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Literature DB >> 22453906

Phosphorylation sites of higher stoichiometry are more conserved.

Chris Soon Heng Tan, Gary D Bader.

Abstract

Mesh：

Substances：

Year: 2012 PMID： 22453906 DOI： 10.1038/nmeth.1941

Source DB: PubMed Journal: Nat Methods ISSN： 1548-7091 Impact factor: 28.547

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5 in total

1. Highly expressed genes in yeast evolve slowly.

Authors: C Pál; B Papp; L D Hurst
Journal: Genetics Date: 2001-06 Impact factor: 4.562

2. Why highly expressed proteins evolve slowly.

Authors: D Allan Drummond; Jesse D Bloom; Christoph Adami; Claus O Wilke; Frances H Arnold
Journal: Proc Natl Acad Sci U S A Date: 2005-09-21 Impact factor: 11.205

3. An evolutionary proteomics approach identifies substrates of the cAMP-dependent protein kinase.

Authors: Yelena V Budovskaya; Joseph S Stephan; Stephen J Deminoff; Paul K Herman
Journal: Proc Natl Acad Sci U S A Date: 2005-09-19 Impact factor: 11.205

4. Global analysis of protein expression in yeast.

Authors: Sina Ghaemmaghami; Won-Ki Huh; Kiowa Bower; Russell W Howson; Archana Belle; Noah Dephoure; Erin K O'Shea; Jonathan S Weissman
Journal: Nature Date: 2003-10-16 Impact factor: 49.962

5. A large-scale method to measure absolute protein phosphorylation stoichiometries.

Authors: Ronghu Wu; Wilhelm Haas; Noah Dephoure; Edward L Huttlin; Bo Zhai; Mathew E Sowa; Steven P Gygi
Journal: Nat Methods Date: 2011-07-03 Impact factor: 28.547

5 in total

7 in total

7. Evaluation of functionality for serine and threonine phosphorylation with different evolutionary ages in human and mouse.

Authors: Benpeng Miao; Qingyu Xiao; Weiran Chen; Yixue Li; Zhen Wang
Journal: BMC Genomics Date: 2018-06-04 Impact factor: 3.969

7 in total

Phosphorylation sites of higher stoichiometry are more conserved.

1. Highly expressed genes in yeast evolve slowly.

2. Why highly expressed proteins evolve slowly.

3. An evolutionary proteomics approach identifies substrates of the cAMP-dependent protein kinase.

4. Global analysis of protein expression in yeast.

5. A large-scale method to measure absolute protein phosphorylation stoichiometries.

Review 1. The coming of age of phosphoproteomics--from large data sets to inference of protein functions.

Review 2. Next-generation proteomics: towards an integrative view of proteome dynamics.

3. Deciphering a global network of functionally associated post-translational modifications.

Review 4. Exploiting holistic approaches to model specificity in protein phosphorylation.

Review 5. Recent findings and technological advances in phosphoproteomics for cells and tissues.

Review 6. Evolution and functional cross-talk of protein post-translational modifications.

7. Evaluation of functionality for serine and threonine phosphorylation with different evolutionary ages in human and mouse.