New records of ichneumon wasps (Hymenoptera, Ichneumonidae) from Malta

Recently some Maltese Hymenoptera were donated to the Hungarian Natural History Museum (HNHM) and some other material was sent to the Natural History Museum in London (BMNH) for identification by the second author. Amongst these specimens were six ichneumon wasp species new to the fauna of Malta. Ichneumonidae taxonomy and nomenclature follow Yu et al. (2012), and host records were traced through this resource. Identifications were based on keys provided by Szépligeti (1905), Schmiedeknecht (1909), Bajári (1960), Townes et al. (1965), Bajári & Móczár (1969), Townes (1969; 1970a; 1970b; 1971), Horstmann (1976), Gauld & Mitchell (1977), Fitton et al. (1988), Wahl (1993), and Tolkanitz (2007). The voucher specimens are deposited in the Hymenoptera Collection of HNHM, Budapest, Hungary (those indicated by a HNHM id. number below), and some duplicate specimens in D. Mifsud’s private insect collection (CDM) in Malta.peer-reviewe

Some Systems Studies of the Innovation Process (Research- Development-Introduction)

This working paper consists of extracts from research studies of the innovation process, development and introduction, undertaken in the USSR, Hungary and the US$.. They were selected and abstracted by Gennady Dobrov, Peter Vas Zoltan and Robert Randolph as part of their general research on the science of policy analysis. Since these studies are not generally accessible, it has seemed worthwhile to make them available to collaborators in the IIASA Innovation Task, and others, in the form of a working paper. We are grateful to Kan Chen, Vladimir Pokrovsky and Edward Roberts for permission to reproduce their material

Effect of chromatic mechanisms on the detection of mesopic incremental targets at different eccentricities

Spectral sensitivity functions for the threshold detection of mesopic incremental targets were compared for different target eccentricities (10, 20, and 30�) and for different mesopic backgrounds (0.1, 0.5 and 1.0 cd m)2). Relative responsivities of achromatic mechanisms (L + M and rods) and chromatic mechanisms (S and |L–M|) were estimated for each eccentricity and background. Chromatic mechanisms contribute significantly to detection but their effect is lower at 30�. A new contrast metric (CCHC2) is introduced to account for the selective adaptation of the photoreceptors and the effects of the chromatic mechanisms i.e. broadening of the range of spectral sensitivity with multiple local maxima and yellow sub-additivity of detection performance. The CCHC2 metric is compared with the achromatic contrast metric of the MOVE model (CMOVE). For the same target, CCHC2 generally predicts a higher visibility level than CMOVE. However, in accordance with visual observations, for grey or yellowish incremental targets appearing at the eccentricities of 20 and 30�, the visibility predicted by CCHC2 is less than the visibility predicted by CMOVE

Importance of Aspartate Residues in Balancing the Flexibility and Fine-Tuning the Catalysis of Human 3‑Phosphoglycerate Kinase

The exact role of the metal ion, usually Mg²⁺, in the catalysis of human 3-phosphoglycerate kinase, a well-studied two-domain enzyme, has not been clarified. Here we have prepared single and double alanine mutants of the potential metal-binding residues, D374 and D218. While all mutations weaken the catalytic interactions with Mg²⁺, they surprisingly strengthen binding of both MgADP and MgATP, and the effects are even more pronounced for ADP and ATP. Thermodynamic parameters of binding indicate an increase in the binding entropy as a reason for the strengthening. In agreement with the experimental results, computer-simulated annealing calculations for the complexes of these mutants have supported the mobility of the nucleotide phosphates and, as a consequence, formation of their new interaction(s) within the active site. A similar type of mobility is suggested to be a characteristic feature of the nucleotide site of the wild-type enzyme, too, both in its inactive open conformation and in the active closed conformation. This mobility of the nucleotide phosphates that is regulated by the aspartate side chains of D218 and D374 through the complexing Mg²⁺ is suggested to be essential in enzyme function