Shopping motivations, retail attributes, and retail format choice in a transitional market : evidence from Vietnam

The purpose of this two-phase, sequential mixed method study is to examine the impact of shopping motivations (utilitarian motivation and hedonic motivation), retail format attributes and demographics on the retail format choice of either a supermarket or a traditional market in a transitional Vietnamese economy. The first phase was a qualitative study which explored the link between shopping motivations and retail format attributes, using in-depth interviews with sixteenth shoppers in Hochiminh city. The reason for gathering qualitative data is to enable the researcher to develop the scale of shopping motivation constructs that is contextually relevant to Vietnam, taking into consideration its cultural backdrop and pace of economic development. This is because similar scales developed in a Western context might not be suitable in measuring and determining motivation constructs in Vietnam. The qualitative study aims to adjust and modify these scales as well as assist in discovering retail format attributes and determining demographics variables that might impact on Vietnamese shoppers’ choice retail format. Based on the findings from this qualitative study, combined with extensive, extant literature reviews, a second phase study was undertaken to develop two instruments. These instruments were used to survey consumers shopping mainly for two kinds of products for their households: non-food products and processed food products. The sample size for the non-food products study was 276 shoppers, and the sample size of the processed-food products study was 301 shoppers. The surveys were conducted in 24 districts of Hochiminh city. Logistic regression modeling was used to analyze the data. Results from the study indicated that shopping motivations (utilitarian motivation and hedonic motivation) impact significantly on retail format choice in a transitional, Vietnamese economy. In addition, “location” and “time convenience” were traditional market attributes that were strong predictors in shoppers’ choice of traditional markets. “Merchandise selection” was an important supermarket attribute in predicting shoppers’ choice of supermarkets. Finally, age and the average household income monthly of Vietnamese were found to be important predictors of retail format choice for only processed food products but not for non-food products

The SMAC mimetic LCL-161 selectively targets JAK2V617F mutant cells.

Background:Evasion from programmed cell death is a hallmark of cancer and can be achieved in cancer cells by overexpression of inhibitor of apoptosis proteins (IAPs). Second mitochondria-derived activator of caspases (SMAC) directly bind to IAPs and promote apoptosis; thus, SMAC mimetics have been investigated in a variety of cancer types. particularly in diseases with high inflammation and NFĸB activation. Given that elevated TNFα levels and NFĸB activation is a characteristic feature of myeloproliferative neoplasms (MPN), we investigated the effect of the SMAC mimetic LCL-161 on MPN cell survival in vitro and disease development in vivo. Methods:To investigate the effect of the SMAC mimetic LCL-161 in vitro, we utilized murine and human cell lines to perform cell viability assays as well as primary bone marrow from mice or humans with JAK2V617F-driven MPN to interrogate myeloid colony formation. To elucidate the effect of the SMAC mimetic LCL-161 in vivo, we treated a JAK2V617F-driven mouse model of MPN with LCL-161 then assessed blood counts, splenomegaly, and myelofibrosis. Results:We found that JAK2V617F-mutated cells are hypersensitive to the SMAC mimetic LCL-161 in the absence of exogenous TNFα. JAK2 kinase activity and NFĸB activation is required for JAK2V617F-mediated sensitivity to LCL-161, as JAK or NFĸB inhibitors diminished the differential sensitivity of JAK2V617F mutant cells to IAP inhibition. Finally, LCL-161 reduces splenomegaly and may reduce fibrosis in a mouse model of JAK2V617F-driven MPN. Conclusion:LCL-161 may be therapeutically useful in MPN, in particular when exogenous TNFα signaling is blocked. NFĸB activation is a characteristic feature of JAK2V617F mutant cells and this sensitizes them to SMAC mimetic induced killing even in the absence of TNFα. However, when exogenous TNFα is added, NFĸB is activated in both mutant and wild-type cells, abolishing the differential sensitivity. Moreover, JAK kinase activity is required for the differential sensitivity of JAK2V617F mutant cells, suggesting that the addition of JAK2 inhibitors to SMAC mimetics would detract from the ability of SMAC mimetics to selectively target JAK2V617F mutant cells. Instead, combination therapy with other agents that reduce inflammatory cytokines but preserve JAK2 signaling in mutant cells may be a more beneficial combination therapy in MPN

HAPPI-2: a Comprehensive and High-quality Map of Human Annotated and Predicted Protein Interactions

BACKGROUND: Human protein-protein interaction (PPI) data is essential to network and systems biology studies. PPI data can help biochemists hypothesize how proteins form complexes by binding to each other, how extracellular signals propagate through post-translational modification of de-activated signaling molecules, and how chemical reactions are coupled by enzymes involved in a complex biological process. Our capability to develop good public database resources for human PPI data has a direct impact on the quality of future research on genome biology and medicine. RESULTS: The database of Human Annotated and Predicted Protein Interactions (HAPPI) version 2.0 is a major update to the original HAPPI 1.0 database. It contains 2,922,202 unique protein-protein interactions (PPI) linked by 23,060 human proteins, making it the most comprehensive database covering human PPI data today. These PPIs contain both physical/direct interactions and high-quality functional/indirect interactions. Compared with the HAPPI 1.0 database release, HAPPI database version 2.0 (HAPPI-2) represents a 485% of human PPI data coverage increase and a 73% protein coverage increase. The revamped HAPPI web portal provides users with a friendly search, curation, and data retrieval interface, allowing them to retrieve human PPIs and available annotation information on the interaction type, interaction quality, interacting partner drug targeting data, and disease information. The updated HAPPI-2 can be freely accessed by Academic users at http://discovery.informatics.uab.edu/HAPPI . CONCLUSIONS: While the underlying data for HAPPI-2 are integrated from a diverse data sources, the new HAPPI-2 release represents a good balance between data coverage and data quality of human PPIs, making it ideally suited for network biology