A Multi-Agent-Based System for eProcurement

E-procurement has become an important function of enterprise information systems. The process of e-procurement includes automatic definition of product requirements, search and selection for suppliers, negotiation and contracting with suppliers. In this paper, we propose a novel agentbased architecture for e-procurement system, in which various agents take such responsibilities as negotiating and contracting. Moreover, the architecture that we propose can monitor transaction status and enhance the flexibility to handle unexpected exceptions, thus leading to agile procurement management

2-Amino-4-(2,4-dichloro­phen­yl)-6-(naphthalen-1-yl)nicotinonitrile

In the crystal structure of the title compound, C22H13Cl2N3, the mol­ecules are connected via inter­molecular C—H⋯N and N—H⋯N hydrogen bonds, forming a three-dimensional network. The dihedral angles between naphthyl ring system and the pyridyl and benzene rings are 55.04 (7) and 75.87 (7)°, respectively, whereas the pyridyl and benzene rings are oriented at a dihedral angle of 59.56 (8)°

Methyl 2-{[2,8-bis­(trifluoro­meth­yl)quinolin-4-yl]­oxy}acetate

In the crystal structure of the title compound, C14H9F6NO3, mol­ecules are connected by inter­molecular C—H⋯O hydrogen bonds. The best planes through the benzene and pyridyl rings make a dihedral angle of 1.59 (12)°

2-Chloro-5-(chloro­meth­yl)pyridine

The title compound, C6H5Cl2N, is almost planar, with an r.m.s. deviation of 0.0146 Å for all atoms except for the 5-choloromethyl Cl atom. The offset Cl atom lies above this plane with a Cl—C—C angle of 111.11 (17)°. In the crystal, mol­ecules are connected via inter­molecular C—H⋯N hydrogen bonds, forming dimers

Assessment of plasma B7-H3 levels in pediatric patients with different degrees of surgical stress

Background: Surgical stress initiates a series of host hormone, metabolism and immune responses, which predominantly affect the homeostatic mechanism of patients with major surgery. B7-H3 is a co-stimulatory molecule and has been shown to participate in both adaptive and innate immune responses. In this study we evaluated the clinical significance of plasma B7-H3 levels in pediatric patients with different types of operation and degrees of surgical stress. Methods: A total of 48 children received pediatric general and cardiac surgery were recruited into this study. Based on the surgical stress scoring, children were divided into moderate stress (n?=?14) and severe stress (n?=?34) groups. Plasma B7-H3 levels were assessed at selected time points: before surgery, immediately after surgery, at day 1, day 3, and day 7 after surgery. Correlations between plasma B7-H3 levels and surgical stress scores were also examined. Results: Plasma B7-H3 levels were significantly decreased in all 48 pediatric patients after surgery compared to the B7-H3 level before surgery (p?<?0.01). Children with general surgery showed significant decreases in plasma B7-H3 immediately after surgery, and at day 3 and day 7 after surgery (p?<?0.05, p?<?0.01), whereas children with cardiac surgery showed reduced plasma B7-H3 immediately after surgery and at day 3 after surgery (p?<?0.05). Plasma B7-H3 in cardiac surgery group was dropped much lower than that in general surgery group at day 1 (p?<?0.05) and day 3 (p?<?0.01) after surgery. Significantly reduced plasma B7-H3 was observed in the severe stress group, but not in the moderate stress group, immediately after surgery and at day 3 after surgery (p?<?0.05), and severe stress group had significantly lower plasma B7-H3 levels than moderate stress group at day 1, day 3, and day 7 after surgery (p?<?0.05). Furthermore, plasma B7-H3 levels at day 1 (p?=?0.01) and day 3 (p?=?0.025) after surgery correlated negatively with surgical stress scores. Conclusions: Plasma B7-H3 levels were decreased significantly in children subjected to pediatric general and cardiac surgery, which is closely associated with the severity of surgical stress. The negative correlation of plasma B7-H3 levels at day 1 and day 3 after surgery with surgical stress scoring implicates that the plasma B7-H3 level might be a useful biomarker for monitoring stress intensity during pediatric surgery

A simple way to fine tune the redox potentials of cobalt ions encapsulated in nitrogen doped graphene molecular catalysts for the oxygen evolution reaction

Co2+ ions encapsulated in nitrogen doped graphene were applied as an oxygen evolution catalyst. Their redox potentials were tuned using different counter anions as liable ligands, and the redox potential related catalytic rates were explored. It was proposed that the electron density of Co2+ ions was a general descriptor for activity

Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin inhibits the proliferation of ARPE-19 cells

<p>Abstract</p> <p>Background</p> <p>The antiproliferative effect of the Hsp90 inhibitor 17-AAG (17-allylamino-17-demethoxygeldanamycin) on human retinal pigment epithelial cells is investigated.</p> <p>Methods</p> <p>MTT and flow cytometry were used to study the antiproliferative effects of the 17-AAG treatment of ARPE-19 cells. 2D gel electrophoresis (2-DE) and mass spectrometry were applied to detect the altered expression of proteins, which was verified by real-time PCR. Gene Ontology analysis and Ingenuity Pathway Analysis (IPA) were utilized to analyze the signaling pathways, cellular location, function, and network connections of the identified proteins. And SOD assay was employed to confirm the analysis.</p> <p>Results</p> <p>17-AAG suppressed the proliferation of ARPE-19 cells by inducing cell cycle arrest and apoptosis. Proteomic analysis revealed that the expression of 94 proteins was altered by a factor of more than 1.5 following exposure to 17-AAG. Of these 94, 87 proteins were identified. Real-time PCR results indicated that Hsp90 and Hsp70, which were not identified by proteomic analysis, were both upregulated upon 17-AAG treatment. IPA revealed that most of the proteins have functions that are related to oxidative stress, as verified by SOD assay, while canonical pathway analysis revealed glycolysis/gluconeogenesis.</p> <p>Conclusions</p> <p>17-AAG suppressed the proliferation of ARPE-19 cells by inducing cell cycle arrest and apoptosis, and possibly by oxidative stress.</p

Structures of the N-Terminal and Middle Domains of E. coli Hsp90 and Conformation Changes upon ADP Binding

Hsp90 is an abundant molecular chaperone involved in many biological systems. We report here the crystal structures of the unliganded and ADP bound fragments containing the N-terminal and middle domains of HtpG, an E. coli Hsp90. These domains are not connected through a flexible linker, as often portrayed in models, but are intimately associated with one another. The individual HtpG domains have similar folding to those of DNA gyrase B but assemble differently, suggesting somewhat different mechanisms for the ATPase superfamily. ADP binds to a subpocket of a large site that is jointly formed by the N-terminal and middle domains and induces conformational changes of the N-terminal domain. We speculate that this large pocket serves as a putative site for binding of client proteins/cochaperones. Modeling shows that ATP is not exposed to the molecular surface, thus implying that ATP activation of hsp90 chaperone activities is accomplished via conformational changes