Spectrum-based deep neural networks for fraud detection

In this paper, we focus on fraud detection on a signed graph with only a small set of labeled training data. We propose a novel framework that combines deep neural networks and spectral graph analysis. In particular, we use the node projection (called as spectral coordinate) in the low dimensional spectral space of the graph's adjacency matrix as input of deep neural networks. Spectral coordinates in the spectral space capture the most useful topology information of the network. Due to the small dimension of spectral coordinates (compared with the dimension of the adjacency matrix derived from a graph), training deep neural networks becomes feasible. We develop and evaluate two neural networks, deep autoencoder and convolutional neural network, in our fraud detection framework. Experimental results on a real signed graph show that our spectrum based deep neural networks are effective in fraud detection

A role for calcineurin in Dictyostelium discoideum phagocytosis

The Ca2+/calmodul1n-dependent protein phosphatase calcinewin is involved in the development of the cellular slime mold Dictyostelium discoideum. Because of its interactions with Ca2+, which appear to influence D. discoideum phagocytosis (Yuan and Chia, 1999, Mol. Biol. Cell 10, 220a), we undertook studies to test whether calcineurin also plays a role in Dictyostelium phagocytosis. The immunosuppressants cyclosporin A and FK506, through the formation of cyclosporin A-cyclophilin A and FK506- FK506-binding protein complexes, respectively, inhibited calcineurin activity. These two calcineurin inhibitors suppressed phagocytosis of fluorescently labeled yeast in a dose-dependent manner. Although it inhib~ted phagocytosis, cyclosporin A had an insignificant effect on the macropinocytosis of the fluid-phase marker fluorescein isothiocyanatedextran. Furthermore, trifluoperazine, a calmodulin antagonist that indirectly inhibits calcinewin, also suppressed phagocytosis in a dosedependent fashion and induced the formation of giant intracellular vacuoles Fluorescence microscopy of cyclosporin A-treated (for 30 min.) cells stained with rhodamine-phalloidin had cytoplasmic chunks of F-actin that were not present in control cells, while cells treated with FK506 and trifluoperazine (also for 30 min.), displayed less cortical but more cytoplasmic F-actin staining than normal cells. Typically, drug-treated cells were smaller and rounder than untreated cells. Our data suggest calcineurin may play a role in D. discoideum phagocytosis, either through the dephosphorylation of actinregulating proteins or other cytoskeletal proteins such as the heavy chain subunit of nonmuscle myosin I1 since dephosphorylation of the latter promotes filament assembly

Integrity of the actin cytoskeleton required for both phagocytosis and macropinocytosis in \u3ci\u3eDictyostelium discoideum\u3c/i\u3e

Filamentous (F-) actin is enriched in cellular extensions, such as phagocytic cups and macropioocytic crowns, of Dlctyostelium discoideum amebae. Previous studies of actin-disrupting agents that implicated the involvement of the actin cytoskeleton in Dictyostelium phagocytosis and pinocytosis, however, have yielded conflicting results. We show that the integrity of the actin cytoskeleton is required for both phagocytosis and macropinocytosis in D. discoideum with latrunculin A (IatA), which binds to monomeric actin, and cytochalasin A (cytA), which caps the plus end of actin filaments. Using rhodamine-phalloidin to visualize F-actin, cells treated for 30 min. with 1 to 4 pM of latA displayed an increasing dissolution of the cortical actin cytoskeleton that was accompanied by the appearance of numerous cytoplasmic dots of F-actin. In parallel, phagocytosis of fluorescently labeled yeast and macropinocytosis of the fluid-phase marker fluorescein isothiocyanate-dextran both were inhibited in a dose-dependent manner. Cells were nearly devoid of F-actin at latA concentrations greater than 5pM whereas the uniform distribution of monomeric actin appeared unaffected. Cells gradually recovered their intact actin cytoskeleton and concomitantly, their phagocytic and macropinocytic activities when latA was removed by washing. To achieve 50% inhibition of phagocytosis or macropinocytosis, five-fold more cytA than latA was required. Unlike latA-treated cells, cytAtreated cells stained with rhodamine phalloidin retained an actin cytoskeleton even at high concentrations (\u3e25 μM), but were smaller and rounder than untreated cells. The cortical F-actin, however, appeared irregular, and almost discontinuous, which made the cells seem stiff and rigid in comparison to normal cells that looked more fluid and plastic. The distinctive alterations in the cytoskeletal patterns reflected the specific modes of action of the drugs on the actin network that was vital for both phagocytosis and macropinocytosis

A role for calcineurin in Dictyostelium discoideum phagocytosis

The Ca2+/calmodul1n-dependent protein phosphatase calcinewin is involved in the development of the cellular slime mold Dictyostelium discoideum. Because of its interactions with Ca2+, which appear to influence D. discoideum phagocytosis (Yuan and Chia, 1999, Mol. Biol. Cell 10, 220a), we undertook studies to test whether calcineurin also plays a role in Dictyostelium phagocytosis. The immunosuppressants cyclosporin A and FK506, through the formation of cyclosporin A-cyclophilin A and FK506- FK506-binding protein complexes, respectively, inhibited calcineurin activity. These two calcineurin inhibitors suppressed phagocytosis of fluorescently labeled yeast in a dose-dependent manner. Although it inhib~ted phagocytosis, cyclosporin A had an insignificant effect on the macropinocytosis of the fluid-phase marker fluorescein isothiocyanatedextran. Furthermore, trifluoperazine, a calmodulin antagonist that indirectly inhibits calcinewin, also suppressed phagocytosis in a dosedependent fashion and induced the formation of giant intracellular vacuoles Fluorescence microscopy of cyclosporin A-treated (for 30 min.) cells stained with rhodamine-phalloidin had cytoplasmic chunks of F-actin that were not present in control cells, while cells treated with FK506 and trifluoperazine (also for 30 min.), displayed less cortical but more cytoplasmic F-actin staining than normal cells. Typically, drug-treated cells were smaller and rounder than untreated cells. Our data suggest calcineurin may play a role in D. discoideum phagocytosis, either through the dephosphorylation of actinregulating proteins or other cytoskeletal proteins such as the heavy chain subunit of nonmuscle myosin I1 since dephosphorylation of the latter promotes filament assembly

