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Recent progress in quantitative phosphoproteomics

Espert Review of Proteomics, 2023
Introduction Protein phosphorylation is a critical post-translational modification involved in the regulation of numerous cellular processes from signal transduction to modulation of enzyme activities.
Katharina I. Zittlau   +5 more
semanticscholar   +1 more source

Evaluation of DDA Library-Free Strategies for Phosphoproteomics and Ubiquitinomics Data-Independent Acquisition Data.

Journal of Proteome Research, 2023
Phosphoproteomics and ubiquitinomics data-independent acquisition (DIA) mass spectrometry (MS) data is typically analyzed by using a data-dependent acquisition (DDA) spectral library.
Chengwen Wen   +10 more
semanticscholar   +1 more source

Phospho-Analyst: An Interactive, Easy-to-Use Web Platform To Analyze Quantitative Phosphoproteomics Data.

Journal of Proteome Research, 2023
Phosphoproteomics is nowadays the method of choice to comprehensively identify and quantify thousands of phosphorylated peptides and their associated proteins with the goal of interrogating changes in signal transduction pathways and other cellular ...
Haijian Zhang   +5 more
semanticscholar   +1 more source

Phosphoproteomics: Methods and Challenges

2023
Protein phosphorylation is a widespread post-translational modification that regulates many biological processes. This covalent modification alters the biochemical properties of proteins and can act as an activity switch or as a docking site for protein-protein interactions.
Kang, Taewook   +3 more
openaire   +2 more sources

ATR phosphoproteomics

2023
R scripts used in the publication for the analysis of the phospho-proteomics dataset.
Jadav, Rathan S   +17 more
  +4 more sources

Phosphoproteomics

Current Protocols in Protein Science, 2007
AbstractProtein phosphorylation is one of the most important mechanisms of regulating protein function in cells, and it plays an important role in controlling diverse biological processes, including cellular proliferation, migration, and metabolism.
Jun, Zhong   +2 more
openaire   +2 more sources

Phosphoproteomics

WIREs Systems Biology and Medicine, 2010
AbstractCurrent analytical protein methods show phosphorylation to be the most ubiquitous, evolutionary conserved post‐translational modification Post‐Translational Modification (PTM). The reversible and transient nature of protein phosphorylation allows signal transduction pathways to carry out diverse cellular functions.
Nurhan, Ozlu   +5 more
openaire   +2 more sources

Subcellular phosphoproteomics

Mass Spectrometry Reviews, 2010
AbstractProtein phosphorylation represents one of the most extensively studied post‐translational modifications, primarily due to the emergence of sensitive methods enabling the detection of this modification both in vitro and in vivo. The availability of enrichment methods combined with sensitive mass spectrometry instrumentation has played a crucial ...
Trost, Matthias   +3 more
openaire   +3 more sources

Improving Phosphoproteomics Profiling Using Data-Independent Mass Spectrometry.

Journal of Proteome Research, 2022
Mass spectrometry-based profiling of the phosphoproteome is a powerful method of identifying phosphorylation events at a systems level. Most phosphoproteomics studies have used data-dependent acquisition (DDA) mass spectrometry as their method of choice.
Aparna Srinivasan   +3 more
semanticscholar   +1 more source

WIDENING THE BOTTLENECK OF PHOSPHOPROTEOMICS: EVOLVING STRATEGIES FOR PHOSPHOPEPTIDE ENRICHMENT.

Mass spectrometry reviews (Print), 2020
Phosphorylation is a form of protein posttranslational modification (PTM) that regulates many biological processes. Whereas phosphoproteomics is a scientific discipline that identifies and quantifies the phosphorylated proteome using mass spectrometry ...
T. Low   +5 more
semanticscholar   +1 more source

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