Bridging the Gap Between Neural Networks and Neuromorphic Hardware with A Neural Network Compiler

Different from developing neural networks (NNs) for general-purpose processors, the development for NN chips usually faces with some hardware-specific restrictions, such as limited precision of network signals and parameters, constrained computation scale, and limited types of non-linear functions. This paper proposes a general methodology to address the challenges. We decouple the NN applications from the target hardware by introducing a compiler that can transform an existing trained, unrestricted NN into an equivalent network that meets the given hardware's constraints. We propose multiple techniques to make the transformation adaptable to different kinds of NN chips, and reliable for restrict hardware constraints. We have built such a software tool that supports both spiking neural networks (SNNs) and traditional artificial neural networks (ANNs). We have demonstrated its effectiveness with a fabricated neuromorphic chip and a processing-in-memory (PIM) design. Tests show that the inference error caused by this solution is insignificant and the transformation time is much shorter than the retraining time. Also, we have studied the parameter-sensitivity evaluations to explore the tradeoffs between network error and resource utilization for different transformation strategies, which could provide insights for co-design optimization of neuromorphic hardware and software.Comment: Accepted by ASPLOS 201

Chiral patterns arising from electrostatic growth models

Recently, unusual and strikingly beautiful seahorse-like growth patterns have been observed under conditions of quasi-two-dimensional growth. These `S'-shaped patterns strongly break two-dimensional inversion symmetry; however such broken symmetry occurs only at the level of overall morphology, as the clusters are formed from achiral molecules with an achiral unit cell. Here we describe a mechanism which gives rise to chiral growth morphologies without invoking microscopic chirality. This mechanism involves trapped electrostatic charge on the growing cluster, and the enhancement of growth in regions of large electric field. We illustrate the mechanism with a tree growth model, with a continuum model for the motion of the one-dimensional boundary, and with microscopic Monte Carlo simulations. Our most dramatic results are found using the continuum model, which strongly exhibits spontaneous chiral symmetry breaking, and in particular finned `S' shapes like those seen in the experiments.Comment: RevTeX, 12 pages, 9 figure

X-Linked thrombocytopenia causing mutations in WASP (L46P and A47D) impair T cell chemotaxis

BACKGROUND: Mutation in the Wiskott-Aldrich syndrome Protein (WASP) causes Wiskott-Aldrich syndrome (WAS), X-linked thrombocytopenia (XLT) and X-linked congenital neutropenia (XLN). The majority of missense mutations causing WAS and XLT are found in the WH1 (WASP Homology) domain of WASP, known to mediate interaction with WIP (WASP Interacting Protein) and CIB1 (Calcium and Integrin Binding). RESULTS: We analyzed two WASP missense mutants (L46P and A47D) causing XLT for their effects on T cell chemotaxis. Both mutants, WASP(R)(L46P) and WASP(R)(A47D) (S1-WASP shRNA resistant) expressed well in Jurkat(WASP-KD) T cells (WASP knockdown), however expression of these two mutants did not rescue the chemotaxis defect of Jurkat(WASP-KD) T cells towards SDF-1α. In addition Jurkat(WASP-KD) T cells expressing these two WASP mutants were found to be defective in T cell polarization when stimulated with SDF-1α. WASP exists in a closed conformation in the presence of WIP, however both the mutants (WASP(R)(L46P) and WASP(R)(A47D)) were found to be in an open conformation as determined in the bi-molecular complementation assay. WASP protein undergoes proteolysis upon phosphorylation and this turnover of WASP is critical for T cell migration. Both the WASP mutants were found to be stable and have reduced tyrosine phosphorylation after stimulation with SDF-1α. CONCLUSION: Thus our data suggest that missense mutations WASP(R)(L46P) or WASP(R)(A47D) affect the activity of WASP in T cell chemotaxis probably by affecting the turnover of the protein. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12929-014-0091-1) contains supplementary material, which is available to authorized users

Structural and Functional Diversity of Acidic Scorpion Potassium Channel Toxins

Background: Although the basic scorpion K + channel toxins (KTxs) are well-known pharmacological tools and potential drug candidates, characterization the acidic KTxs still has the great significance for their potential selectivity towards different K + channel subtypes. Unfortunately, research on the acidic KTxs has been ignored for several years and progressed slowly. Principal Findings: Here, we describe the identification of nine new acidic KTxs by cDNA cloning and bioinformatic analyses. Seven of these toxins belong to three new a-KTx subfamilies (a-KTx28, a-KTx29, and a-KTx30), and two are new members of the known k-KTx2 subfamily. ImKTx104 containing three disulfide bridges, the first member of the a-KTx28 subfamily, has a low sequence homology with other known KTxs, and its NMR structure suggests ImKTx104 adopts a modified cystine-stabilized a-helix-loop-b-sheet (CS-a/b) fold motif that has no apparent a-helixs and b-sheets, but still stabilized by three disulfide bridges. These newly described acidic KTxs exhibit differential pharmacological effects on potassium channels. Acidic scorpion toxin ImKTx104 was the first peptide inhibitor found to affect KCNQ1 channel, which is insensitive to the basic KTxs and is strongly associated with human cardiac abnormalities. ImKTx104 selectively inhibited KCNQ1 channel with a Kd of 11.69 mM, but was less effective against the basic KTxs-sensitive potassium channels. In addition to the ImKTx104 toxin, HeTx204 peptide, containing a cystine-stabilized a-helix-loop-helix (CS-a/a) fold scaffold motif