Studies on the catalytic domains of multiple JmjC oxygenases using peptide substrates

Epigenetics

Volumn 9, Issue 12, 2014, Pages 1596-1603

  Williams, Sophie T ^a   Walport, Louise J ^a   Hopkinson, Richard J ^a   Madden, Sarah K ^a   Chowdhury, Rasheduzzaman ^a   Schofield, Christopher J ^a   Kawamura, Akane ^a,b  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

2OG oxygenases; Demethylation; Epigenetics; Histone; JmjC histone demethylase; Methyllysine

Indexed keywords

2 OXOGLUTARIC ACID; AMINO ACID; FORMALDEHYDE DEHYDROGENASE; HISTONE H3; JMJC OXYGENASE; N METHYL LYSINE; OXYGENASE; UNCLASSIFIED DRUG; C14ORF169 PROTEIN, HUMAN; EPSILON-N-METHYLLYSINE; F BOX PROTEIN; HISTONE; HISTONE DEMETHYLASE; KDM2A PROTEIN, HUMAN; KDM3A PROTEIN, HUMAN; KDM4A PROTEIN, HUMAN; KDM5C PROTEIN, HUMAN; KDM6B PROTEIN, HUMAN; KDM8 PROTEIN, HUMAN; LYSINE; MINA PROTEIN, HUMAN; N DEMETHYLASE; NONHISTONE PROTEIN; NUCLEAR PROTEIN; PEPTIDE FRAGMENT; UTX PROTEIN, HUMAN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DECARBOXYLATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HISTONE DEMETHYLATION; HUMAN; HUMAN CELL; HYDROXYLATION; IMMUNOPRECIPITATION; KDM4 CATALYTIC DOMAIN; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PEPTIDE SYNTHESIS; PHYLOGENY; PROTEIN BINDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; RADIOACTIVITY; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SEQUENCE HOMOLOGY; X RAY ANALYSIS; AMINO ACID SEQUENCE; ANALOGS AND DERIVATIVES; CHEMISTRY; ENZYME SPECIFICITY; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CHROMOSOMAL PROTEINS, NON-HISTONE; F-BOX PROTEINS; HISTONE DEMETHYLASES; HISTONES; HUMANS; HYDROXYLATION; JUMONJI DOMAIN-CONTAINING HISTONE DEMETHYLASES; LYSINE; MOLECULAR SEQUENCE DATA; NUCLEAR PROTEINS; OXIDOREDUCTASES, N-DEMETHYLATING; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

EID: 84922022543     PISSN: 15592294     EISSN: 15592308     Source Type: Journal    
DOI: 10.4161/15592294.2014.983381     Document Type: Article

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