Tohoku University

About: Tohoku University is a education organization based out in Sendai, Japan. It is known for research contribution in the topics: Magnetization & Alloy. The organization has 72116 authors who have published 170791 publications receiving 3941714 citations. The organization is also known as: Tōhoku daigaku.

Thermodynamic properties of a spin-1/2 spin-liquid state in a κ -type organic salt

Abstract: Spins in a two-dimensional triangular lattice are geometrically frustrated and cannot form an ordered ground state. Instead, a spin-liquid state is expected, and now thermodynamic measurements suggest that a spin liquid exists down to the lowest temperatures. In two-dimensional triangular lattices, geometric frustration prohibits the formation of ordering even at the lowest temperatures, and therefore a liquid-like ground state is expected. The spin-liquid problem has been one of the central topics of condensed-matter science for more than 30 yr in relation to the resonating-valence-bond model1. One of the characteristic features proposed is the existence of a linear temperature-dependent contribution to the heat capacity, as the degeneracy of the energy states should give rise to gapless excitations. Here, we show thermodynamic evidence for the realization of a spin-liquid ground state through a single-crystal calorimetric study of the dimer-based organic charge-transfer salt κ-(BEDT-TTF)2Cu2(CN)3, with a triangular lattice structure down to 75 mK. In addition, we report an unexpected hump structure in the heat capacity around 6 K, which may indicate a crossover into the quantum spin liquid.

Global patterns of leaf mechanical properties

Abstract: Leaf mechanical properties strongly influence leaf lifespan, plant-herbivore interactions, litter decomposition and nutrient cycling, but global patterns in their interspecific variation and underlying mechanisms remain poorly understood. We synthesize data across the three major measurement methods, permitting the first global analyses of leaf mechanics and associated traits, for 2819 species from 90 sites worldwide. Key measures of leaf mechanical resistance varied c. 500-800-fold among species. Contrary to a long-standing hypothesis, tropical leaves were not mechanically more resistant than temperate leaves. Leaf mechanical resistance was modestly related to rainfall and local light environment. By partitioning leaf mechanical resistance into three different components we discovered that toughness per density contributed a surprisingly large fraction to variation in mechanical resistance, larger than the fractions contributed by lamina thickness and tissue density. Higher toughness per density was associated with long leaf lifespan especially in forest understory. Seldom appreciated in the past, toughness per density is a key factor in leaf mechanical resistance, which itself influences plant-animal interactions and ecosystem functions across the globe.

Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins

Abstract: TRANSCRIPTION factor NF-E2 is crucial for regulating erythroid-specific gene expression1. Cloning of the NF-E2 p45 protein has revealed that it contains a basic region–leucine zipper (b-zip) domain which associates with another unidentified protein (of relative molecular mass 18,000) to form functional NF-E2 (ref. 2). We show here that products of the maf proto-oncogene family3–5, MafF, MafG and MafK (the small Maf proteins) which possess a b-zip DNA-binding domain but lack a canonical transactivation domain3, directly control the DNA-binding properties of p45 by heterodimeric association with p45. Whereas homodimers of the small Maf proteins act as negative regulators, heterodimers composed of Maf and p45 support active transcription in vivo. These results indicate that one (or all) of the small Maf proteins is the second constituent chain required for NF-E2 activity, and that negative as well as positive regulation can be achieved through an NF-E2 site, depending on the equilibrium concentrations of p45 and the Maf proteins inside erythroid cells.