The authors present a novel DFT technique based on multimode Illinois scan architecture (MILS) for low pin count test that simultaneously reduces test data volume and test application time. By using the proposed technique, significant savings in test data volume, and testing time can be obtained without modifying the clock tree of the design and with a very small combinational area overhead. Experimental results for two large industrial circuits show that the test data volume and test application time reduction of the order of 100times can be achieved in all cases with less than 1% area overhead over ILS.

An embedded test stimulus decompressor is presented for the test patterns decompression, which can reduce the required channels and vector memory of automatic test equipment (ATE) for complex processor circuit. The proposed decompressor mainly consists of a periodically alterable MUX network which has multiple configurations to decode the input information flexibly and efficiently. In order to reduce the number of test patterns and configurations, a test patterns compaction algorithm, using CI-Graph merging, is proposed. With the proposed periodically alterable MUX network and the patterns compaction algorithm, smaller test data volume and required external pins can be achieved as compared to previous techniques

Scan compression technology innovation has broken out into solving the data volume problem keeping the test application time gains relatively constant over the generations of technologies. While data volume reductions are important there is a need to take the test application time gains to the next level as it has a direct impact to the cost of test. In this paper an enhancement to combinational compression is described that relies on increasing the encoding bandwidth for aggressive test application time targets. An architecture is described that adds very little area overhead to a combinational compression architecture by reusing the internal scan chains of the design for encoding bandwidth for a set of the test patterns.

Coumarins are a highly privileged scaffold in medicinal chemistry. It is present in many natural products and is reported to display various pharmacological properties. A large plethora of compounds based on the coumarin ring system have been synthesized and were found to possess biological activities such as anticonvulsant, antiviral, anti-inflammatory, antibacterial, antioxidant as well as neuroprotective properties. Despite the wide activity spectrum of coumarins, its naturally occurring derivatives are yet to be investigated in detail. In the current study, a chemical library was created to assemble all chemical information related to naturally occurring coumarins from the literature. Additionally, a multi-stage virtual screening combining QSAR modeling, molecular docking, and ADMET prediction was conducted against monoamine oxidase B and acetylcholinesterase, two relevant targets known for their neuroprotective properties and 'disease-modifying' potential in Parkinson's and Alzheimer's disease. Our findings revealed ten coumarin derivatives that may act as dual-target drugs against MAO-B and AChE. Two coumarin candidates were selected from the molecular docking study: CDB0738 and CDB0046 displayed favorable interactions for both proteins as well as suitable ADMET profiles. The stability of the selected coumarins was assessed through 100 ns molecular dynamics simulations which revealed promising stability through key molecular interactions for CDB0738 to act as dual inhibitor of MAO-B and AChE. However, experimental studies are necessary to evaluate the bioactivity of the proposed candidate. The current results may generate an increasing interest in bioprospecting naturally occurring coumarins as potential candidates against relevant macromolecular targets by encouraging virtual screening studies against our chemical library.Communicated by Ramaswamy H. Sarma.

Protein kinases are the family of attractive enzyme targets for drug design with relevance to cancer biology. Serine arginine protein kinase 1 (SRPK1) is responsible for the phosphorylation of serine/arginine (SR)-rich proteins. Alternative Splicing Factor/Splicing Factor 2 (ASF/SF2) involved in mRNA editing. ASF/SF2 is over expressed in many cancers and plays crucial roles in the cell survival. Phosphorylation of ASF/SF2 is decisive for its functions in cancer. In search of potential anti cancer therapeutic agents for attenuating phosphorylation of ASF/SF2, we have explored specific and potential inhibitors of SRPK1 from natural and drug like compounds databases using in-silico methods. Compound ZINC02154892 (C02) was found to be the most potent inhibitor for SRPK1. In-vitro molecular and cell biology studies have shown C02 as a potent and specific inhibitor of phosphorylation of ASF/SF2 and cell survival in leukemic cell line. Structural analysis of SRPK1 with compound C02 revealed a unique pattern of binding targeting ATP binding site along with inhibiting recruitment of ASF/SF2 by SRPK1. The possibilities of compound C02 to be used as a lead compound paving way for the development of potent and specific inhibitors of SRPK1 for designing of novel potential anticancer inhibitor is inferred from the current studies.