Critical Success factors for ERP Implementation: A content analysis of empirical Findings

Enterprise resource planning (ERP) systems are software packages that allow companies to have greater real time visibility and control over their operations. Through a review of the ERP literature, seven critical success factors (CSFs) were identified based on the study of Nah and Delgado (2006). Content analysis was then employed on 16 published articles that reported CSFs for ERP. Correspondingly, this paper aimed to combine various results in order to determine the CSFs that contribute to success in the implementation of ERP systems. We found that the ERP CSFs referred to top management support and championship in a majority of articles, while communication was less mentioned

A data mining approach to face detection [J

a b s t r a c t In this paper, we propose a novel face detection method based on the MAFIA algorithm. Our proposed method consists of two phases, namely, training and detection. In the training phase, we first apply Sobel's edge detection operator, morphological operator, and thresholding to each training image, and transform it into an edge image. Next, we use the MAFIA algorithm to mine the maximal frequent patterns from those edge images and obtain the positive feature pattern. Similarly, we can obtain the negative feature pattern from the complements of edge images. Based on the feature patterns mined, we construct a face detector to prune non-face candidates. In the detection phase, we apply a sliding window to the testing image in different scales. For each sliding window, if the slide window passes the face detector, it is considered as a human face. The proposed method can automatically find the feature patterns that capture most of facial features. By using the feature patterns to construct a face detector, the proposed method is robust to races, illumination, and facial expressions. The experimental results show that the proposed method has outstanding performance in the MIT-CMU dataset and comparable performance in the BioID dataset in terms of false positive and detection rate

Determining Antibody-Binding Site of Streptococcal Pyrogenic Exotoxin B to Protect Mice from Group A Streptococcus Infection

<div><p>Streptococcal pyrogenic exotoxin B (SPE B), a cysteine protease, is an important virulence factor in group A streptococcal (GAS) infection. SPE B binds and cleaves antibody isotypes and further impairs the immune system by inhibiting complement activation. In this study, we examined the antibody-binding site of SPE B and used it to block SPE B actions during GAS infection. We constructed different segments of the <em>spe B</em> gene and induced them to express different recombinant fragments of SPE B. Using an enzyme-linked immunosorbent assay (ELISA), we found that residues 345–398 of the C-terminal domain of SPE B (rSPE B_345–398), but not the N-terminal domain, was the major binding site for antibody isotypes. Using a competitive ELISA, we also found that rSPE B_345–398 bound to the Fc portion of IgG. The <em>in vitro</em> functional assays indicate that rSPE B_345–398 not only interfered with cleavage of antibody isotypes but also interfered with SPE B-induced inhibition of complement activation. Immunization of BALB/c mice using rSPE B_345–398 was able to induce production of a high titer of anti-rSPE B_345–398 antibodies and efficiently protected mice from GAS-induced death. These findings suggest that SPE B uses its C-terminal domain to bind the Fc portion of IgG and that immunization of mice with this binding domain (rSPE B_345–398) could protect mice from GAS infection.</p> </div

Effect of SPE B on immunoglobulins.

<p>(A) Either 400 µg/ml of purified IgG or the IgM-IgA mixture was incubated with 20 µg/ml of mSPE B or C192S for 1 h with 5 mM DTT-0.1 mM EDTA. The reaction mixture was separated using 12% SDS-PAGE and blotted using goat anti-human IgG, IgM, or IgA, as described in Materials and Methods. (B) Either 400 µg/ml of purified IgG or the IgM-IgA mixture was incubated with 20 µg/ml of mSPE B for 1, 2 or 18 h with 5 mM DTT-0.1 mM EDTA. The reaction mixture was separated using 12% SDS-PAGE and blotted using goat anti-human IgG, IgM, or IgA, as described in Materials and Methods.</p

Expression of SPE B truncations.

<p>Cloning and expression of different <i>speB</i> gene segments were described in Materials and Methods. zSPE B represents zymogen SPE B. (A) Different recombinant SPE B fragments (rSPE B_146–280, rSPE B_146–398, rSPE B_281–358, rSPE B_345–398), C192S, mSPE B, or BSA were verified by 12% SDS-PAGE, and their molecular weights are shown. (B) The antigenicity of different rSPE B fragments, C192S, mSPE B was determined by western blotting with anti-SPE B antibody, as described in Materials and Methods.</p

Binding of rSPE B_345–398 and human IgG.

<p>(A) Either protein L or protein A was incubated with purified human IgG at a molar ratio of 2.5 for 30 min at 37°C. (B) Protein A was incubated with purified human IgG at different molar ratios for 30 min at 37°C. The reaction mixtures mentioned above were added to microtiter plates that were pre-coated with purified rSPE B_345–398 or BSA. Absorbance values were read at 650 nm, and the relative binding activity was calculated as described in Materials and Methods. *<i>P</i><0.05, **<i>P</i><0.01 compared with values determined for IgG only group. (C) Purified human IgG or the different concentrations (0.5–5 µM) of Fc fragment of human IgG were added to microtiter plates that were pre-coated with purified rSPE B_345–398 or C192S, as described in Materials and Methods. Absorbance values were read at 650 nm. **<i>P</i><0.01 compared with values determined for PBS group.</p

Effect of rSPE B_345–398 on SPE B-mediated inhibition of classical complement activation.

<p>The human sera diluted with specific buffers provided by the Wielisa COMPL300 Total Complement Functional Screen kit were incubated with 20 µg/ml of mSPE B in the absence or presence of different concentrations of rSPE B_345–398, and the complement activation by human sera was detected using an ELISA assay. The percent inhibition of complement activity was calculated as described in Materials and Methods.</p