Hall Effect and Resistivity in High-Tc Superconductors: The Conserving Approximation

The Hall coefficient (R_H) of high-Tc cuprates in the normal state shows the striking non-Fermi liquid behavior: R_H follows a Curie-Weiss type temperature dependence, and |R_H|>>1/|ne| at low temperatures in the under-doped compounds. Moreover, R_H is positive for hole-doped compounds and is negative for electron-doped ones, although each of them has a similar hole-like Fermi surface. In this paper, we give the explanation of this long-standing problem from the standpoint of the nearly antiferromagnetic (AF) Fermi liquid. We consider seriously the vertex corrections for the current which are indispensable to satisfy the conservation laws, which are violated within the conventional Boltzmann transport approximation. The obtained total current J_k takes an enhanced value and is no more perpendicular to the Fermi surface due to the strong AF fluctuations. By virtue of this mechanism, the anomalous behavior of R_H in high-Tc cuprates is neutrally explained. We find that both the temperature and the (electron, or hole) doping dependences of R_H in high-T_c cuprates are reproduced well by numerical calculations based on the fluctuation-exchange (FLEX) approximation, applied to the single-band Hubbard model. We also discuss the temperature dependence of R_H in other nearly AF metals, e.g., V_2O_3, kappa-BEDT-TTF organic superconductors, and heavy fermion systems close to the AF phase boundary.Comment: 19 pages, to appear in Phys. Rev. B, No.59, Vol.22, 199

Selective Phosphorylation Modulates the PIP2 Sensitivity of the CaM-SK Channel Complex

Phosphatidylinositol bisphosphate (PIP2) regulates the activities of many membrane proteins including ion channels through direct interactions. However, the affinity of PIP2 is so high for some channel proteins that its physiological role as a modulator has been questioned. Here we show that PIP2 is an important cofactor for activation of small conductance Ca2+-activated potassium channels (SK) by Ca2+-bound calmodulin (CaM). Removal of the endogenous PIP2 inhibits SK channels. The PIP2-binding site resides at the interface of CaM and the SK C-terminus. We further demonstrate that the affinity of PIP2 for its target proteins can be regulated by cellular signaling. Phosphorylation of CaM T79, located adjacent to the PIP2-binding site, by Casein Kinase 2 reduces the affinity of PIP2 for the CaM-SK channel complex by altering the dynamic interactions among amino acid residues surrounding the PIP2-binding site. This effect of CaM phosphorylation promotes greater channel inhibition by G-protein-mediated hydrolysis of PIP2

Wholesale pricing in a small open economy

This paper addresses the empirical analysis of wholesale profit margins using data of the Dutch wholesale sector, 1986. At the heart of the analysis is the typical nature of wholesale production: wholesalers do not produce a tangible product, but offer a service capacity. This has an immediate impact on the identification, interprelation and measurement of determinants of profit variations. A model is set up to explain variations in wholesale profit margins, which is inspired by two widely applied approaches to industry pricing: the behavioural mark-up model and the marginalist price-cost model