Nonspecific interactions alter lipopolysaccharide patterns and protein mobility on sodium dodecyl sulfate polyacrylamide gels

In testing whether bacterial lipopolysaccharide (LPS) was a natural substrate for an esterase from the soil amebae Dictyostelium discoideum, we observed altered banding patterns of the LPS and changed protein mobility on sodium dodecyl sulfate (SDS) polyacrylamide gels after incubation of LPS with the enzyme. The initial interpretation of these results was that the enzyme had removed ester-linked acyl chains from the LPS, leading to a change in its migration on gels. However, esterase inactivated by treatment with either dithiothreitol (DTT), heat, or SDS generated the same mobility shifts. Bovine serum albumin (BSA) also induced the same change in the electrophoretic pattern. We conclude that the altered LPS patterns and protein mobility on SDS gels were caused by nonspecific interactions between LPS and protein

Nonspecific interactions alter lipopolysaccharide patterns and protein mobility on sodium dodecyl sulfate polyacrylamide gels

In testing whether bacterial lipopolysaccharide (LPS) was a natural substrate for an esterase from the soil amebae Dictyostelium discoideum, we observed altered banding patterns of the LPS and changed protein mobility on sodium dodecyl sulfate (SDS) polyacrylamide gels after incubation of LPS with the enzyme. The initial interpretation of these results was that the enzyme had removed ester-linked acyl chains from the LPS, leading to a change in its migration on gels. However, esterase inactivated by treatment with either dithiothreitol (DTT), heat, or SDS generated the same mobility shifts. Bovine serum albumin (BSA) also induced the same change in the electrophoretic pattern. We conclude that the altered LPS patterns and protein mobility on SDS gels were caused by nonspecific interactions between LPS and protein

One-Class Adversarial Nets for Fraud Detection

Many online applications, such as online social networks or knowledge bases, are often attacked by malicious users who commit different types of actions such as vandalism on Wikipedia or fraudulent reviews on eBay. Currently, most of the fraud detection approaches require a training dataset that contains records of both benign and malicious users. However, in practice, there are often no or very few records of malicious users. In this paper, we develop one-class adversarial nets (OCAN) for fraud detection using training data with only benign users. OCAN first uses LSTM-Autoencoder to learn the representations of benign users from their sequences of online activities. It then detects malicious users by training a discriminator with a complementary GAN model that is different from the regular GAN model. Experimental results show that our OCAN outperforms the state-of-the-art one-class classification models and achieves comparable performance with the latest multi-source LSTM model that requires both benign and malicious users in the training phase.Comment: Update Fig 2, add Fig 7, and add reference

Tubulin and Neurofilament Proteins Are Transported Differently in Axons of Chicken Motoneurons

1. We previously showed that actin is transported in an unassembled form with its associated proteins actin depolymerizing factor, cofilin, and profilin. Here we examine the specific activities of radioactively labeled tubulin and neurofilament proteins in subcellular fractions of the chicken sciatic nerve following injection of L-[35S]methionine into the lumbar spinal cord. 2. At intervals of 12 and 20 days after injection, nerves were cut into 1-cm segments and separated into Triton X-100-soluble and particulate fractions. Analysis of the fractions by high-resolution two-dimensional gel electrophoresis, immunoblotting, fluorography, and computer densitometry showed that tubulin was transported as a unimodal wave at a slower average rate (2–2.5 mm/day) than actin (4–5 mm/day). Moreover, the specific activity of soluble tubulin was five times that of its particulate form, indicating that tubulin is transported in a dimeric or small oligomeric form and is assembled into stationary microtubules. 3. Neurofilament triplet proteins were detected only in the particulate fractions and transported at a slower average rate (1 mm/day) than either actin or tubulin. 4. Our results indicate that the tubulin was transported in an unpolymerized form and that the neurofilament proteins were transported in an insoluble, presumably polymerized form

Tubulin and Neurofilament Proteins Are Transported Differently in Axons of Chicken Motoneurons

1. We previously showed that actin is transported in an unassembled form with its associated proteins actin depolymerizing factor, cofilin, and profilin. Here we examine the specific activities of radioactively labeled tubulin and neurofilament proteins in subcellular fractions of the chicken sciatic nerve following injection of L-[35S]methionine into the lumbar spinal cord. 2. At intervals of 12 and 20 days after injection, nerves were cut into 1-cm segments and separated into Triton X-100-soluble and particulate fractions. Analysis of the fractions by high-resolution two-dimensional gel electrophoresis, immunoblotting, fluorography, and computer densitometry showed that tubulin was transported as a unimodal wave at a slower average rate (2–2.5 mm/day) than actin (4–5 mm/day). Moreover, the specific activity of soluble tubulin was five times that of its particulate form, indicating that tubulin is transported in a dimeric or small oligomeric form and is assembled into stationary microtubules. 3. Neurofilament triplet proteins were detected only in the particulate fractions and transported at a slower average rate (1 mm/day) than either actin or tubulin. 4. Our results indicate that the tubulin was transported in an unpolymerized form and that the neurofilament proteins were transported in an insoluble, presumably polymerized form