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10.1038/nchembio.2358

http://scihub22266oqcxt.onion/10.1038/nchembio.2358
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C5438047!5438047!28346405
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suck abstract from ncbi


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pmid28346405      Nat+Chem+Biol 2017 ; 13 (6): 610-2
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  • Structural and functional insight into human O-GlcNAcase #MMPMID28346405
  • Roth C; Chan S; Offen WA; Hemsworth GR; Willems LI; King DT; Varghese V; Britton R; Vocadlo DJ; Davies GJ
  • Nat Chem Biol 2017[Jun]; 13 (6): 610-2 PMID28346405show ga
  • O-GlcNAc hydrolase, OGA, removes O-linked N-acetylglucosamine (O-GlcNAc) from myriad nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments we determined the 3-D structure of human OGA, revealing an unusual helix exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors having clinical value.
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