Unambiguous characterization of site-specific phosphorylation of leucine-rich repeat fli-i-interacting protein 2 (LRRFIP2) in toll-like receptor 4 (TLR4)-mediated signaling

Journal of Biological Chemistry

Volumn 286, Issue 13, 2011, Pages 10897-10910

  Gunawardena, Harsha P ^a   Huang, Yi ^b   Kenjale, Roma ^b   Wang, Haiyang ^b   Xie, Ling ^b   Chen, Xian ^a,b  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEINS; BIOLOGICAL CHARACTERIZATION; CELLULAR RESPONSE; COLLISION-ACTIVATED DISSOCIATIONS; DRIVING FORCES; DYNAMIC CHANGES; DYNAMIC INTERACTION; ELECTRON TRANSFER DISSOCIATION; ISOTOPE LABELING; LABEL FREE; LABEL-FREE APPROACH; LEUCINE-RICH REPEATS; PHOSPHORYLATION SITES; QUANTITATIVE PROTEOMICS; SERINE RESIDUES; SIGNALING PATHWAYS; SITE DIRECTED MUTAGENESIS; SITE-SPECIFIC; TIME COURSE; TOLL-LIKE RECEPTOR 4;

AMINO ACIDS; CELL CULTURE; DISSOCIATION; ISOTOPES; MASS SPECTROMETRY; MOLECULAR BIOLOGY; PROTEINS; SIGNALING;

PHOSPHORYLATION;

CELL PROTEIN; LEUCINE RICH REPEAT FLI 1 INTERACTING PROTEIN 2; LIPOPOLYSACCHARIDE; MYELOID DIFFERENTIATION FACTOR 88; SERINE; TOLL LIKE RECEPTOR 4; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CELL STIMULATION; CELL STRAIN HEK293; COLLISIONALLY ACTIVATED DISSOCIATION; CONTROLLED STUDY; ELECTRON TRANSPORT; HUMAN; HUMAN CELL; ISOTOPE LABELING; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEOMICS; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS;

ANIMALS; CARRIER PROTEINS; HEK293 CELLS; HUMANS; LIPOPOLYSACCHARIDES; MICE; MUTAGENESIS, SITE-DIRECTED; MUTATION, MISSENSE; MYELOID DIFFERENTIATION FACTOR 88; NF-KAPPA B; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION; TOLL-LIKE RECEPTOR 4;

EID: 79953177908     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.168179     Document Type: Article

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