Criteria for effective zero-deforestation commitments

Zero-deforestation commitments are a type of voluntary sustainability initiative that companies adopt to signal their intention to reduce or eliminate deforestation associated with commodities that they produce, trade, and/or sell. Because each company defines its own zero-deforestation commitment goals and implementation mechanisms, commitment content varies widely. This creates challenges for the assessment of commitment implementation or effectiveness. Here, we develop criteria to assess the potential effectiveness of zero-deforestation commitments at reducing deforestation within a company supply chain, regionally, and globally. We apply these criteria to evaluate 52 zero-deforestation commitments made by companies identified by Forest 500 as having high deforestation risk. While our assessment indicates that existing commitments converge with several criteria for effectiveness, they fall short in a few key ways. First, they cover just a small share of the global market for deforestation-risk commodities, which means that their global impact is likely to be small. Second, biome-wide implementation is only achieved in the Brazilian Amazon. Outside this region, implementation occurs mainly through certification programs, which are not adopted by all producers and lack third-party near-real time deforestation monitoring. Additionally, around half of all commitments include zero-net deforestation targets and future implementation deadlines, both of which are design elements that may reduce effectiveness. Zero-net targets allow promises of future reforestation to compensate for current forest loss, while future implementation deadlines allow for preemptive clearing. To increase the likelihood that commitments will lead to reduced deforestation across all scales, more companies should adopt zero-gross deforestation targets with immediate implementation deadlines and clear sanction-based implementation mechanisms in biomes with high risk of forest to commodity conversion.ISSN:0959-3780ISSN:1872-949

One-Step Preservation of Phosphoproteins and Tissue Morphology at Room Temperature for Diagnostic and Research Specimens

BACKGROUND: There is an urgent need to measure phosphorylated cell signaling proteins in cancer tissue for the individualization of molecular targeted kinase inhibitor therapy. However, phosphoproteins fluctuate rapidly following tissue procurement. Snap-freezing preserves phosphoproteins, but is unavailable in most clinics and compromises diagnostic morphology. Formalin fixation preserves tissue histomorphology, but penetrates tissue slowly, and is unsuitable for stabilizing phosphoproteins. We originated and evaluated a novel one-step biomarker and histology preservative (BHP) chemistry that stabilizes signaling protein phosphorylation and retains formalin-like tissue histomorphology with equivalent immunohistochemistry in a single paraffin block. RESULTS: Total protein yield extracted from BHP-fixed, routine paraffin-embedded mouse liver was 100% compared to snap-frozen tissue. The abundance of 14 phosphorylated proteins was found to be stable over extended fixation times in BHP fixed paraffin embedded human colon mucosa. Compared to matched snap-frozen tissue, 8 phosphoproteins were equally preserved in mouse liver, while AMPKβ1 Ser108 was slightly elevated after BHP fixation. More than 25 tissues from mouse, cat and human specimens were evaluated for preservation of histomorphology. Selected tissues were evaluated in a multi-site, independent pathology review. Tissue fixed with BHP showed equivalent preservation of cytoplasmic and membrane cytomorphology, with significantly better nuclear chromatin preservation by BHP compared to formalin. Immunohistochemical staining of 13 non-phosphorylated proteins, including estrogen receptor alpha, progesterone receptor, Ki-67 and Her2, was equal to or stronger in BHP compared to formalin. BHP demonstrated significantly improved immunohistochemical detection of phosphorylated proteins ERK Thr202/Tyr204, GSK3-α/β Ser21/Ser9, p38-MAPK Thr180/Tyr182, eIF4G Ser1108 and Acetyl-CoA Carboxylase Ser79. CONCLUSION: In a single paraffin block BHP preserved the phosphorylation state of several signaling proteins at a level comparable to snap-freezing, while maintaining the full diagnostic immunohistochemical and histomorphologic detail of formalin fixation. This new tissue fixative has the potential to greatly facilitate personalized medicine, biobanking, and phospho-proteomic research

The role of private philanthropy in sustainability standards

Peer reviewe

Conceptualizing and measuring support for democracy : a new approach

Much of what we know about public support for democracy is based on survey questions about “democracy,” a term that varies in meaning across countries and likely prompts uncritically supportive responses. This paper proposes a new approach to measuring support for democracy. We develop a battery of 17 survey questions that cover all eight components of liberal democracy as defined by the V-Dem project. We then ask respondents from 19 national samples to evaluate these rights and institutions. We find considerable heterogeneity across countries in how our items cohere, especially in less developed contexts. Yet, those items that are more weakly connected with general support for liberal democracy tend to reveal the influence of political events and actors, arguably indicating weaknesses in political cultures. We further identify a concise subset of seven items that provide a reliable and valid measure of support for liberal democracy across our different samples

The Nature of the UC Double Bond: Pushing the Stability of High-Oxidation-State Uranium Carbenes to the Limit

Treatment of [K(BIPMMesH)] (BIPMMes={C(PPh 2NMes)2}2-; Mes=C6H 2-2,4,6-Me3) with [UCl4(thf)3] (1equiv) afforded [U(BIPMMesH)(Cl)3(thf)] (1), which generated [U(BIPMMes)(Cl)2(thf)2] (2), following treatment with benzyl potassium. Attempts to oxidise 2 resulted in intractable mixtures, ligand scrambling to give [U(BIPMMes) 2] or the formation of [U(BIPMMesH)(O)2(Cl) (thf)] (3). The complex [U(BIPMDipp)(μ-Cl)4(Li) 2(OEt2)(tmeda)] (4) (BIPMDipp={C(PPh 2NDipp)2}2-; Dipp=C6H 3-2,6-iPr2; tmeda=N,N,N′,N′- tetramethylethylenediamine) was prepared from [Li2(BIPM Dipp)(tmeda)] and [UCl4(thf)3] and, following reflux in toluene, could be isolated as [U(BIPMDipp)(Cl) 2(thf)2] (5). Treatment of 4 with iodine (0.5equiv) afforded [U(BIPMDipp)(Cl)2(μ-Cl)2(Li)(thf) 2] (6). Complex 6 resists oxidation, and treating 4 or 5 with N-oxides gives [{U(BIPMDippH)(O)2- (μ-Cl) 2Li(tmeda)] (7) and [{U(BIPMDippH)(O)2(μ-Cl) }2] (8). Treatment of 4 with tBuOLi (3equiv) and I2 (1equiv) gives [U(BIPMDipp)(OtBu)3(I)] (9), which represents an exceptionally rare example of a crystallographically authenticated uranium(VI)-carbon σ bond. Although 9 appears sterically saturated, it decomposes over time to give [U(BIPMDipp)(OtBu)3]. Complex 4 reacts with PhCOtBu and Ph2CO to form [U(BIPMDipp) (μ-Cl)4(Li)2(tmeda)(OCPhtBu)] (10) and [U(BIPM Dipp)(Cl)(μ-Cl)2(Li)(tmeda)(OCPh2)] (11). In contrast, complex 5 does not react with PhCOtBu and Ph2CO, which we attribute to steric blocking. However, complexes 5 and 6 react with PhCHO to afford (DippNPPh2)2C=C(H)Ph (12). Complex 9 does not react with PhCOtBu, Ph2CO or PhCHO; this is attributed to steric blocking. Theoretical calculations have enabled a qualitative bracketing of the extent of covalency in early-metal carbenes as a function of metal, oxidation state and the number of phosphanyl substituents, revealing modest covalent contributions to U=C double bonds. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim