Design and analysis of the green climate fund

The Green Climate Fund （GCF） has been one of the core issues of the world climate summits under the United Nations Framework Convention on Climate Change （UNFCCC） in recent years. However, the GCF has not progressed smoothly, and currently there are no satisfactory schemes for raising and distributing the fund. This paper first discusses how to finance the GCF among Annex II countries. It introduces the ＇preference score compromises＇ （PSC） approach which is based on environmental responsibility and economic capacity, with historical emissions as an indicator for environmental responsibility and GDP as indicator for economic capacity. The results show that the United States and the European Union are the two largest contributors to the GCF, sponsoring more than 80% of the funds. Second, we discuss how to allocate the funds among non-Annex II parties. The ＇adaptation needs＇ （AN） approach, which takes account of economic strength and climate damages, is proposed to achieve the adaptation purpose of the GCF, and the results reveal that African countries with high levels of climate vulnerability could get most funds, with a share of almost 30%. Regarding the mitigation purpose of the GCF, this research introduces two approaches： the ＇carbon reduction contribution＇ （CC） approach and the ＇incremental cost＇ （IC） approach. Both approaches could achieve significant reductions in carbon emissions in non-Annex II parties, whereas the latter may provide limited adaptation finance but result in more mitigation effects. This paper also develops a method to combine abatement efficiency and adaptation fairness of the GCF, and we find that with an equal split between the AN and CC （or AN and IC） approaches, the amount of USD 100 billion could finance an emissions reduction of 1613 MtCO2 （2477 MtCO2）, while allocating USD 16 （or USD 9） per capita for adaptation in non-Annex II parties. The schemes proposed may be useful for promoting the development of the GCF in the future.     

Anderson localization of a non-interacting Bose-Einstein condensate

Anderson localization of waves in disordered media was originally predicted fifty years ago, in the context of transport of electrons in crystals. The phenomenon is much more general and has been observed in a variety of systems, including light waves. However, Anderson localization has not been observed directly for matter waves. Owing to the high degree of control over most of the system parameters (in particular the interaction strength), ultracold atoms offer opportunities for the study of disorder-induced localization. Here we use a non-interacting Bose-Einstein condensate to study Anderson localization. The experiment is performed with a one-dimensional quasi-periodic lattice-a system that features a crossover between extended and exponentially localized states, as in the case of purely random disorder in higher dimensions. Localization is clearly demonstrated through investigations of the transport properties and spatial and momentum distributions. We characterize the crossover, finding that the critical disorder strength scales with the tunnelling energy of the atoms in the lattice. This controllable system may be used to investigate the interplay of disorder and interaction (ref. 7 and references therein), and to explore exotic quantum phases.     

Phosphorylation of p27BBP/eIF6 and its association with the cytoskeleton are developmentally regulated in Xenopus oogenesis

p27^BBP/eIF6 is an evolutionarily conserved regulator of ribosomal function. It is necessary for 60S biogenesis and impedes improper joining of 40S and 60S subunits, regulated by protein kinase C or Efl1p. No data on p27^BBP/eIF6 during early development of Metazoa are available. We studied the distribution, post-translational changes and association with the cytoskeleton of p27^BBP/ eIF6 during Xenopus oogenesis and early development. Results indicate that p27^BBP/eIF6 is present throughout oogenesis, partly associated with 60S subunits, partly free and with little cytoskeleton bound. During prophase I, p27^BBP/eIF6 is detected as a single band of 27-kDa. Upon maturation induced by progesterone or protein kinase C, a serine-phosphorylated 29 kDa isoform appears and is kept throughout development to the neurula stage. Confocal microscopy showed that the distribution of p27^BBP/eIF6 and its association with the cytoskeleton varies according to oogenesis stages. Briefly, in stage 6 oocytes, p27^BBP/eIF6 has a limited dot-like distribution, and does not co-localize with cytokeratin, whereas upon maturation it spreads throughout the cytoplasm. After fertilization, a large fraction coalesces around cytomembranes and a cytochalasin B-sensitive co-localization with cytokeratin occurs. RNAse removes p27^BBP/eIF6 from the cytokeratin fibres. Developmental data suggest a role of p27^BBP/eIF6 in controlling ribosomal availability or regulating cross-talk between ribosomes and the cytoskeleton.Received 7 April 2005; received after revision 11 May 2005; accepted 25 May 2005R. Carotenuto and N. De Marco contributed equally to the paper     

The oxidation of cystamine and other sulfur-diamines by diamine-oxidase preparations

Riassunto Le diamine solforate cistamina e lantionamina sono ossidate con velocità comparabile a quella della cadaverina dalla diamino-ossidasi. Il solfone della lantionamina è ossidato più lentamente ed il disolfossido della cistamina non è ossidato affatto. Benchè dall'ossidazione della cistamina si produca una mole di ammoniaca per mole di substrato, il consumo di ossigeno è due volte più elevato del teorico, indicante una ulteriore ossidazione del prodotto metabolico della reazione. Tuttavia taurina, ipotaurina e solfati, non sono determinabili nel deproteinizzato finale.     

Structure and evolution of vertebrate aldehyde oxidases: from gene duplication to gene suppression

Aldehyde oxidases (AOXs) and xanthine dehydrogenases (XDHs) belong to the family of molybdo-flavoenzymes. Although AOXs are not identifiable in fungi, these enzymes are represented in certain protists and the majority of plants and vertebrates. The physiological functions and substrates of AOXs are unknown. Nevertheless, AOXs are major drug metabolizing enzymes, oxidizing a wide range of aromatic aldehydes and heterocyclic compounds of medical/toxicological importance. Using genome sequencing data, we predict the structures of AOX genes and pseudogenes, reconstructing their evolution. Fishes are the most primitive organisms with an AOX gene (AOXα), originating from the duplication of an ancestral XDH. Further evolution of fishes resulted in the duplication of AOXα into AOXβ and successive pseudogenization of AOXα. AOXβ is maintained in amphibians and it is the likely precursors of reptilian, avian, and mammalian AOX1. Amphibian AOXγ is a duplication of AOXβ and the likely ancestor of reptilian and avian AOX2, which, in turn, gave rise to mammalian AOX3L1. Subsequent gene duplications generated the two mammalian genes, AOX3 and AOX4. The evolution of mammalian AOX genes is dominated by pseudogenization and deletion events. Our analysis is relevant from a structural point of view, as it provides information on the residues characterizing the three domains of each mammalian AOX isoenzyme. We cloned the cDNAs encoding the AOX proteins of guinea pig and cynomolgus monkeys, two unique species as to the evolution of this enzyme family. We identify chimeric RNAs from the human AOX3 and AOX3L1 pseudogenes with potential to encode a novel microRNA.