Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue

Molecular and Cellular Proteomics

Volumn 6, Issue 1, 2007, Pages 72-87

  Wiśniewski, Jacek R ^a   Zougman, Alexandre ^a   Krüger, Sonja ^a   Mann, Matthias ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS DNA; HISTONE H1; LYSINE;

ACCURACY; ACETYLATION; AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CELL CULTURE; CONTROLLED STUDY; HUMAN; HUMAN CELL; ION TRAP MASS SPECTROMETRY; METHYLATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; UBIQUITINATION;

ACETYLATION; AMINO ACID SEQUENCE; ANIMALS; CHROMATOGRAPHY, LIQUID; HELA CELLS; HISTONES; HUMANS; LYSINE; MASS SPECTROMETRY; METHYLATION; MICE; MICE, INBRED C57BL; MOLECULAR SEQUENCE DATA; PEPTIDE MAPPING; PEPTIDES; PHOSPHORYLATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; UBIQUITIN;

EID: 33846488609     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M600255-MCP200     Document Type: Article

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