Andrzej K. Bednarek

TL;DR: Interestingly, the presence of WW domains in the structure of WWOX indicate the likelihood that this protein physically interacts with other proteins, and it is speculated that WWOX may span the yet uncharacterized common fragile site FRA16D region.

TL;DR: It is demonstrated that ectopic WWOX expression strongly inhibits anchorage-independent growth in soft agar of breast cancer cell lines MDA-MB-435 and T47D and suggests that abnormalities affecting this gene at the genomic and transcriptional level may be of relevance in carcinogenesis.

TL;DR: Serial analysis of gene expression on estrogen-responsive breast cancer cells after exposure to this hormone provides a comprehensive view of the changes induced by E2 on the transcriptional program of human E2-responsive cells, and identifies novel and previously unsuspected gene targets whose expression is affected by this hormone.

TL;DR: It is demonstrated, using peptides, that the arrayed domains retain their binding integrity and it is shown that the protein-domain chip can 'fish' proteins out of a total cell lysate; these domain-bound proteins can then be detected on the chip with a specific antibody, thus producing an interaction map for a cellular protein of interest.

TL;DR: It is demonstrated that WWOX contains a Group I WW domain that binds known cellular proteins containing the specific ligand PPXY and that endogenous WWOX and SIMPLE co-localize to perinuclear compartments of MCF-7 human breast cancer cells.