The Experts below are selected from a list of 6156 Experts worldwide ranked by ideXlab platform
S. Y.y. Lo - One of the best experts on this subject based on the ideXlab platform.
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development of an rfid based Sushi management system the case of a conveyor belt Sushi restaurant
International Journal of Production Economics, 2008Co-Authors: Eric W T Ngai, S. Y.y. LoAbstract:We describe the design and development of a radio-frequency identification (RFID)-based Sushi management (RFSM) system in a conveyor-belt Sushi restaurant to enhance operational efficiency. The system is designed to help a conveyor-belt Sushi restaurant to achieve better inventory control, responsive replenishment, and food safety control, as well as to improve its quality of service. This study demonstrates the significance and benefits of using RFID technology specifically in the food industry. The lessons learned from this effort help to support and further the academic and practitioner literature, especially in the area of RFID systems development. Finally, we address the limitations of this study and several areas of future development.
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Development of an RFID-based Sushi management system: The case of a conveyor-belt Sushi restaurant
International Journal of Production Economics, 2008Co-Authors: Eric W T Ngai, F. F.c. Suk, S. Y.y. LoAbstract:We describe the design and development of a radio-frequency identification (RFID)-based Sushi management (RFSM) system in a conveyor-belt Sushi restaurant to enhance operational efficiency. The system is designed to help a conveyor-belt Sushi restaurant to achieve better inventory control, responsive replenishment, and food safety control, as well as to improve its quality of service. This study demonstrates the significance and benefits of using RFID technology specifically in the food industry. The lessons learned from this effort help to support and further the academic and practitioner literature, especially in the area of RFID systems development. Finally, we address the limitations of this study and several areas of future development. © 2007 Elsevier B.V. All rights reserved.
Eric W T Ngai - One of the best experts on this subject based on the ideXlab platform.
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development of an rfid based Sushi management system the case of a conveyor belt Sushi restaurant
International Journal of Production Economics, 2008Co-Authors: Eric W T Ngai, S. Y.y. LoAbstract:We describe the design and development of a radio-frequency identification (RFID)-based Sushi management (RFSM) system in a conveyor-belt Sushi restaurant to enhance operational efficiency. The system is designed to help a conveyor-belt Sushi restaurant to achieve better inventory control, responsive replenishment, and food safety control, as well as to improve its quality of service. This study demonstrates the significance and benefits of using RFID technology specifically in the food industry. The lessons learned from this effort help to support and further the academic and practitioner literature, especially in the area of RFID systems development. Finally, we address the limitations of this study and several areas of future development.
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Development of an RFID-based Sushi management system: The case of a conveyor-belt Sushi restaurant
International Journal of Production Economics, 2008Co-Authors: Eric W T Ngai, F. F.c. Suk, S. Y.y. LoAbstract:We describe the design and development of a radio-frequency identification (RFID)-based Sushi management (RFSM) system in a conveyor-belt Sushi restaurant to enhance operational efficiency. The system is designed to help a conveyor-belt Sushi restaurant to achieve better inventory control, responsive replenishment, and food safety control, as well as to improve its quality of service. This study demonstrates the significance and benefits of using RFID technology specifically in the food industry. The lessons learned from this effort help to support and further the academic and practitioner literature, especially in the area of RFID systems development. Finally, we address the limitations of this study and several areas of future development. © 2007 Elsevier B.V. All rights reserved.
Yannick Jacques - One of the best experts on this subject based on the ideXlab platform.
