The cytoplasmic and transmembrane domains of the p75 and Trk A receptors regulate high affinity binding to nerve growth factor.

Esposito, D; Patel, P; Stephens, R M; Perez, P; Chao, M V; Kaplan, D R; Hempstead, B L

Esposito, D; Patel, P; Stephens, R M; Perez, P; Chao, M V; Kaplan, D R; Hempstead, B L.

Affiliation

Esposito D; Division of Hematology, Weill Medical College of Cornell University, New York, New York 10021, USA.

J Biol Chem ; 276(35): 32687-95, 2001 Aug 31.

Article in En | MEDLINE | ID: mdl-11435417

Subject(s)

Nerve Growth Factor/metabolism; Receptor, trkA/metabolism; Receptors, Nerve Growth Factor/metabolism; Animals; Binding Sites; Cell Line; Cell Membrane/metabolism; Cytoplasm/metabolism; Humans; Kinetics; Ligands; Models, Molecular; Protein Conformation; Receptor, Nerve Growth Factor; Receptor, trkA/chemistry; Receptor, trkA/genetics; Receptors, Nerve Growth Factor/chemistry; Receptors, Nerve Growth Factor/genetics; Recombinant Fusion Proteins/metabolism; Spodoptera; Transfection

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Collection: 01-internacional Database: MEDLINE Main subject: Receptors, Nerve Growth Factor / Receptor, trkA / Nerve Growth Factor Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: J Biol Chem Year: 2001 Document type: Article Affiliation country: United States Country of publication: United States

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