The MADF-BESS Protein CP60 Is Recruited to Insulators via CP190 and Has Redundant Functions in .

Drosophila CP190 and CP60 are transcription factors that are associated with centrosomes during mitosis. CP190 is an essential transcription factor and preferentially binds to housekeeping gene promoters and insulators through interactions with architectural proteins, including Su(Hw) and dCTCF. CP60 belongs to a family of transcription factors that contain the N-terminal MADF domain and the C-terminal BESS domain, which is characterized by the ability to homodimerize.

The BEAF-32 Protein Directly Interacts with Z4/putzig and Chriz/Chromator Proteins in Drosophila melanogaster.

In Drosophila, the BEAF-32, Z4/putzig, and Chriz/Chromator proteins colocalize in the interbands of polytene chromosomes. It was assumed that these proteins can form a complex that affects the structure of chromatin. However, the mechanism of the formation of such a complex has not been studied.

The Chriz Protein Promotes the Recruitment of the Z4 Protein to the STAT-Dependent Promoters.

Proteins Z4/putzig and Chriz/Chromator are involved in the chromatin organization on the promoters of the majority of Drosophila genes. It was shown that the Chriz protein region from aa 273 to 503 is required for the interaction with the Z4 protein. Deletion of this sequence leads to derepression of a number of STAT-dependent genes and development of melanotic tumors in flies.

[Iron deficiency syndromes and their correction with nutritional support in elderly patients with colo-rectal cancer.].

51 patients with operated colorectal cancer T1N0M0, T3N1M0 and T4N0M1 at the age of 67±2,3 years receiving adjuvant chemotherapy and nutritional support (NS) were examined. Nutritional status was assessed using alimentazione-volume diagnosis to the points on L.N.

Studying Interactions between the Mod(mdg4)-67.2 Protein and Other Mod(mdg4) Isoforms in the Embryonic Cells of Drosophila melanogaster.

It is found that, in embryonic D. melanogaster cells, Mod(mdg4) protein isoforms can interact with each other through BTB domains. However, this nonspecific interaction is destroyed as a result of recruitment of protein complexes to the chromatin sites.