Asymmetrical radical formation in D- and L-alanines irradiated with yttrium-90β-rays

Radical formation in^{9 0}Y--irradiated D- and L-alanines was studied using ESR. It was observed that the relative radical concentration by -irradiation was distinguishably (13.9–21.5%) more in D-alanine than in L-alanine. Discussion was made on the possible mechanisms for the observed results.     

Enantiomeric cuparene-type sesquiterpenoids from Bazzania pompeana

Two enantiomeric cuparene-type sesquiterpenoids, (R)-(−)-cuparene (1) and (R)-(−)-δ-cuparenol (2), have been isolated from the liverwort, Bazzania pompeana. The structures and absolute configurations of the two compounds have been determined.     

Kinetic analysis of the polymerization process of actin.

The polymerization process of actin was examined by measuring the amount of flow birefringence and by analyzing release of labeled inorganic phosphate from the bound [gamma-32P]ATP upon polymerization of G-actin to F-actin. Comparison of the above experimental results with the electron microscopic data of Kawamura and Maruyama (J. Biochem., 67, 437-457, 1970) suggested that growth and redistribution steps occurred simultaneously during polymerization. Attempt was made to simulate the polymerization process of actin by calculating the kinetic equations numerically. The results of simulation suggested that it was necessary to take into consideration the association and dissociation between F-actin particles as well as the association and dissociation between F-actin and G-actin.     

Effects of rosuvastatin on electronegative LDL as characterized by capillary isotachophoresis: the ROSARY Study

Electronegative LDL, a charge-modified LDL (cm-LDL) subfraction that is more negatively charged than normal LDL, has been shown to be inflammatory. We previously showed that pravastatin and simvastatin reduced the electronegative LDL subfraction, fast-migrating LDL (fLDL), as analyzed by capillary isotachophoresis (cITP). The present study examined the effects of rosuvastatin on the more electronegative LDL subfraction, very-fast-migrating LDL (vfLDL), and small, dense charge-modified LDL (sd-cm-LDL) subfractions. Patients with hypercholesterolemia or those who were being treated with statins (n = 81) were treated with or switched to 2.5 mg/d rosuvastatin for 3 months. Rosuvastatin treatment effectively reduced cITP cm-LDL subfractions of LDL (vfLDL and fLDL) or sdLDL (sd-vfLDL and sd-fLDL), which were closely related to each other but were different from the normal subfraction of LDL [slow-migrating LDL (sLDL)] or sdLDL (sd-sLDL) in their relation to the levels of remnant-like particle cholesterol (RLP-C), apolipoprotein (apo) C-II, and apoE. The percent changes in cm-LDL or sd-cm-LDL caused by rosuvastatin were correlated with those in the particle concentrations of LDL or sdLDL measured as LDL-apoB or sdLDL-apoB and the levels of HDL-C, RLP-C, apoC-II, and apoE. In conclusion, rosuvastatin effectively reduced both the vfLDL subfraction and sd-cm-LDL subfractions as analyzed by cITP.     

Land-cover changes and distribution of wetland species in small valley habitats that developed in a Late Pleistocene middle terrace region

Wetlands Ecology and Management - Small valley topology on terraced uplands is a unique groundwater-dependent ecosystem in East Asia. Traditionally, this characteristic valley topology has been...     

Structure of the Atg12–Atg5 conjugate reveals a platform for stimulating Atg8–PE conjugation

Atg12 is conjugated to Atg5 through enzymatic reactions similar to ubiquitination. The Atg12–Atg5 conjugate functions as an E3‐like enzyme to promote lipidation of Atg8, whereas lipidated Atg8 has essential roles in both autophagosome formation and selective cargo recognition during autophagy. However, the molecular role of Atg12 modification in these processes has remained elusive. Here, we report the crystal structure of the Atg12–Atg5 conjugate. In addition to the isopeptide linkage, Atg12 forms hydrophobic and hydrophilic interactions with Atg5, thereby fixing its position on Atg5. Structural comparison with unmodified Atg5 and mutational analyses showed that Atg12 modification neither induces a conformational change in Atg5 nor creates a functionally important architecture. Rather, Atg12 functions as a binding module for Atg3, the E2 enzyme for Atg8, thus endowing Atg5 with the ability to interact with Atg3 to facilitate Atg8 lipidation.     

Synthesis and Binding Properties of Oligonucleotides Containing an Azobenzene Linker

Abstract

Incorporation of an azobenzene-4,4′-diamide group via a linker arm into the 3′-hydroxyl function of one oligonucleotide segment and the 5′-OH of other oligonucleotide has been described. The binding of the oligonucleotides containing the azobenzene linker was investigated by UV melting behaviors. The azobenzene linker has been shown to be useful as an effective bridge for stabilizing hairpin duplex and triplex.     

Comparison of the host-handling behavior of Eretmocerus mundus on Bemisia tabaci B biotype, Q biotype and Trialeurodes vaporariorum

Host-handling behaviors of Eretmocerus mundus (Mercet) (Hymenoptera: Aphelinidae) toward first to fourth instar nymphs of the Bemisia tabaci (Gennadius) (Homoptera: Aleyrodidae) B and Q biotypes and of Trialeurodes vaporariorum (Westwood) (Homoptera: Aleyrodidae) were compared under laboratory conditions. The host acceptance rates differed among host stages but not among host species or biotypes. In all host species and biotypes, the parasitoids stopped their host-handling behavior before oviposition more often with older hosts. The total host-handling time was longer for the fourth instars than for younger instars, mainly due to the longer oviposition times and probing times. E. mundus showed marking behavior for the B. tabaci B and Q biotypes, but not for T. vaporariorum. In conclusion, E. mundus could parasitize all whitefly biotypes and species used in this study, but both B. tabaci biotypes were more suitable hosts than T. vaporariorum. The younger instars were good oviposition targets in all hosts.