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The structure of hyperthermophilic β-N-acetylglucosaminidase reveals a novel dimer architecture associated with the active site.

Mine S, Kado Y, Watanabe M, Fukuda Y, Abe Y, Ueda T, Kawarabayasi Y, Inoue T, Ishikawa K
FEBS J 281 5092-103 (2014)
Cited: 2 times
EuropePMC logo PMID: 25227262

Articles - 3wo8 mentioned but not cited (1)

  1. The structure of hyperthermophilic β-N-acetylglucosaminidase reveals a novel dimer architecture associated with the active site. Mine S, Kado Y, Watanabe M, Fukuda Y, Abe Y, Ueda T, Kawarabayasi Y, Inoue T, Ishikawa K. FEBS J 281 5092-5103 (2014)


Articles citing this publication (1)

  1. On the phosphorylase activity of GH3 enzymes: A β-N-acetylglucosaminidase from Herbaspirillum seropedicae SmR1 and a glucosidase from Saccharopolyspora erythraea. Ducatti DR, Carroll MA, Jakeman DL. Carbohydr Res 435 106-112 (2016)


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