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Accelerating the Association of the Most Stable Protein-Ligand Complex by More than Two Orders of Magnitude.
- Published in:
- Angewandte Chemie, 2016, v. 128, n. 32, p. 9496, doi. 10.1002/ange.201603652
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Acceleration of protein folding by four orders of magnitude through a single amino acid substitution.
- Published in:
- Scientific Reports, 2015, p. 11840, doi. 10.1038/srep11840
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Accelerating the Association of the Most Stable Protein-Ligand Complex by More than Two Orders of Magnitude.
- Published in:
- Angewandte Chemie International Edition, 2016, v. 55, n. 32, p. 9350, doi. 10.1002/anie.201603652
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- Article
Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
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- Scientific Reports, 2017, p. 43588, doi. 10.1038/srep43588
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- Article
Stochastic chain termination in bacterial pilus assembly.
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- Nature Communications, 2023, v. 14, n. 1, p. 1, doi. 10.1038/s41467-023-43449-y
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(4 R)- and (4 S)-Fluoroproline in the Conserved cis-Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering.
- Published in:
- ChemBioChem, 2013, v. 14, n. 9, p. 1053, doi. 10.1002/cbic.201300178
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- Article
Inside Cover: (4 R)- and (4 S)-Fluoroproline in the Conserved cis-Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering (ChemBioChem 9/2013).
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- ChemBioChem, 2013, v. 14, n. 9, p. 1018, doi. 10.1002/cbic.201390030
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Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy
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- FEBS Letters, 2011, v. 585, n. 1, p. 111, doi. 10.1016/j.febslet.2010.11.013
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Quality control of disulfide bond formation in pilus subunits by the chaperone FimC.
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- Nature Chemical Biology, 2012, v. 8, n. 8, p. 707, doi. 10.1038/nchembio.1019
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