PLDMS: Phosphopeptide Library Dephosphorylation Followed by Mass Spectrometry Analysis to Determine the Specificity of Phosphatases for Dephosphorylation Site Sequences-Reference-Cited by-同舟云学术

PLDMS: Phosphopeptide Library Dephosphorylation Followed by Mass Spectrometry Analysis to Determine the Specificity of Phosphatases for Dephosphorylation Site Sequences

Published:2022 Issue: Volume: Page:43-64
ISSN:1064-3745
Container-title:Methods in Molecular Biology
language:
Short-container-title:

Author:

Kokot Thomas,Hoermann Bernhard,Helm Dominic,Chojnacki Jeremy E.,Savitski Mikhail M.,Köhn Maja

Publisher

Springer US

Link

https://link.springer.com/content/pdf/10.1007/978-1-0716-2317-6_2

Reference25 articles.

1. Deribe YL, Pawson T, Dikic I (2010) Post-translational modifications in signal integration. Nat Struct Mol Biol 17:666–672

2. Khoury GA, Baliban RC, Floudas CA (2011) Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database. Sci Rep 1:srep00090

3. Ochoa D, Jarnuczak AF, Viéitez C et al (2020) The functional landscape of the human phosphoproteome. Nat Biotechnol 38:365–373

4. Sharma K, D’Souza RCJ, Tyanova S et al (2014) Ultradeep human Phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. Cell Rep 8:1583–1594

5. Beltrao P, Bork P, Krogan NJ, van Noort V (2013) Evolution and functional cross-talk of protein post-translational modifications. Mol Syst Biol 9:714

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Phosphoproteomic Approaches for Identifying Phosphatase and Kinase Substrates;Molecules;2023-04-24

2. Emerging insights into serine/threonine-specific phosphoprotein phosphatase function and selectivity;Journal of Cell Science;2022-10-01