Literature DB >> 25411699

Proteomic approaches for site-specific O-GlcNAcylation analysis.

Sheng Wang1, Feng Yang, David G Camp, Karin Rodland, Wei-Jun Qian, Tao Liu, Richard D Smith.   

Abstract

O-GlcNAcylation is a dynamic protein post-translational modification of serine or threonine residues by an O-linked monosaccharide N-acetylglucosamine (O-GlcNAc). O-GlcNAcylation was discovered three decades ago and its significance has been implicated in several disease states, such as metabolic diseases, cancer and neurological diseases. Yet it remains technically challenging to characterize comprehensively and quantitatively because of its low abundance, low stoichiometry and extremely labile nature under conventional collision-induced dissociation tandem MS conditions. Herein, we review the recent advances addressing these challenges in developing proteomic approaches for site-specific O-GlcNAcylation analysis, including specific enrichment of O-GlcNAc peptides/proteins, unambiguous site-determination of O-GlcNAc modification and quantitative analysis of O-GlcNAcylation.

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Year:  2014        PMID： 25411699      PMCID： PMC4275047          DOI： 10.4155/bio.14.239

Source DB:  PubMed          Journal:  Bioanalysis        ISSN： 1757-6180            Impact factor:   2.681


  85 in total

Review 1.  Vertebrate protein glycosylation: diversity, synthesis and function.

Authors:  Kelley W Moremen; Michael Tiemeyer; Alison V Nairn
Journal:  Nat Rev Mol Cell Biol       Date:  2012-06-22       Impact factor: 94.444

2.  O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry.

Authors:  Keith Vosseller; Jonathan C Trinidad; Robert J Chalkley; Christian G Specht; Agnes Thalhammer; Aenoch J Lynn; June O Snedecor; Shenheng Guan; Katalin F Medzihradszky; David A Maltby; Ralf Schoepfer; Alma L Burlingame
Journal:  Mol Cell Proteomics       Date:  2006-02-01       Impact factor: 5.911

3.  Supplemental activation method for high-efficiency electron-transfer dissociation of doubly protonated peptide precursors.

Authors:  Danielle L Swaney; Graeme C McAlister; Matthew Wirtala; Jae C Schwartz; John E P Syka; Joshua J Coon
Journal:  Anal Chem       Date:  2007-01-15       Impact factor: 6.986

4.  Comparative analysis of cleavable azobenzene-based affinity tags for bioorthogonal chemical proteomics.

Authors:  Yu-Ying Yang; Markus Grammel; Anuradha S Raghavan; Guillaume Charron; Howard C Hang
Journal:  Chem Biol       Date:  2010-11-24

5.  Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code.

Authors:  Kaoru Sakabe; Zihao Wang; Gerald W Hart
Journal:  Proc Natl Acad Sci U S A       Date:  2010-11-02       Impact factor: 11.205

6.  GlcNAcylation plays an essential role in breast cancer metastasis.

Authors:  Yuchao Gu; Wenyi Mi; Yuqing Ge; Haiyan Liu; Qiong Fan; Cuifang Han; Jing Yang; Feng Han; Xinzhi Lu; Wengong Yu
Journal:  Cancer Res       Date:  2010-07-07       Impact factor: 12.701

7.  Enrichment and site mapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry.

Authors:  Zihao Wang; Namrata D Udeshi; Meaghan O'Malley; Jeffrey Shabanowitz; Donald F Hunt; Gerald W Hart
Journal:  Mol Cell Proteomics       Date:  2009-08-19       Impact factor: 5.911

8.  Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.

Authors:  Wagner B Dias; Win D Cheung; Zihao Wang; Gerald W Hart
Journal:  J Biol Chem       Date:  2009-06-08       Impact factor: 5.157

9.  Effect of chemical modifications on peptide fragmentation behavior upon electron transfer induced dissociation.

Authors:  Marco L Hennrich; Paul J Boersema; Henk van den Toorn; Nikolai Mischerikow; Albert J R Heck; Shabaz Mohammed
Journal:  Anal Chem       Date:  2009-09-15       Impact factor: 6.986

10.  Neutron-encoded mass signatures for multiplexed proteome quantification.

Authors:  Alexander S Hebert; Anna E Merrill; Derek J Bailey; Amelia J Still; Michael S Westphall; Eric R Strieter; David J Pagliarini; Joshua J Coon
Journal:  Nat Methods       Date:  2013-02-24       Impact factor: 28.547
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  5 in total

1.  Quantitative proteomics identifies altered O-GlcNAcylation of structural, synaptic and memory-associated proteins in Alzheimer's disease.

Authors:  Sheng Wang; Feng Yang; Vladislav A Petyuk; Anil K Shukla; Matthew E Monroe; Marina A Gritsenko; Karin D Rodland; Richard D Smith; Wei-Jun Qian; Cheng-Xin Gong; Tao Liu
Journal:  J Pathol       Date:  2017-07-28       Impact factor: 7.996

Review 2.  Post-translational modifications in tumor-associated carbonic anhydrases.

Authors:  Anna Di Fiore; Claudiu T Supuran; Andrea Scaloni; Giuseppina De Simone
Journal:  Amino Acids       Date:  2021-08-26       Impact factor: 3.520

3.  New Insights Into the Biology of Protein O-GlcNAcylation: Approaches and Observations.

Authors:  Toni Mueller; Xiaosen Ouyang; Michelle S Johnson; Wei-Jun Qian; John C Chatham; Victor Darley-Usmar; Jianhua Zhang
Journal:  Front Aging       Date:  2021-03-12

4.  O-GlcNAcylation Suppresses the Ion Current IClswell by Preventing the Binding of the Protein ICln to α-Integrin.

Authors:  Roberta Costa; Alessia Remigante; Davide A Civello; Emanuele Bernardinelli; Zoltán Szabó; Rossana Morabito; Angela Marino; Antonio Sarikas; Wolfgang Patsch; Markus Paulmichl; Tamás Janáky; Attila Miseta; Tamás Nagy; Silvia Dossena
Journal:  Front Cell Dev Biol       Date:  2020-11-19

5.  Defining the Dynamic Regulation of O-GlcNAc Proteome in the Mouse Cortex---the O-GlcNAcylation of Synaptic and Trafficking Proteins Related to Neurodegenerative Diseases.

Authors:  Van N Huynh; Sheng Wang; Xiaosen Ouyang; Willayat Y Wani; Michelle S Johnson; Balu K Chacko; Anil G Jegga; Wei-Jun Qian; John C Chatham; Victor M Darley-Usmar; Jianhua Zhang
Journal:  Front Aging       Date:  2021-09-29
  5 in total

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