Modulation of p36 phosphorylation in human cells: studies using anti-p36 monoclonal antibodies. | Zendy

Clare M. Isacke | Zendy; Ian S. Trowbridge | Zendy; Tony Hunter | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Modulation of p36 phosphorylation in human cells: studies using anti-p36 monoclonal antibodies.

Author(s) -

Clare M. Isacke,

Ian S. Trowbridge,

Tony Hunter

Publication year - 1986

Publication title -

molecular and cellular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.14

H-Index - 327

eISSN - 1067-8824

pISSN - 0270-7306

DOI - 10.1128/mcb.6.7.2745

Subject(s) - phosphorylation , biology , monoclonal antibody , microbiology and biotechnology , serine , tyrosine , epidermal growth factor , tyrosine phosphorylation , tyrosine kinase , antibody , signal transduction , biochemistry , immunology , receptor

We have characterized two monoclonal antibodies which recognize human p36. These have been used to examine the sites and extent of serine and tyrosine phosphorylation of p36 in human cells treated with epidermal growth factor and platelet-derived growth factor and in human cells transformed with viruses whose oncogenes encode protein-tyrosine kinases.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research