Technion – Israel Institute of Technology

About: Technion – Israel Institute of Technology is a education organization based out in Haifa, Israel. It is known for research contribution in the topics: Population & Upper and lower bounds. The organization has 31714 authors who have published 79377 publications receiving 2603976 citations. The organization is also known as: Technion Israel Institute of Technology & Ṭekhniyon, Makhon ṭekhnologi le-Yiśraʼel.

How to Construct Polar Codes

Abstract: A method for efficiently constructing polar codes is presented and analyzed. Although polar codes are explicitly defined, straightforward construction is intractable since the resulting polar bit-channels have an output alphabet that grows exponentially with he code length. Thus the core problem that needs to be solved is that of faithfully approximating a bit-channel with an intractably large alphabet by another channel having a manageable alphabet size. We devise two approximation methods which "sandwich" the original bit-channel between a degraded and an upgraded version thereof. Both approximations can be efficiently computed, and turn out to be extremely close in practice. We also provide theoretical analysis of our construction algorithms, proving that for any fixed $\epsilon > 0$ and all sufficiently large code lengths $n$, polar codes whose rate is within $\epsilon$ of channel capacity can be constructed in time and space that are both linear in $n$.

Anderson localization of light

Abstract: The Anderson localization of light within disordered media has become a topic of great interest in recent years. Here the characterization of the effect and its related phenomena are reviewed, with a discussion on the role that nonlinearity and quantum correlated photons can play.

Green tea polyphenol (-)-epigallocatechin-3-gallate prevents N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced dopaminergic neurodegeneration.

Abstract: In the present study we demonstrate neuroprotective property of green tea extract and (-)-epigallocatechin-3-gallate in N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mice model of Parkinson's disease. N-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine neurotoxin caused dopamine neuron loss in substantia nigra concomitant with a depletion in striatal dopamine and tyrosine hydroxylase protein levels. Pretreatment of mice with either green tea extract (0.5 and 1 mg/kg) or (-)-epigallocatechin-3-gallate (2 and 10 mg/kg) prevented these effects. In addition, the neurotoxin caused an elevation in striatal antioxidant enzymes superoxide dismutase (240%) and catalase (165%) activities, both effects being prevented by (-)-epigallocatechin-3-gallate. (-)-Epigallocatechin-3-gallate itself also increased the activities of both enzymes in the brain. The neuroprotective effects are not likely to be caused by inhibition of N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine conversion to its active metabolite 1-methyl-4-phenylpyridinium by monoamine oxidase-B, as both green tea and (-)-epigallocatechin-3-gallate are very poor inhibitors of this enzyme in vitro (770 microg/mL and 660 microM, respectively). Brain penetrating property of polyphenols, as well as their antioxidant and iron-chelating properties may make such compounds an important class of drugs to be developed for treatment of neurodegenerative diseases where oxidative stress has been implicated.

Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein–Barr virus nuclear antigen 1

Abstract: The Epstein–Barr virus (EBV) encoded nuclear antigen (EBNA) 1 is expressed in latently infected B lymphocytes that persist for life in healthy virus carriers and is the only viral protein regularly detected in all EBV associated malignancies. The Gly-Ala repeat domain of EBNA1 was shown to inhibit in cis the presentation of major histocompatibility complex (MHC) class I restricted cytotoxic T cell epitopes from EBNA4. It appears that the majority of antigens presented via the MHC I pathway are subject to ATP-dependent ubiquitination and degradation by the proteasome. We have investigated the influence of the repeat on this process by comparing the degradation of EBNA1, EBNA4, and Gly-Ala containing EBNA4 chimeras in a cell-free system. EBNA4 was efficiently degraded in an ATP/ubiquitin/proteasome-dependent fashion whereas EBNA1 was resistant to degradation. Processing of EBNA1 was restored by deletion of the Gly-Ala domain whereas insertion of Gly-Ala repeats of various lengths and in different positions prevented the degradation of EBNA4 without appreciable effect on ubiquitination. Inhibition was also achieved by insertion of a Pro-Ala coding sequence. The results suggest that the repeat may affect MHC I restricted responses by inhibiting antigen processing via the ubiquitin/proteasome pathway. The presence of regularly interspersed Ala residues appears to be important for the effect.