Record-High Thermoelectric Performance in Al-Doped ZnO via Anderson Localization of Band Edge States.

Oxides are of interest for thermoelectrics due to their high thermal stability, chemical inertness, low cost, and eco-friendly constituting elements. Here, adopting a unique synthesis route via chemical co-precipitation at strongly alkaline conditions, one of the highest thermoelectric performances for ZnO ceramics (  21.5 µW cm K and  0.

Measurement setup for Nernst and Seebeck effect at high temperatures and magnetic fields tested on elemental bismuth and full-Heusler compounds.

In this work, a measurement setup to study the Seebeck and Nernst effect at high temperatures and high magnetic fields is introduced and discussed. The measurement system allows for simultaneous measurements of both thermoelectric effects up to 700 K and magnetic fields up to 12 T. Based on theoretical concepts, measurement equations are derived that counteract constant spurious offset voltages and, therefore, inhibit systematic errors in the measurement setup.

High thermoelectric performance in metallic NiAu alloys via interband scattering.

Thermoelectric materials seamlessly convert thermal into electrical energy, making them promising for power generation and cooling applications. Although historically the thermoelectric effect was first discovered in metals, state-of-the-art research focuses on semiconductors. Here, we discover unprecedented thermoelectric performance in metals and realize ultrahigh power factors up to 34 mW m K in binary NiAu alloys, more than twice larger than in any bulk material above room temperature, reaching ∼ 0.

Local feedback mechanisms in human breast cancer.

Breast function and development are controlled by a variety of both local and systemic signals. Many of these signals are exerted by hormones and cytokines which are believed to be effectors in autoregulatory feedback loops. Recent studies have also suggested the involvement of such mechanisms in human breast cancer.

Dimerization of the insulin-like growth factor II/mannose 6-phosphate receptor.

The insulin-like growth factor II/mannose 6-phosphate receptor (IGF2R) interacts with lysosomal enzymes through two binding domains in its extracytoplasmic domain. We report in the accompanying article (Byrd, J. C.

Truncated forms of the insulin-like growth factor II (IGF-II)/mannose 6-phosphate receptor encompassing the IGF-II binding site: characterization of a point mutation that abolishes IGF-II binding.

Complete understanding of the functional significance of insulin-like growth factor II (IGF-II) binding by the IGF-II/mannose-6-phosphate (Man-6-P) receptor requires mapping and ultimately mutational analysis of the receptor's IGF-II binding domain. Recent advances have localized the IGF-II binding site to extracytoplasmic repeats 10-11. To improve resolution of the binding site map, a nested set of epitope-tagged, truncated forms of the human IGF-II/Man-6-P receptor were transiently expressed in COS-7 cells.

Localization of the insulin-like growth factor II (IGF-II) binding/cross-linking site of the IGF-II/mannose 6-phosphate receptor to extracellular repeats 10-11.

The insulin-like growth factor II (IGF-II) binding/cross-linking domain of the IGF-II/Man-6-P receptor was mapped by sequencing receptor fragments covalently attached to IGF-II. Rat placental or bovine liver receptors were purified by pentamannosyl-6-phosphate-Sepharose chromatography, affinity-labeled with 125I-IGF-II using disuccinimidyl tartrate, and digested with endoproteinase Glu-C. Analysis of small scale digests by gel electrophoresis revealed radiolabeled bands of approximately 17 kDa (rat) or approximately 18 kDa (bovine).