ABSTRACT
Low-carbon buildings (LCBs) are still in the early stages of development in China. The promotion and implementation of associated policies are not yet fully matured. Meanwhile, their status as public goods exacerbates the uncertainty and complexity regarding anticipated gains and potential losses. Few studies have explored the impact of perception parameters on the decision-making processes of LCBs' stakeholders. Thus, combined with prospect theory, this paper establishes a tripartite game model composed of governments, developers, and consumers to explore their interactions and influences in different stages. Real-life scenarios are further utilized to validate the effectiveness of the model in predicting the behaviors under respective preferences. The results show that the increase in subsidy and penalty intensity instead diminishes the enthusiasm for LCBs. More specifically, the existing subsidy policies offer limited incentives to consumers. With the addition of the perception parameter, there exist differences in the sensitivity of consumers and developers towards risk levels and potential losses. The findings also highlight the importance of consumers in the LCBs market. Future policies should encourage developers and consumers to jointly promote the LCBs implementation.
Subject(s)
Carbon , Emotions , China , Government , Policy , Game TheoryABSTRACT
Six pyrrolizidine alkaloids were isolated from the whole herb of Liparis nervosa together with two previously known ones. Their structures were elucidated by extensive spectroscopic analyses and chemical reactions. The cytotoxicity of the isolates was evaluated against A549, HepG2, and MCF-7 human cancer cell lines; however, no significant growth inhibition was observed. All compounds were evaluated for the inhibition of LPS-induced nitric oxide (NO) production in RAW264.7 macrophages, and most significantly inhibited NO production with IC50 values in the range of 2.16-38.25 µM.
Subject(s)
Lipopolysaccharides/antagonists & inhibitors , Macrophages/drug effects , Nitric Oxide/antagonists & inhibitors , Orchidaceae/chemistry , Pyrrolizidine Alkaloids/pharmacology , Animals , Cell Survival/drug effects , Dose-Response Relationship, Drug , Hep G2 Cells , Humans , Lipopolysaccharides/pharmacology , MCF-7 Cells , Macrophages/metabolism , Mice , Molecular Conformation , Nitric Oxide/biosynthesis , Pyrrolizidine Alkaloids/chemistry , Pyrrolizidine Alkaloids/isolation & purification , Structure-Activity Relationship , Tumor Cells, CulturedABSTRACT
Ten new nervogenic acid derivatives (1-4, 6-11) and one known compound (5) have been isolated from Liparis nervosa. Their structures were determined using extensive spectroscopic analysis, including 1D and 2D NMR experiments. Compounds 3, 4, 9, 10, and 11 were evaluated for their cytotoxicity against A549, H460, Hela, MCF-7, Caco2, and HepG2 human cancer cell lines.
Subject(s)
Antineoplastic Agents, Phytogenic/chemistry , Antineoplastic Agents, Phytogenic/pharmacology , Orchidaceae/chemistry , Caco-2 Cells/drug effects , Cell Line, Tumor , Disaccharides/chemistry , Drug Screening Assays, Antitumor , HeLa Cells/drug effects , Hemiterpenes/chemistry , Humans , Inhibitory Concentration 50 , Magnetic Resonance Spectroscopy , Molecular Structure , Parabens/chemistryABSTRACT
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ABSTRACT
The centrosymmetric mol-ecule of the title compound, [Zn(C(16)H(11)N(6))(2)(H(2)O)(2)], contains one Zn(2+) ion located on a center of symmetry, two 3-[4-(1H-imidazol-1-yl)phen-yl]-5-(pyridin-2-yl)-1H-1,2,4-triazol-1-ide (Ippyt) ligands and two coordinating water mol-ecules. The Zn(II) ion is six-coordinated in a distorted octa-hedral coordination geometry by four N atoms from two Ippyt ligands and by two O atoms from two water mol-ecules. Adjacent units are inter-connected though O-Hâ¯N hydrogen bonds, forming a three-dimensional network.
