Nepsilon-formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function
about
The functional diversity of protein lysine methylationProteomics in epigenetics: new perspectives for cancer researchH1 histones: current perspectives and challengesProtein lysine acylation and cysteine succination by intermediates of energy metabolismQuantitative analysis of histone modifications: formaldehyde is a source of pathological n(6)-formyllysine that is refractory to histone deacetylasesISPTM: an iterative search algorithm for systematic identification of post-translational modifications from complex proteome mixturesQuantitative proteomic analysis of histone modificationsQuantitative mass spectrometry of histones H3.2 and H3.3 in Suz12-deficient mouse embryonic stem cells reveals distinct, dynamic post-translational modifications at Lys-27 and Lys-36Controlled modification of biomolecules by ultrashort laser pulses in polar liquidsDiscovery of lysine post-translational modifications through mass spectrometric detectionProteomic interrogation of human chromatin.Regulation of autotrophic CO2 fixation in the archaeon Thermoproteus neutrophilus.Mapping of six somatic linker histone H1 variants in human breast cancer cells uncovers specific features of H1.2.Peroxynitrite-induced nitrative and oxidative modifications alter tau filament formation.A comprehensive view of the epigenetic landscape. Part II: Histone post-translational modification, nucleosome level, and chromatin regulation by ncRNAs.Breaking the histone code with quantitative mass spectrometry.Collective mass spectrometry approaches reveal broad and combinatorial modification of high mobility group protein A1a.Histone H1 Variants in Arabidopsis Are Subject to Numerous Post-Translational Modifications, Both Conserved and Previously Unknown in Histones, Suggesting Complex Functions of H1 in Plants.The H1 linker histones: multifunctional proteins beyond the nucleosomal core particle.The Emerging Hallmarks of Cancer MetabolismProteomic characterization of novel histone post-translational modifications.Dosimetry of N⁶-formyllysine adducts following [¹³C²H₂]-formaldehyde exposures in rats.Post-translational modification of proteins in toxicological research: focus on lysine acylation.Quantitative proteomics reveals histone modifications in crosstalk with H3 lysine 27 methylation.The requirement for proteomics to unravel stem cell regulatory mechanisms.The methylproteome and the intracellular methylation network.The enigmatic role of H2Bub1 in cancer.Epigenetic modifications of the neuroproteome.Developmental and environmental epigenetic programming of the endocrine pancreas: consequences for type 2 diabetes.The path to life's origins. Remaining hurdles.Posttranslational modifications of human histone H3: an update.The growing landscape of lysine acetylation links metabolism and cell signalling.Comprehensive Catalog of Currently Documented Histone Modifications.The contribution of mass spectrometry-based proteomics to understanding epigenetics.SET domain-mediated lysine methylation in lower organisms regulates growth and transcription in hosts.Histone Modifications and Cancer.Genetic Incorporation of N(ε)-Formyllysine, a New Histone Post-translational Modification.Dynamics and dispensability of variant-specific histone H1 Lys-26/Ser-27 and Thr-165 post-translational modifications.Loss of nuclear flavanols during drought periods in Taxus baccata.Challenges ahead for mass spectrometry and proteomics applications in epigenetics.
P2860
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P2860
Nepsilon-formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function
description
2008 nî lūn-bûn
@nan
2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Nepsilon-formylation of lysine ...... gulation of chromatin function
@ast
Nepsilon-formylation of lysine ...... gulation of chromatin function
@en
Nepsilon-formylation of lysine ...... gulation of chromatin function
@nl
type
label
Nepsilon-formylation of lysine ...... gulation of chromatin function
@ast
Nepsilon-formylation of lysine ...... gulation of chromatin function
@en
Nepsilon-formylation of lysine ...... gulation of chromatin function
@nl
prefLabel
Nepsilon-formylation of lysine ...... gulation of chromatin function
@ast
Nepsilon-formylation of lysine ...... gulation of chromatin function
@en
Nepsilon-formylation of lysine ...... gulation of chromatin function
@nl
P2093
P2860
P356
P1476
Nepsilon-formylation of lysine ...... gulation of chromatin function
@en
P2093
Alexandre Zougman
Jacek R Wisniewski
Matthias Mann
P2860
P356
10.1093/NAR/GKM1057
P407
P577
2008-02-01T00:00:00Z