Literature DB >> 21321551

Molecular recognition: O-GlcNAc transfer: size matters.

Laurie M Gay, Xiaowei Zheng, Daan M F van Aalten.   

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Year:  2011        PMID： 21321551      PMCID： PMC3513710          DOI： 10.1038/nchembio.529

Source DB:  PubMed          Journal:  Nat Chem Biol        ISSN： 1552-4450            Impact factor:   15.040


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  9 in total

1.  Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability.

Authors:  Won Ho Yang; Ji Eun Kim; Hyung Wook Nam; Jung Won Ju; Hoe Suk Kim; Yu Sam Kim; Jin Won Cho
Journal:  Nat Cell Biol       Date:  2006-09-10       Impact factor: 28.824

2.  A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo.

Authors:  Scott A Yuzwa; Matthew S Macauley; Julia E Heinonen; Xiaoyang Shan; Rebecca J Dennis; Yuan He; Garrett E Whitworth; Keith A Stubbs; Ernest J McEachern; Gideon J Davies; David J Vocadlo
Journal:  Nat Chem Biol       Date:  2008-06-29       Impact factor: 15.040

3.  Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.

Authors:  Sai Prasad N Iyer; Gerald W Hart
Journal:  J Biol Chem       Date:  2003-04-30       Impact factor: 5.157

4.  Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides.

Authors:  Robert J Chalkley; Agnes Thalhammer; Ralf Schoepfer; A L Burlingame
Journal:  Proc Natl Acad Sci U S A       Date:  2009-05-19       Impact factor: 11.205

5.  Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation.

Authors:  Carlos Martinez-Fleites; Matthew S Macauley; Yuan He; David L Shen; David J Vocadlo; Gideon J Davies
Journal:  Nat Struct Mol Biol       Date:  2008-06-08       Impact factor: 15.369

Review 6.  Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins.

Authors:  Gerald W Hart; Michael P Housley; Chad Slawson
Journal:  Nature       Date:  2007-04-26       Impact factor: 49.962

7.  The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha.

Authors:  Martin Jínek; Jan Rehwinkel; Brooke D Lazarus; Elisa Izaurralde; John A Hanover; Elena Conti
Journal:  Nat Struct Mol Biol       Date:  2004-09-12       Impact factor: 15.369

8.  Cell-penetrant, nanomolar O-GlcNAcase inhibitors selective against lysosomal hexosaminidases.

Authors:  Helge C Dorfmueller; Vladimir S Borodkin; Marianne Schimpl; Xiaowei Zheng; Robert Kime; Kevin D Read; Daan M F van Aalten
Journal:  Chem Biol       Date:  2010-11-24

9.  Structural insights into mechanism and specificity of O-GlcNAc transferase.

Authors:  Andrew J Clarke; Ramon Hurtado-Guerrero; Shalini Pathak; Alexander W Schüttelkopf; Vladimir Borodkin; Sharon M Shepherd; Adel F M Ibrahim; Daan M F van Aalten
Journal:  EMBO J       Date:  2008-09-25       Impact factor: 11.598
  9 in total
  1 in total

1.  The active site of O-GlcNAc transferase imposes constraints on substrate sequence.

Authors:  Shalini Pathak; Jana Alonso; Marianne Schimpl; Karim Rafie; David E Blair; Vladimir S Borodkin; Osama Albarbarawi; Daan M F van Aalten
Journal:  Nat Struct Mol Biol       Date:  2015-08-03       Impact factor: 15.369
  1 in total

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