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Corrigendum: Evidence for a Boat Conformation at the Transition State of GH76 α-1,6-Mannanases-Key Enzymes in Bacterial and Fungal Mannoprotein Metabolism.
- Published in:
- Angewandte Chemie International Edition, 2016, v. 55, n. 6, p. 1949, doi. 10.1002/anie.201511540
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Evidence for a Boat Conformation at the Transition State of GH76 α-1,6-Mannanases-Key Enzymes in Bacterial and Fungal Mannoprotein Metabolism.
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- Angewandte Chemie International Edition, 2015, v. 54, n. 18, p. 5378, doi. 10.1002/anie.201410502
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- Article
Berichtigung: Evidence for a Boat Conformation at the Transition State of GH76 α-1,6-Mannanases-Key Enzymes in Bacterial and Fungal Mannoprotein Metabolism.
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- Angewandte Chemie, 2016, v. 128, n. 6, p. 1985, doi. 10.1002/ange.201511540
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- Publication type:
- Article
Evidence for a Boat Conformation at the Transition State of GH76 α-1,6-Mannanases-Key Enzymes in Bacterial and Fungal Mannoprotein Metabolism.
- Published in:
- Angewandte Chemie, 2015, v. 127, n. 18, p. 5468, doi. 10.1002/ange.201410502
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- Article
Spiro‐epoxyglycosides as Activity‐Based Probes for Glycoside Hydrolase Family 99 Endomannosidase/Endomannanase.
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- Chemistry - A European Journal, 2018, v. 24, n. 39, p. 9983, doi. 10.1002/chem.201801902
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- Article
Glycoprotein misfolding in the endoplasmic reticulum: identification of released oligosaccharides reveals a second ER-associated degradation pathway for Golgi-retrieved proteins.
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- Cellular & Molecular Life Sciences, 2013, v. 70, n. 15, p. 2799, doi. 10.1007/s00018-013-1304-6
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- Article
Corrigendum: Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism.
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- Nature, 2015, v. 520, n. 7547, p. 388, doi. 10.1038/nature14334
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- Article
Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism.
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- Nature, 2015, v. 517, n. 7533, p. 165, doi. 10.1038/nature13995
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- Article
Structural and Kinetic Dissection of the endo-α-1,2-Mannanase Activity of Bacterial GH99 Glycoside Hydrolases from Bacteroides spp.
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- Chemistry - A European Journal, 2015, v. 21, n. 5, p. 1966, doi. 10.1002/chem.201405539
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- Article