(Q22061729)

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Phosphoproteomic Analysis of the Mouse Brain Cytosol Reveals a Predominance of Protein Phosphorylation in Regions of Intrinsic Sequence Disorder

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Phosphoproteomic analysis of the mouse brain cytosol reveals a predominance of protein phosphorylation in regions of intrinsic sequence disorder

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5 January 2020

Phosphoproteomic analysis of the mouse brain cytosol reveals a predominance of protein phosphorylation in regions of intrinsic sequence disorder (English)

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5 January 2020

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Mark O. Collins

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Mark O Collins

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Collins

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5 January 2020

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Seth G N Grant

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5 January 2020

Jyoti Choudhary

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5 January 2020

Iain D G Campuzano

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5 January 2020

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Lu Yu

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3 April 2008

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5 January 2020

Molecular & Cellular Proteomics

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5 January 2020

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5 January 2020

1331-1348

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5 January 2020

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5 January 2020

Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae

1 reference

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Proteomic analysis of in vivo phosphorylated synaptic proteins.

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Comprehensive identification of phosphorylation sites in postsynaptic density preparations

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Global, in vivo, and site-specific phosphorylation dynamics in signaling networks

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Reproducible isolation of distinct, overlapping segments of the phosphoproteome

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Large-scale phosphorylation analysis of mouse liver

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Exploring the phosphoproteome with mass spectrometry

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Analysis of protein phosphorylation on a proteome-scale

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Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.

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Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry

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The folding energy landscape and phosphorylation: modeling the conformational switch of the NFAT regulatory domain

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The importance of intrinsic disorder for protein phosphorylation

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Robust enrichment of phosphorylated species in complex mixtures by sequential protein and peptide metal-affinity chromatography and analysis by tandem mass spectrometry.

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Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations

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Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions.

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Control of intrinsically disordered stathmin by multisite phosphorylation.

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RNA association or phosphorylation of the RS domain prevents aggregation of RS domain-containing proteins.

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Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes

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Intrinsically unstructured proteins evolve by repeat expansion

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Identifiers

10.1074/MCP.M700564-MCP200

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Consolidated OpenCitations Corpus – April 2017

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18388127%20AND%20SRC:MED&resulttype=core&format=json

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