Identifying and quantifying in vivo methylation sites by heavy methyl SILAC - Test2 - elhamkhani - TriplyDB

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

http://www.wikidata.org/entity/Q28241075

about

Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications Ataxin-2-like is a regulator of stress granules and processing bodies Specificity of the chromodomain Y chromosome family of chromodomains for lysine-methylated ARK(S/T) motifs Friend of Prmt1, a novel chromatin target of protein arginine methyltransferases Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry H3R42me2a is a histone modification with positive transcriptional effects Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniques Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins.The functional diversity of protein lysine methylation An unexpected journey: lysine methylation across the proteome Proteomics in epigenetics: new perspectives for cancer research Post-transcriptional control of gene expression by AUF1: mechanisms, physiological targets, and regulation Decoding protein networks during virus entry by quantitative proteomics An inhibitor of KDM5 demethylases reduces survival of drug-tolerant cancer cells Mass spectrometry-based proteomics turns quantitative ESNOQ, proteomic quantification of endogenous S-nitrosation Increased protein arginine methylation in chronic hypoxia: role of protein arginine methyltransferases Jmjd2b antagonizes H3K9 trimethylation at pericentric heterochromatin in mammalian cells ISPTM: an iterative search algorithm for systematic identification of post-translational modifications from complex proteome mixtures Arginine Demethylation of G3BP1 Promotes Stress Granule Assembly Quantitative proteomic analysis of histone modifications Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity.A method for systematic mapping of protein lysine methylation identifies functions for HP1β in DNA damage response.iMethyl-PseAAC: identification of protein methylation sites via a pseudo amino acid composition approach Comprehending dynamic protein methylation with mass spectrometry Analysis of N-glycoproteins using genomic N-glycosite prediction.Arginine methylation controls the subcellular localization and functions of the oncoprotein splicing factor SF2/ASF PAT-H-MS coupled with laser microdissection to study histone post-translational modifications in selected cell populations from pathology samples.Discovery of lysine post-translational modifications through mass spectrometric detection Proteomic interrogation of human chromatin.Chemical and biochemical approaches in the study of histone methylation and demethylation Methods for Activity Analysis of the Proteins that Regulate Histone Methylation Transportin-1 and Transportin-2: protein nuclear import and beyond.Complications in the assignment of 14 and 28 Da mass shift detected by mass spectrometry as in vivo methylation from endogenous proteins.Quantitative proteomic discovery of dynamic epigenome changes that control human cytomegalovirus (HCMV) infection Perspectives on the discovery of small-molecule modulators for epigenetic processes.Kinetics of re-establishing H3K79 methylation marks in global human chromatin.Emerging technologies to map the protein methylome.The effect of PRMT1-mediated arginine methylation on the subcellular localization, stress granules, and detergent-insoluble aggregates of FUS/TLS.Autoregulation of ribosome biosynthesis by a translational response in fission yeast.

P2860

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P2860

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

http://www.wikidata.org/entity/Q28241075

description

2004 nî lūn-bûn

@nan

2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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name

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

@ast

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

@en

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

@nl

type

label

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

@ast

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

@en

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

@nl

prefLabel

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

@ast

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

@en

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

@nl

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Identifying and quantifying in vivo methylation sites by heavy methyl SILAC

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Gerhard Mittler

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

Matthias Mann

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

Shao-En Ong

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

P2860

Epigenetic regulation of gene expression: how the genome integrates intrinsic and environmental signals

Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3

PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays

Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.

Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1

Accurate quantitation of protein expression and site-specific phosphorylation

Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein

Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics

Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains

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119-26

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scholarly article

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2284140

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10.1038/NMETH715

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2

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1

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7953281

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1049948218

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15782174

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