Agile SoC Development with Open ESP

ESP is an open-source research platform for heterogeneous SoC design. The platform combines a modular tile-based architecture with a variety of application-oriented flows for the design and optimization of accelerators. The ESP architecture is highly scalable and strikes a balance between regularity and specialization. The companion methodology raises the level of abstraction to system-level design and enables an automated flow from software and hardware development to full-system prototyping on FPGA. For application developers, ESP offers domain-specific automated solutions to synthesize new accelerators for their software and to map complex workloads onto the SoC architecture. For hardware engineers, ESP offers automated solutions to integrate their accelerator designs into the complete SoC. Conceived as a heterogeneous integration platform and tested through years of teaching at Columbia University, ESP supports the open-source hardware community by providing a flexible platform for agile SoC development.Comment: Invited Paper at the 2020 International Conference On Computer Aided Design (ICCAD) - Special Session on Opensource Tools and Platforms for Agile Development of Specialized Architecture

Deviation of Internal Magnetic Field in the CrSe2 Triangular Lattice with Li Intercalation

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Magnetic Phases in Sr(1-x) Ca(x)Co(2)P(2) Studied by μ+ SR

20th International Conference on Magnetism, ICM 2015In order to elucidate the dependence of the magnetic ground state on the Ca content (x) in Sr1-xCaxCo2P2 (0 ≤x ≤1, ThCr2Si2-type structure), we have performed muon spin rotation− and relaxation (μ+SR) experiments on Sr1-xCax Co2P2 powder samples mainly in a zero applied field. The end member compound, SrCo2P2, is found to be paramagnetic down to 19 mK. As x increases, such a paramagnetic ground state is observed down to 1.8 K until x = 0.45. Then, as x increases further, a short-range antiferromagnetic (AF) ordered phase appears at low temperatures for 0.48 ≤ x ≤ 0.75, and finally, a long-range AF ordered phase is stabilized for x > 0.75. The internal magnetic field of the other end member compound, CaCo2P2, is well consistent with that of the A-type AF order state, which was proposed from neutron scattering experiments. The phase diagram determined with μ+SR is different from that proposed by macroscopic measurements. For an isostructural compound, LaCo2P2, static magnetic order is found to be formed below <∼ 130 K

Deglycosylated anti-amyloid beta antibodies induce amyloid beta sequestration with reduced microglial phagocytosis and cytokine release

Accumulation of amyloid beta (Abeta) is a pathological hallmark of Alzheimer\u27s disease, and lowering Abeta is a promising therapeutic approach. Intact anti-Abeta antibodies reduce brain Abeta through two pathways: enhanced microglial phagocytosis and Abeta transfer from the brain to the periphery (Abeta sequestration). While activation of microglia, which is essential for microglial phagocytosis, is necessarily accompanied by undesired neuroinflammatory events, the capacity for sequestration does not seem to be linked to such effects. We and other groups have found that simple Abeta binding agents are sufficient to reduce brain Abeta through the sequestration pathway. In this study, we aimed to eliminate potentially deleterious immune activation from antibodies without affecting the ability to induce sequestration. The glycan portion of immunoglobulin is critically involved in interactions with immune effectors including the Fc receptor and complement c1q; deglycosylation eliminates these interactions, while antigen (Abeta)-binding affinity is maintained. In this study, we investigated whether deglycosylated anti-Abeta antibodies reduce microglial phagocytosis and neuroinflammation without altering the capacity to induce Abeta sequestration. Deglycosylated antibodies maintained Abeta binding affinity. Deglycosylated antibodies did not enhance Abeta phagocytosis or cytokine release in primary cultured microglia, whereas intact antibodies did so significantly. Intravenous injection of deglycosylated antibodies elevated plasma Abeta levels and induced Abeta sequestration to a similar or greater degree compared with intact antibodies in an Alzheimer\u27s transgenic mouse model without or with Abeta plaque pathology. We conclude that deglycosylated antibodies effectively induced Abeta sequestration without provoking neuroinflammation; thus, these deglycosylated antibodies may be optimal for sequestration therapy for Alzheimer\u27s disease