-273X), 2019, v. 9, n. 8, p. 309, doi. 10.3390/biom9080309
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- Article
Misfolding of a Single Disulfide Bonded Globular Protein into a Low-Solubility Species Conformationally and Biophysically Distinct from the Native One.
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- Biomolecules (2218-273X), 2019, v. 9, n. 6, p. 250, doi. 10.3390/biom9060250
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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
Reverse Engineering Analysis of the High-Temperature Reversible Oligomerization and Amyloidogenicity of PSD95-PDZ3.
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- Molecules, 2022, v. 27, n. 9, p. 2813, doi. 10.3390/molecules27092813
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- Article
Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR.
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- Scientific Reports, 2020, v. 10, n. 1, p. N.PAG, doi. 10.1038/s41598-020-76486-4
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- Article
Design and Escherichia coli Expression of a Natively Folded Multi-Disulfide Bonded Influenza H1N1-PR8 Receptor-Binding Domain (RBD).
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- International Journal of Molecular Sciences, 2024, v. 25, n. 7, p. 3943, doi. 10.3390/ijms25073943
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- Article
Direct Analysis of Mitochondrial Damage Caused by Misfolded/Destabilized Proteins.
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- International Journal of Molecular Sciences, 2022, v. 23, n. 17, p. 9881, doi. 10.3390/ijms23179881
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- Article