Gold‐Catalyzed C–S Aryl‐Group Transfer in Zinc Finger Proteins

Three Subfamilies of KRAB Zinc Finger Proteins

Natural and artificial zinc finger proteins

Zinc finger proteins acquire DNA-binding ability by Zn (II) complexation. In the zinc finger domain of the Cys2His2 type, each finger is approximately 30 amino acid residues long and consists of a simple ββα–fold stabilized by chelation of a zinc ion with the conserved Cys2His2 residues. A zinc finger motif of Cys2His2 offers an attractive framework for the design of a novel DNA-binding protein...

The Ikaros family of zinc-finger proteins

Ikaros represents a zinc-finger protein family important for lymphocyte development and certain other physiological processes. The number of family members is large, with alternative splicing producing various additional isoforms from each of the five homologous genes in the family. The functional forms of Ikaros proteins could be even more diverse due to protein-protein interactions readily es...

Zinc finger proteins as designer transcription factors.

Recent progress in the design and selection of novel zinc finger proteins with desired DNA binding specificities now allows construction of tailor-made DNA-binding proteins that specifically recognize almost any predetermined DNA sequence. Such novel or "designer" zinc finger proteins with desired DNA binding specificities can serve as efficient transcription factors in various mammalian cell l...

Advances in the Host Antiviral CCCH-Zinc Finger Proteins

Zinc-finger proteins (ZFPs) are the largest transcription factor family in human genome. They have recently become an area of intense study because of their broad range of biological functions, including development, differentiation, metabolism, autophagy, cancer progression and more recently because they are attractive targets for antiviral therapy [1]. The zinc fingers was first recognized as...