A large-scale method to measure absolute protein phosphorylation stoichiometries. - Wikidata - wikimedia - TriplyDB

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

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

http://www.wikidata.org/entity/Q42847626

about

Recent findings and technological advances in phosphoproteomics for cells and tissues Evolution and functional cross-talk of protein post-translational modifications Quantifying ubiquitin signaling Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Status of large-scale analysis of post-translational modifications by mass spectrometry Mapping and analysis of phosphorylation sites: a quick guide for cell biologists Computational phosphoproteomics: from identification to localization Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases Activation and inhibition of Snf1 kinase activity by phosphorylation within the activation loop.Mass Spectrometry-Based Approaches to Understand the Molecular Basis of Memory Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse The Die Is Cast: Precision Electrophilic Modifications Contribute to Cellular Decision Making Proteome-wide analysis of arginine monomethylation reveals widespread occurrence in human cells Quantitative proteomic analysis of histone modifications Top-down mass spectrometry for the analysis of combinatorial post-translational modifications.Functional decorations: post-translational modifications and heart disease delineated by targeted proteomics.The coming of age of phosphoproteomics--from large data sets to inference of protein functions Large-scale label-free phosphoproteomics: from technology to data interpretation.Phospho-iTRAQ data article: Assessing isobaric labels for the large-scale study of phosphopeptide stoichiometry.Multi-omics approaches to disease.Does reversible cysteine oxidation link the Western diet to cardiac dysfunction?Quantitative investigation of human cell surface N-glycoprotein dynamics.Stoichiometry of site-specific lysine acetylation in an entire proteome.Current technologies to identify protein kinase substrates in high throughput A method to determine lysine acetylation stoichiometries.Identification and validation of inhibitor-responsive kinase substrates using a new paradigm to measure kinase-specific protein phosphorylation index Phosphorylation stoichiometries of human eukaryotic initiation factors Novel mass spectrometric method for phosphorylation quantification using cerium oxide nanoparticles and tandem mass tags Emerging mass spectrometry techniques for the direct analysis of microbial colonies.Sequential enrichment with titania-coated magnetic mesoporous hollow silica microspheres and zirconium arsenate-modified magnetic nanoparticles for the study of phosphoproteome of HL60 cells Integrating phosphoproteomics in systems biology.Sequential selective enrichment of phosphopeptides and glycopeptides using amine-functionalized magnetic nanoparticles.Diverse and divergent protein post-translational modifications in two growth stages of a natural microbial community.Evaluating multiplexed quantitative phosphopeptide analysis on a hybrid quadrupole mass filter/linear ion trap/orbitrap mass spectrometer.Large-scale determination of absolute phosphorylation stoichiometries in human cells by motif-targeting quantitative proteomics.Post-translational modifications and lipid binding profile of insect cell-expressed full-length mammalian synaptotagmin 1 Reg1 protein regulates phosphorylation of all three Snf1 isoforms but preferentially associates with the Gal83 isoform Multiscale analysis of the murine intestine for modeling human diseases.Perspectives on: SGP symposium on mitochondrial physiology and medicine: mitochondrial proteome design: from molecular identity to pathophysiological regulation.Single-step inline hydroxyapatite enrichment facilitates identification and quantitation of phosphopeptides from mass-limited proteomes with MudPIT

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P2860

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

http://www.wikidata.org/entity/Q42847626

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

@zh-tw

2011年论文

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2011年论文

@zh

2011年论文

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name

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

@en

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

@nl

type

label

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

@en

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

@nl

prefLabel

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

@en

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

@nl

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

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Bo Zhai

http://www.w3.org/2001/XMLSchema#string

Edward L Huttlin

http://www.w3.org/2001/XMLSchema#string

Mathew E Sowa

http://www.w3.org/2001/XMLSchema#string

Ronghu Wu

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Wilhelm Haas

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P2860

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis

Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS

Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources

An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database

Assay development for the determination of phosphorylation stoichiometry using multiple reaction monitoring methods with and without phosphatase treatment: application to breast cancer signaling pathways

Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry

A tissue-specific atlas of mouse protein phosphorylation and expression

Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution

Length-dependent prediction of protein intrinsic disorder.

N-Terminal peptide labeling strategy for incorporation of isotopic tags: a method for the determination of site-specific absolute phosphorylation stoichiometry.

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8

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phosphorylation

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3146562

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