Copper-mediated cross-linking of S100A4, but not of S100A2, results in proinflammatory effects in melanoma cells

Biochemical and Biophysical Research Communications

Volumn 413, Issue 3, 2011, Pages 494-498

  Haase Kohn, Cathleen ^a   Wolf, Susann ^a   Lenk, Jens ^a   Pietzsch, Jens ^a  

^a INSTITUTE OF ION BEAM PHYSICS AND MATERIALS RESEARCH   (Germany)

Author keywords

A375; Bivalent cations; Cysteine residues; Oxidation; RAGE; S100

Indexed keywords

ADVANCED GLYCATION END PRODUCT; CALCIUM BINDING PROTEIN; CALVASCULIN; COPPER; CYSTEINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN S100A2; SYNAPTOTAGMIN I; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; ELECTROPHORESIS; HUMAN; HUMAN CELL; MASS SPECTROMETRY; MELANOMA CELL; NUCLEOTIDE SEQUENCE; OXIDATION; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN STRUCTURE; RECEPTOR BINDING; TUMOR MICROENVIRONMENT;

AMINO ACID SEQUENCE; CELL LINE, TUMOR; CHEMOTACTIC FACTORS; COPPER; CROSS-LINKING REAGENTS; CYSTEINE; GLYCOSYLATION END PRODUCTS, ADVANCED; HUMANS; INFLAMMATION; MELANOMA; MOLECULAR SEQUENCE DATA; NF-KAPPA B; OXIDATION-REDUCTION; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, IMMUNOLOGIC; S100 PROTEINS; TUMOR MICROENVIRONMENT; TUMOR NECROSIS FACTOR-ALPHA;

EID: 80053323736     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.08.132     Document Type: Article

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