Mechanism of Redox-mediated Guanine Nucleotide Exchange on Redox-active Rho GTPases

How to Change the Redox Potential of Guanine?

Due to some important applications of guanine electrode in scientific and technology research such as electro-chemical DNA based biosensors, and a problem of high redox potential of guanine (0.81 V), our research study concentrates on reducing guanine redox potential by substituting Cu, Ag, Au, CH3, C2H5 and Cl on sites of 1, 2 and 9 of guanine. A 5.0% reduction...

Prognostic value of rho GTPases and rho guanine nucleotide dissociation inhibitors in human breast cancers.

PURPOSE Rho family members are small GTPases that are known to regulate malignant transformation and motility of cancer cells. The activities of Rhos are regulated by molecules such as guanine nucleotide dissociation inhibitors (GDIs). This study determined the levels of expression and the distribution of Rho-A, -B, -C, and -G, and Rho-6, -7, and -8, as well as Rho-GDI-beta, and Rho-GDI-gamma, ...

Nucleotide Exchange Factor Vav1 Regulates The Hemopoietic Rho/Rac Guanine

The Rho Family Guanine Nucleotide Exchange Factor Vav-2 Regulates the Development of Cell-Mediated Cytotoxicity

Previous pharmacologic and genetic studies have demonstrated a critical role for the low molecular weight GTP-binding protein RhoA in the regulation of cell-mediated killing by cytotoxic lymphocytes. However, a specific Rho family guanine nucleotide exchange factor (GEF) that activates this critical regulator of cellular cytotoxicity has not been identified. In this study, we provide evidence t...

Structural mechanism of disulphide bond - mediated redox

The oxidation of cysteine sulphydryl in proteins produces sulphenic acid that can form a reversible disulphide bond with another cysteine. The disulphide bond formation often triggers switches in protein structure and activity, especially when the distance between the two cysteine sulphur atoms is longer than the resulting disulphide bond distance. As an early example for the reversible disulph...