Inactivation by Hg2+ and methylmercury of the glutamine/amino acid transporter (ASCT2) reconstituted in liposomes: Prediction of the involvement of a CXXC motif by homology modelling

Biochemical Pharmacology

Volumn 80, Issue 8, 2010, Pages 1266-1273

  Oppedisano, Francesca ^a   Galluccio, Michele ^a   Indiveri, Cesare ^a  

^a UNIVERSITY OF CALABRIA   (Italy)

Author keywords

ASCT2; Glutamine; Liposomes; Membrane; Methylmercury; Transport

Indexed keywords

ACETYLCYSTEINE; AMINO ACID TRANSPORTER; ANTIOXIDANT; CARBOCISTEINE; CYSTEINE; GLUTAMINE; LIPOSOME; MERCURIC CHLORIDE; MERCURY; MERSALYL; METHYLMERCURY; SODIUM; ASCT2 PROTEIN, RAT; METHYLMERCURY DERIVATIVE;

ANIMAL TISSUE; ARTICLE; CONCENTRATION RESPONSE; CONTROLLED STUDY; IC 50; METAL BINDING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEOLIPOSOME; PYROCOCCUS HORIKOSHII; RAT; STRUCTURE ANALYSIS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; METABOLISM; PROTEIN BINDING; PROTEIN CONFORMATION; TRANSPORT AT THE CELLULAR LEVEL;

AMINO ACID MOTIFS; AMINO ACID TRANSPORT SYSTEM ASC; BINDING SITES; BIOLOGICAL TRANSPORT; GLUTAMINE; LIPOSOMES; MERCURIC CHLORIDE; MERCURY; MERSALYL; METHYLMERCURY COMPOUNDS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; SODIUM;

EID: 77956227928     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2010.06.032     Document Type: Article

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