Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena

Proceedings of the National Academy of Sciences of the United States of America

Volumn 96, Issue 26, 1999, Pages 14967-14972

  Strahl, Brian D ^a   Ohba, Reiko ^a   Cook, Richard G ^b   Allis, C David ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H3; LYSINE; METHYLTRANSFERASE;

ACETYLATION; ARTICLE; CHROMATIN STRUCTURE; ENZYME ACTIVITY; GENE ACTIVATION; GENE EXPRESSION; GENETIC CONSERVATION; HUMAN; HUMAN CELL; METHYLATION; NONHUMAN; PRIORITY JOURNAL; TRANSACTIVATION; TRANSCRIPTION REGULATION; YEAST;

ACETYLTRANSFERASES; AMINO ACID SEQUENCE; ANIMALS; CELL NUCLEUS; HELA CELLS; HISTONE ACETYLTRANSFERASES; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; LYSINE; METHYLATION; METHYLTRANSFERASES; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; SACCHAROMYCES CEREVISIAE PROTEINS; SPECIES SPECIFICITY; TETRAHYMENA THERMOPHILA; TRANSCRIPTION, GENETIC; YEASTS;

PROTOZOA; TETRAHYMENA;

EID: 0033592999     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.96.26.14967     Document Type: Article

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