IPv6 security and forensics

The 2016 Sixth International Conference on Innovative Computing Technology (INTECH), Dublin, Ireland, 24-26 August 2016IPv4 is the historical addressing protocol used for all devices connected worldwide. It has survived for over 30 years and has been an integral part of the Internet revolution. However, due to its limitation, IPv4 is being replacing by IPv6. Today, IPv6 is more and more widely used on the Internet. On the other hand, criminals are also well aware of the introduction of IPv6. They are continuously seeking new methods to make profit, hiding their activities, infiltrate or exfiltrate important data from companies. The introduction of this new protocol may provide savvy cybercriminals more opportunities to discover new system vulnerabilities and exploit them. To date, there is little research on IPv6 security and forensics in the literature. In this paper, we look at different types of IPv6 attacks and we present a new approach to investigate IPv6 network attack with case studies

IPv6 Security and Forensics

IPv4 is the historical addressing protocol used for all devices connected worldwide. It has survived for over 30 years and has been an integral part of the Internet revolution. However, due to its limitation, IPv4 is being replacing by IPv6. Today, IPv6 is more and more widely used on the Internet. On the other hand, criminals are also well aware of the introduction of IPv6. They are continuously seeking new methods to make profit, hiding their activities, infiltrate or exfiltrate important data from companies. The introduction of this new protocol may provide savvy cybercriminals more opportunities to discover new system vulnerabilities and exploit them. To date, there is little research on IPv6 security and forensics in the literature. In this paper, we look at different types of IPv6 attacks and we present a new approach to investigate IPv6 network attack with case studies

PHARMACY PRACTICE Using Clinical Pharmacy Support Technicians to Optimize Pharmaceutical Care in the Intensive Care Unit

Even as the scope of pharmacy practice expands, impediments to optimal delivery of pharmaceutical care remain. These include shortages of pharmacists, increasing complexity of medication regimens, and increasing acuity of patients an

Bifunctional family 3 glycoside hydrolases from barley with alpha-L-arabinofuranosidase and beta-D-xylosidase activity - Characterization, primary structures, and COOH-terminal processing

An alpha-l-arabinofuranosidase and a beta-d-xylosidase, designated ARA-I and XYL, respectively, have been purified about 1,000-fold from extracts of 5-day-old barley (Hordeum vulgare L.) seedlings using ammonium sulfate fractional precipitation, ion exchange chromatography, chromatofocusing, and size-exclusion chromatography. The ARA-I has an apparent molecular mass of 67 kDa and an isoelectric point of 5.5, and its catalytic efficiency during hydrolysis of 4'-nitrophenyl alpha-l-arabinofuranoside is only slightly higher than during hydrolysis of 4'-nitrophenyl beta-d-xyloside. Thus, the enzyme is actually a bifunctional alpha-l-arabinofuranosidase/beta-d-xylosidase. In contrast, the XYL enzyme, which also has an apparent molecular mass of 67 kDa and an isoelectric point of 6.7, preferentially hydrolyzes 4'-nitrophenyl beta-d-xyloside, with a catalytic efficiency approximately 30-fold higher than with 4'-nitrophenyl alpha-l-arabinofuranoside. The enzymes hydrolyze wheat flour arabinoxylan slowly but rapidly hydrolyze oligosaccharide products released from this polysaccharide by (1 --> 4)-beta-d-xylan endohydrolase. Both enzymes hydrolyze (1 --> 4)-beta-d-xylopentaose, and ARA-I can also degrade (1 --> 5)-alpha-l-arabinofuranohexaose. ARA-I and XYL cDNAs encode mature proteins of 748 amino acid residues which have calculated molecular masses of 79.2 and 80.5 kDa, respectively. Both are family 3 glycoside hydrolases. The discrepancies between the apparent molecular masses obtained for the purified enzymes and those predicted from the cDNAs are attributable to COOH-terminal processing, through which about 130 amino acid residues are removed from the primary translation product. The genes encoding the ARA-I and XYL have been mapped to chromosomes 2H and 6H, respectively. ARA-I transcripts are most abundant in young roots, young leaves, and developing grain, whereas XYL mRNA is detected in most barley tissues.Robert C Lee, Maria Hrmova, Rachel A Burton, Jelle Lahnstein, Geoffrey B Finche

Mutated Barley (1,3)-beta-D-Glucan Endohydrolases Synthesize Crystalline (1,3)-beta-D-Glucans

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.Barley (1,3)-beta-D-glucan endohydrolases (EC ), inactivated by site-directed mutagenesis of their catalytic nucleophiles, show autocondensation glucosynthetic activity with alpha-laminaribiosyl fluoride and heterocondensation glycosynthetic activity with alpha-laminaribiosyl fluoride and 4'-nitrophenyl beta-D-glucopyranoside. The native enzyme is a retaining endohydrolase of the family 17 group and catalyzes glycosyl transfer reactions at high substrate concentrations. Catalytic efficiencies (k(cat) K(m)(-1)) of mutants E231G, E231S, and E231A as glycosynthases are 28.9, 0.9, and 0.5 x 10(-4) m(-1) s(-1), respectively. Glycosynthase reactions appear to be processive and proceed with pH optima of 6-8 and yields of up to 75%. Insoluble products formed during the glycosynthase reaction appear as lamellar, hexagonal crystals when observed by electron microscopy. Methylation, NMR, and matrix-assisted laser desorption ionization time-of-flight analyses show that the reaction products are linear (1,3)-beta-D-glucans with a degree of polymerization of 30-34, whereas electron and x-ray diffraction patterns indicate that these (1,3)-beta-D-glucan chains adopt a parallel, triple helical conformation. The (1,3)-beta-D-glucan triple helices are orientated perpendicularly to the plane of the lamellar crystals. The barley (1,3)-beta-D-glucan glycosynthases have considerable potential for tailored and high efficiency synthesis of (1,3)-beta-D-linked oligo- and polysaccharides, some of which could have immunomodulating activity, or for the coupling of (1,3)-beta-D-linked glucosyl residues onto other oligosaccharides or glycoproteins.Maria Hrmova, Tomoya Imai, Simon J. Rutten, Jon K. Fairweather, Ludovic Pelosi, Vincent Bulone, Hugues Driguez, and Geoffrey B. Finche