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Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide.
- Published in:
- Acta Crystallographica: Section F, Structural Biology Communications, 2015, v. 71, n. 3, p. 295, doi. 10.1107/S2053230X15001065
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- Article
The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.
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- FEBS Journal, 2017, v. 284, n. 24, p. 4343, doi. 10.1111/febs.14310
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- Article
Cwp2 from Clostridium difficile exhibits an extended three domain fold and cell adhesion in vitro.
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- FEBS Journal, 2017, v. 284, n. 17, p. 2886, doi. 10.1111/febs.14157
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- Article
Molecular features of the sortase enzyme family.
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- FEBS Journal, 2015, v. 282, n. 11, p. 2097, doi. 10.1111/febs.13288
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- Article
Structure and function of a Clostridium difficile sortase enzyme.
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- Scientific Reports, 2015, p. 9449, doi. 10.1038/srep09449
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- Article
A Novel, Orally Delivered Antibody Therapy and Its Potential to Prevent Clostridioides difficile Infection in Pre-clinical Models.
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- Frontiers in Microbiology, 2020, v. 11, p. N.PAG, doi. 10.3389/fmicb.2020.578903
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- Article