ABSTRACT
Mitochondrial DNA (mtDNA) is packaged into bacterial nucleoid-like structures, each containing several mtDNA molecules. The distribution of nucleoids during mitochondrial fission and fusion events and during cytokinesis is important to the segregation of mitochondrial genomes in heteroplasmic cells bearing a mixture of wild-type and mutant mtDNA molecules. We report fractionation of HeLa cell mtDNA nucleoids into two subsets of complexes that differ in their sedimentation velocity and their association with cytoskeletal proteins. Pulse labeling studies indicated that newly replicated mtDNA molecules are evenly represented in the rapidly and slowly sedimenting fractions. Slowly sedimenting nucleoids were immunoaffinity purified using antibodies to either of two abundant mtDNA-binding proteins, TFAM or mtSSB. These two different immunoaffinity procedures yielded very similar sets of proteins, with 21 proteins in common, including most of the proteins previously shown to play roles in mtDNA replication and transcription. In addition to previously identified mitochondrial proteins, multiple peptides were observed for one novel DNA metabolic protein, the DEAH-box helicase DHX30. Antibodies raised against a recombinant fragment of this protein confirmed the mitochondrial localization of a specific isoform of DHX30.
Subject(s)
DNA, Mitochondrial/genetics , Mitochondria/metabolism , Mitochondrial Membranes/metabolism , Amino Acid Sequence , Animals , HeLa Cells , Humans , Mitochondrial Proteins/chemistry , Molecular Chaperones/metabolism , Molecular Sequence Data , Protein Binding , Protein Folding , Protein IsoformsABSTRACT
Mitochondrial DNA (mtDNA) is not packaged in nucleosomal particles, but has been reported to associate with the mitochondrial inner membrane. Gentle lysis of Xenopus oocyte mitochondria with nonionic detergent liberates a nucleoprotein complex containing mtDNA associated with a previously characterized DNA binding partner, mitochondrial transcription factor A (mtTFA), as well as a series of inner membrane proteins identified by sequencing. More extensive detergent treatment stripped most of these proteins from the DNA, leaving a limited number of proteins in a nucleoid core. Sequencing of the major proteins retained in association with mtDNA revealed the expected mtDNA binding proteins, mtTFA and mitochondrial single-stranded DNA binding protein (mtSSB), as well as four proteins not previously reported to associate with mtDNA. These include adenine nucleotide translocator 1, the lipoyl-containing E2 subunits of pyruvate dehydrogenase and branched chain alpha-ketoacid dehydrogenase and prohibitin 2. The association of several of these proteins with mtTFA-containing mtDNA nucleoids was confirmed by immunoprecipitation.
Subject(s)
DNA, Mitochondrial/metabolism , DNA-Binding Proteins/metabolism , Mitochondria/metabolism , Mitochondrial Proteins/metabolism , 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)/metabolism , Adenine Nucleotide Translocator 1/metabolism , Animals , Dihydrolipoyllysine-Residue Acetyltransferase/metabolism , Female , Intracellular Membranes/metabolism , Oocytes/metabolism , Prohibitins , Repressor Proteins/metabolism , Transcription Factors/metabolism , Xenopus Proteins , Xenopus laevisABSTRACT
Phage HK022 Nun protein excludes phage lambda by binding nascent lambda-nut RNA and inducing termination and transcript release. In contrast, in a purified in vitro system, Nun arrests transcription on lambdaDNA templates without dissociation of the transcription elongation complex (TEC). Our evidence indicates that transcription-repair coupling factor (Mfd) frees Nun-arrested RNA polymerase. The activity of Nun is enhanced in an mfd-null mutant, consistent with prolonged association of Nun with the TEC. Furthermore, expression of lambda nut RNA in the mfd mutant titrates Nun, allowing superinfecting lambda to form plaques. Finally, addition of Mfd releases a Nun-arrested transcription complex in vitro.
