Two different combinations of RNA-binding domains determine the RNA binding specificity of nucleolin.

Ginisty, H; Amalric, F; Bouvet, P

Ginisty, H; Amalric, F; Bouvet, P.

Affiliation

Ginisty H; Laboratoire de Pharmacologie et de Biologie Structurale, CNRS UMR 5089, 205 route de Narbonne, 31077 Toulouse Cedex, France.

J Biol Chem ; 276(17): 14338-43, 2001 Apr 27.

Article in En | MEDLINE | ID: mdl-11278842

Subject(s)

Phosphoproteins/chemistry; Phosphoproteins/metabolism; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/metabolism; RNA/metabolism; Animals; Base Sequence; Conserved Sequence; Cricetinae; DNA Mutational Analysis; Dose-Response Relationship, Drug; Gene Deletion; Kinetics; Molecular Sequence Data; Mutation; Phosphoproteins/genetics; Plasmids/metabolism; Protein Binding; Protein Conformation; Protein Structure, Tertiary; RNA, Ribosomal/metabolism; RNA-Binding Proteins/genetics; Recombinant Proteins/metabolism; Transcription, Genetic; Ultraviolet Rays; Xenopus; Nucleolin

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Collection: 01-internacional Database: MEDLINE Main subject: Phosphoproteins / RNA / RNA-Binding Proteins Limits: Animals Language: En Journal: J Biol Chem Year: 2001 Document type: Article Affiliation country: France Country of publication: United States

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