Literature DB >> 3199814

Characterization of p29, an estrogen-receptor associated tumor marker.

A I Coffer1, R J King.   

Abstract

Monoclonal antibody D5, raised against cytosolic human estrogen receptor (ER) reacts with p29, a receptor-associated cytoplasmic serine phosphoprotein which does not bind steroid, While p29 selectively binds GTP and to a lesser extent ATP, in vitro GTP binding does not result in p29 phosphorylation. Under ER activating conditions, p29 associates with cytosolic ER; GTP, ATP and sodium molybdate block formation of immunoprecipitable p29-ER complexes. Nucleotide binding data suggest a role for p29 in the estrogen response machinery, possibly at the level of phosphate or nucleotide metabolism.

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Year:  1988        PMID: 3199814     DOI: 10.1016/0022-4731(88)90281-6

Source DB:  PubMed          Journal:  J Steroid Biochem        ISSN: 0022-4731            Impact factor:   4.292


  4 in total

1.  Immunological evidence for the identity between the hsp27 estrogen-regulated heat shock protein and the p29 estrogen receptor-associated protein in breast and endometrial cancer.

Authors:  D R Ciocca; E H Luque
Journal:  Breast Cancer Res Treat       Date:  1991-12       Impact factor: 4.872

2.  GTP analogues cause preferential translocation of an 18 kDa cytosolic G-protein to the membrane fraction in the ZR-75-1 human breast-cancer cell line.

Authors:  J Levy; R J King
Journal:  Biochem J       Date:  1990-10-01       Impact factor: 3.857

3.  The 29-kDa proteins phosphorylated in thrombin-activated human platelets are forms of the estrogen receptor-related 27-kDa heat shock protein.

Authors:  M E Mendelsohn; Y Zhu; S O'Neill
Journal:  Proc Natl Acad Sci U S A       Date:  1991-12-15       Impact factor: 11.205

4.  A 27 kDa heat shock protein that has anomalous prognostic powers in early and advanced breast cancer.

Authors:  S Love; R J King
Journal:  Br J Cancer       Date:  1994-04       Impact factor: 7.640

  4 in total

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