Shin Numao
Novartis
22 Papers
141 Citations
Shin Numao is an academic researcher from Novartis. The author has contributed to research in topics: Glycosylation & N-linked glycosylation. The author has an hindex of 15, co-authored 22 publications. Previous affiliations of Shin Numao include ETH Zurich & École Polytechnique Fédérale de Lausanne.
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Papers
Definition of the bacterial N-glycosylation site consensus sequence.
Michael Kowarik,N. Martin Young,Shin Numao,Benjamin L. Schulz,Isabelle Hug,Nico Callewaert,Dominic C Mills,David C. Watson,Marcela Hernandez,John F. Kelly,Michael Wacker,Markus Aebi +11 more
TL;DR: Bacterial N‐glycosylation site selection is more specific than the eukaryotic equivalent with respect to the polypeptide acceptor sequence.
A combined method for producing homogeneous glycoproteins with eukaryotic N-glycosylation
Flavio Schwarz,Wei Huang,Cishan Li,Benjamin L. Schulz,Christian Lizak,Alessandro Palumbo,Shin Numao,Dario Neri,Markus Aebi,Lai-Xi Wang +9 more
TL;DR: A novel method for producing homogeneous eukaryotic N-glycoproteins by engineering and functional transfer of the C. jejuni glycosylation machinery in E. coli to express Glycosylated proteins with the key GlcNAc-Asn linkage is described.
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Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni.
TL;DR: In this paper, the authors used a synthetic disaccharide glycan donor (GalNAc-α1,3-bacillosamine-pyrophosphate-undecaprenyl) and a peptide acceptor substrate (KDFNVSKA) to demonstrate the ability of PglB to transfer a wide variety of saccharides.
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Insights into the Mechanism of Drosophila melanogaster Golgi α-Mannosidase II through the Structural Analysis of Covalent Reaction Intermediates
TL;DR: The structure of three different covalent glycosyl-enzyme intermediates have been determined to 1.2-Å resolution for the Golgi α-mannosidase II from Drosophila melanogaster by use of fluorinated sugar analogues, both with the wild-type enzyme and a mutant enzyme in which the acid/base catalyst has been removed.
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Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
TL;DR: Structural studies of all three inhibitors and the specific cleavage pattern of HPA make it possible to outline the simplest sequence of enzymatic reactions likely involved upon acarbose binding, and suggest that the +3 binding subsite may be sufficiently flexible to bind the alpha-(1-6) branch points in polysaccharide substrates, and therefore may play a role in allowing efficient cleavage in the direct vicinity of such junctures.
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