Examining post-translational modification-mediated protein-protein interactions using a chemical proteomics approach

Protein Science

Volumn 22, Issue 3, 2013, Pages 287-295

  Li, Xiang ^a,b   Foley, Emily A ^a   Kawashima, Shigehiro A ^a   Molloy, Kelly R ^c   Li, Yinyin ^c   Chait, Brian T ^c   Kapoor, Tarun M ^a  

^a Laboratory of Stem Cell Andtumor Biology Neurosurgery and Cellular Biochemistry and Biophysics   (United States)

^b UNIVERSITY OF HONG KONG   (Hong Kong)

^c ROCKEFELLER UNIVERSITY   (United States)

Author keywords

Chemical proteomics; Histone; Phosphorylation; Post translational modification; Protein protein interaction

Indexed keywords

HISTONE H3; LYSINE; PEPTIDES AND PROTEINS; PROTEIN HYDROLYSATE; PROTEIN KIF2A; PROTEIN MCAK; SURVIVIN; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; CELL DIVISION; CROSS LINKING ASSISTED AND STABLE ISOTOPE LABELING IN CELL CULTURE BASED PROTEIN IDENTIFICATION; HISTONE PHOSPHORYLATION; HUMAN; HUMAN CELL; POST TRANSLATIONAL MODIFICATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; PROTEOMICS;

BIOLOGICAL MARKERS; CELL DIVISION; CHROMOSOMAL PROTEINS, NON-HISTONE; HELA CELLS; HISTONES; HUMANS; INHIBITOR OF APOPTOSIS PROTEINS; KINESIN; LYSINE; METHYLATION; MOLECULAR PROBE TECHNIQUES; PEPTIDE FRAGMENTS; PHOSPHORYLATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEOMICS; RECOMBINANT PROTEINS; THREONINE; YEASTS;

PHOS; SCHIZOSACCHAROMYCETACEAE;

EID: 84878306488     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2210     Document Type: Article

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