Found: 9
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Tetracycline‐modifying enzyme SmTetX from Stenotrophomonas maltophilia.
- Published in:
- Acta Crystallographica: Section F, Structural Biology Communications, 2023, v. 79, n. 7, p. 180, doi. 10.1107/S2053230X23005381
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- Article
A highly active S1‐P1 nuclease from the opportunistic pathogen Stenotrophomonas maltophilia cleaves c‐di‐GMP.
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- FEBS Letters, 2023, v. 597, n. 16, p. 2103, doi. 10.1002/1873-3468.14683
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- Article
Trp–His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer.
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- Scientific Reports, 2019, v. 9, n. 1, p. N.PAG, doi. 10.1038/s41598-019-50105-3
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- Article
Crystallographic fragment screening‐based study of a novel FAD‐dependent oxidoreductase from Chaetomium thermophilum. Corrigendum.
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- Acta Crystallographica: Section D, Structural Biology, 2021, v. 77, n. 7, p. 980, doi. 10.1107/S2059798321006100
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- Article
Crystallographic fragment screening‐based study of a novel FAD‐dependent oxidoreductase from Chaetomium thermophilum.
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- Acta Crystallographica: Section D, Structural Biology, 2021, v. 77, n. 6, p. 755, doi. 10.1107/S2059798321003533
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- Article
Structural and Catalytic Properties of S1 Nuclease from Aspergillus oryzae Responsible for Substrate Recognition, Cleavage, Non–Specificity, and Inhibition.
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- PLoS ONE, 2016, v. 11, n. 12, p. 1, doi. 10.1371/journal.pone.0168832
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- Article
Domain structure of HelD, an interaction partner of Bacillus subtilis RNA polymerase.
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- FEBS Letters, 2019, v. 593, n. 9, p. 996, doi. 10.1002/1873-3468.13385
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- Article
Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase.
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- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-20158-4
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- Article
Comparison of enzymatic activities and proteomic profiles of Butyrivibrio fibrisolvens grown on different carbon sources.
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- Proteome Science, 2019, v. 17, n. 1, p. N.PAG, doi. 10.1186/s12953-019-0150-3
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- Article