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soluble interleukin 15 receptor α il 15rα Sushi as a selective and potent agonist of il 15 action through il 15rβ γ hyperagonist il 15 il 15rα fusion proteins
Journal of Biological Chemistry, 2006Co-Authors: Erwan Mortier, Agnes Quemener, Patricia Vusio, Inken Lorenzen, Yvan Boublik, Joachim Grotzinger, Ariane Plet, Yannick JacquesAbstract:Abstract Interleukin-15 (IL-15) is crucial for the generation of multiple lymphocyte subsets (natural killer (NK), NK-T cells, and memory CD8 T cells), and transpresentation of IL-15 by monocytes and dendritic cells has been suggested to be the dominant activating process of these lymphocytes. We have previously shown that a natural soluble form of IL-15Rα chain corresponding to the entire extracellular domain of IL-15Rα behaves as a high affinity IL-15 antagonist. In sharp contrast with this finding, we demonstrate in this report that a recombinant, soluble Sushi domain of IL-15Rα, which bears most of the binding affinity for IL-15, behaves as a potent IL-15 agonist by enhancing its binding and biological effects (proliferation and protection from apoptosis) through the IL-15Rβ/γ heterodimer, whereas it does not affect IL-15 binding and function of the tripartite IL-15Rα/β/γ membrane receptor. Our results suggest that, if naturally produced, such soluble Sushi domains might be involved in the IL-15 transpresentation mechanism. Fusion proteins (RLI and ILR), in which IL-15 and IL-15Rα-Sushi are attached by a flexible linker, are even more potent than the combination of IL-15 plus sIL-15Rα-Sushi. After binding to IL-15Rβ/γ, RLI is internalized and induces a biological response very similar to the IL-15 high affinity response. Such hyper-IL-15 fusion proteins appear to constitute potent adjuvants for the expansion of lymphocyte subsets.
J Ding - One of the best experts on this subject based on the ideXlab platform.
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atomic force microscopy study of the antimicrobial action of Sushi peptides on gram negative bacteria
Biochimica et Biophysica Acta, 2007Co-Authors: Ang Li, Bow Ho, J DingAbstract:The antibacterial effect of the endotoxin-binding Sushi peptides against Gram-negative bacteria (GNB) is investigated in this study. Similar characteristics observed for Atomic force microscopy (AFM) images of peptide-treated Escherichia coli and Pseudomonas aeruginosa suggest that the Sushi peptides (S3) evoke comparable mechanism of action against different strains of GNB. The results also indicate that the Sushi peptides appear to act in three stages: damage of the bacterial outer membrane, permeabilization of the inner membrane and disintegration of both membranes. The AFM approach has provided vivid and detailed close-up images of the GNB undergoing various stages of antimicrobial peptide actions at the nanometer scale. The AFM results support our hypothesis that the S3 peptide perturbs the GNB membrane via the “carpet-model” and thus, provide important insights into their antimicrobial mechanisms.
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the specificity of Sushi peptides for endotoxin and anionic phospholipids potential application of popg as an adjuvant for anti lps strategies
Biochemical Society Transactions, 2006Co-Authors: Peng Li, Bow Ho, J DingAbstract:Sushi peptides [S1 (Sushi 1 peptide) and S3] are derived from the LPS (lipopolysaccharide; also known as endotoxin)-binding domains of an LPS-sensitive serine protease, Factor C, from the horseshoe crab (Carcinoscorpius rotundicauda). S1 and S3 interact at high affinity with LPS. The intermolecular disulphide bonding in the S3 dimer is indispensable for its LPS binding, disruption and consequent neutralization. Simultaneously, the specific interaction between the Sushi peptides and bacterial membrane phospholipids further explains the selective propensity of these peptides for the Gram-negative bacteria. Our findings yield insights into a complex molecular paradigm in which the juxtaposition of LPS molecules and the anionic phospholipid POPG (1-palmitoyl-2-oleoyl phosphatidylglycerol) on the bacterial outer membrane confers such interfacial properties which create the optimal environment for the interaction between the peptides and bacterial membrane lipids.
