Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli

Molecular and Cellular Proteomics

Volumn 8, Issue 2, 2009, Pages 215-225

  Zhang, Junmei ^a   Sprung, Robert ^a,f   Pei, Jimin ^a,b   Tan, Xiaohong ^c   Kim, Sungchan ^d   Zhu, Heng ^e   Liu, Chuan Fa ^c   Grishin, Nick V ^a,b   Zhao, Ying ^a,g  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^c Nanyang Technological University   (Singapore)

^d Hallym University   (South Korea)

^e JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^f VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^g UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE;

ACETYLATION; ARTICLE; CELL LYSATE; ENERGY METABOLISM; ESCHERICHIA COLI; GENE EXPRESSION; GENETIC CONSERVATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROKARYOTIC CELL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN MODIFICATION; SCREENING; WESTERN BLOTTING;

ACETYLATION; AMINO ACID MOTIFS; ANIMALS; BLOTTING, WESTERN; CITRIC ACID CYCLE; COMPUTATIONAL BIOLOGY; CONSERVED SEQUENCE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; EVOLUTION, MOLECULAR; GLYCOLYSIS; LYSINE; PROTEIN BIOSYNTHESIS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEOMICS; STRESS, PHYSIOLOGICAL; SUBSTRATE SPECIFICITY; TRANSCRIPTION, GENETIC;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MAMMALIA; PROKARYOTA;

EID: 61649089277     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M800187-MCP200     Document Type: Article

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