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Literature DB >> 28212757

A Prob(e)able Route to Lysine Acylation.

Abstract

Non-enzymatic modification of proteins by acyl-CoA species involved in intermediary metabolism is a possible explanation for widespread protein acylation. In this issue, Kulkarni et al. (2017) develop a set of chemoproteomic probes to interrogate the role of malonyl-CoA in mediating protein malonylation and find malonylation influences glycolysis in cancer cells.

Entities: Chemical Disease Gene Species

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Year: 2017 PMID： 28212757 PMCID： PMC5503691 DOI： 10.1016/j.chembiol.2017.01.011

Source DB: PubMed Journal: Cell Chem Biol ISSN： 2451-9448 Impact factor: 8.116

12 in total

1. Stoichiometry of site-specific lysine acetylation in an entire proteome.

Authors: Josue Baeza; James A Dowell; Michael J Smallegan; Jing Fan; Daniel Amador-Noguez; Zia Khan; John M Denu
Journal: J Biol Chem Date: 2014-06-10 Impact factor: 5.157

2. Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.

Authors: Raymond E Moellering; Benjamin F Cravatt
Journal: Science Date: 2013-08-02 Impact factor: 47.728

3. SIRT5 Regulates both Cytosolic and Mitochondrial Protein Malonylation with Glycolysis as a Major Target.

Authors: Yuya Nishida; Matthew J Rardin; Chris Carrico; Wenjuan He; Alexandria K Sahu; Philipp Gut; Rami Najjar; Mark Fitch; Marc Hellerstein; Bradford W Gibson; Eric Verdin
Journal: Mol Cell Date: 2015-06-11 Impact factor: 17.970

4. Identification of lysine succinylation as a new post-translational modification.

Authors: Zhihong Zhang; Minjia Tan; Zhongyu Xie; Lunzhi Dai; Yue Chen; Yingming Zhao
Journal: Nat Chem Biol Date: 2010-12-12 Impact factor: 15.040

5. Discovering Targets of Non-enzymatic Acylation by Thioester Reactivity Profiling.

Authors: Rhushikesh A Kulkarni; Andrew J Worth; Thomas T Zengeya; Jonathan H Shrimp; Julie M Garlick; Allison M Roberts; David C Montgomery; Carole Sourbier; Benjamin K Gibbs; Clementina Mesaros; Yien Che Tsai; Sudipto Das; King C Chan; Ming Zhou; Thorkell Andresson; Allan M Weissman; W Marston Linehan; Ian A Blair; Nathaniel W Snyder; Jordan L Meier
Journal: Cell Chem Biol Date: 2017-02-02 Impact factor: 8.116

6. Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.

Authors: Amelia J Still; Brendan J Floyd; Alexander S Hebert; Craig A Bingman; Joshua J Carson; Drew R Gunderson; Brendan K Dolan; Paul A Grimsrud; Kristin E Dittenhafer-Reed; Donald S Stapleton; Mark P Keller; Michael S Westphall; John M Denu; Alan D Attie; Joshua J Coon; David J Pagliarini
Journal: J Biol Chem Date: 2013-07-17 Impact factor: 5.157

A Prob(e)able Route to Lysine Acylation.

1. Stoichiometry of site-specific lysine acetylation in an entire proteome.

2. Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.

3. SIRT5 Regulates both Cytosolic and Mitochondrial Protein Malonylation with Glycolysis as a Major Target.

4. Identification of lysine succinylation as a new post-translational modification.

5. Discovering Targets of Non-enzymatic Acylation by Thioester Reactivity Profiling.

6. Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.

Review 7. The growing landscape of lysine acetylation links metabolism and cell signalling.

Review 8. Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases.

9. Malonyl-CoA decarboxylase inhibition is selectively cytotoxic to human breast cancer cells.

10. Phenotype-based cell-specific metabolic modeling reveals metabolic liabilities of cancer.

1. Emerging Roles for SIRT5 in Metabolism and Cancer.