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high therapeutic index of factor c Sushi peptides potent antimicrobials against pseudomonas aeruginosa
Antimicrobial Agents and Chemotherapy, 2001Co-Authors: Bow Ho, Miang Lon Ng, J DingAbstract:Factor C protein isolated from the horseshoe crab, Carcinoscorpius rotundicauda , has endotoxin binding capability. Synthetic peptides of 34 amino acids based on the sequence of two regions of factor C (Sushi 1 and Sushi 3) as well as their corresponding mutants exhibited activities against 30 clinical isolates of Pseudomonas aeruginosa . Collectively, all four peptides demonstrated exceptionally effective bactericidal activity against P. aeruginosa with 90% minimal bactericidal concentrations (MBC 90 s) in the range of 0.06 to 0.25 μg/ml (16 to 63 nM). Viable bacteria were reduced by 90% after 7 min and were totally eradicated within 40 to 50 min. These peptides are minimally hemolytic against both rabbit and human erythrocytes even at concentrations up to 1,600-fold their MBC 90 s. Both in vitro and in vivo studies indicate that cytotoxic effects are small even at 1,000-fold their MBC 90 s. Furthermore, the Sushi peptides are tolerant of high-salt and adverse pH conditions. These findings demonstrate the promising therapeutic potential of the Sushi peptides.
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definition of endotoxin binding sites in horseshoe crab factor c recombinant Sushi proteins and neutralization of endotoxin by Sushi peptides
The FASEB Journal, 2000Co-Authors: Miang Lon Patricia Ng, Pooi Kat William Chong, Bow Ho, J DingAbstract:Three truncated fragments, harboring different Sushi domains, namely, Sushi123, Sushi1, and Sushi3 domains, of Factor C were produced as biologically active secreted recombinant proteins. Sushi1 and 3 each has a high-affinity LPS binding site with Kd of 10−9 to 10−10 M. Positive cooperativity in Sushi123 resulted in a 1000-fold increase in Kd2. The core LPS binding region of Sushi1 and 3 reside in two 34-mer peptides, S1 and S3. A rigidly held disulfide-bonded structure is not essential but is important for LPS binding, as confirmed by a 100- to 10000-fold decrease in affinity. Both S1 and S3 can inhibit LAL reaction and LPS-induced hTNF-α secretion with different potency. LAL assay revealed that at least two molecules of S1 bind cooperatively to one LPS molecule, with Hill’s coefficient of 2.42. The LPS binding by S3 is independent and noncooperative. The modified SΔ1 and SΔ3 peptides exhibited increased LPS neutralization potential although its LPS binding affinities indicated only a 10-fold improvement...
Foo Y Liew - One of the best experts on this subject based on the ideXlab platform.
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the Sushi domain of soluble il 15 receptor alpha is essential for binding il 15 and inhibiting inflammatory and allogenic responses in vitro and in vivo
Journal of Immunology, 2001Co-Authors: Michael Orchardson, Alastair J Gracie, Bernard P Leung, Hui Guan, Wanda Niedbala, Gavin K Paterson, Iain B Mcinnes, Foo Y LiewAbstract:IL-15 is a pleiotropic cytokine that plays important roles in both innate and adaptive immunity. It is associated with a range of immunopathology, including rheumatoid arthritis and allograft rejection. IL-15 functions through the trimeric IL-15R complex, which consists of a high affinity binding a-chain and the common IL-2R b- and g-chains. Characterization of IL-15/IL-15R interactions may facilitate the development of improved IL-15 antagonists for therapeutic interventions. We previously constructed soluble murine IL-15Ra (sIL-15Ra) by deleting the cytoplasmic and transmembrane domains. To localize the functional domain of IL-15Ra, we have now constructed various truncated versions of sIL-15Ra. The shortest region retaining IL-15 binding activity is a 65-aa sequence spanning the Sushi domain of IL-15Ra. Sushi domains, common motifs in protein-protein interactions, contain four cysteines forming two disulfide bonds in a 1-3 and 2-4 pattern. Amino acid substitution of the first or fourth cysteine in sIL-15Ra completely abolished its IL-15 binding activity. This also abrogated the ability of sIL-15Ra to neutralize IL-15- induced proinflammatory cytokine production and anti-apoptotic response in vitro. Furthermore, the mutant sIL-15Ra lost its ability to inhibit carrageenan-induced local inflammation and allogenic cell-induced T cell proliferation and cytokine production in vivo. Thus, the Sushi domain is critical for the functional activity of sIL-15Ra.
