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RISS 인기검색어
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- 저자 : Razin, Ehud (검색결과 9 건)
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A. Alizadeh Razin,H. Yari,B. Ramezanzadeh 한국공업화학회 2015 Journal of Industrial and Engineering Chemistry Vol.31 No.-
The main objective of this study is to investigate how the weathering of underneath electro deposition(ED) layer affects the overall stone-chipping behavior of an automotive coating system. The ED-coatedpanels were exposed to natural weathering condition before being further coated with top layers. It wasfound that the underneath layer weathering has a deleterious effect on the chipping and adhesion of thewhole coating system. The chemistry and morphology of the weathered ED layer demonstrated that thechalky-like ED surface could not provide a desired foundation for top layers, leading to a coatingstructure collapse.
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Breast Cancer in Morocco: A Literature Review
Slaoui, Meriem,Razine, Rachid,Ibrahimi, Azeddine,Attaleb, Mohammed,El Mzibri, Mohammed,Amrani, Mariam Asian Pacific Journal of Cancer Prevention 2014 Asian Pacific journal of cancer prevention Vol.15 No.3
In Morocco, breast cancer is the most prevalent cancer in women and a major public health problem. Several Moroccan studies have focused on studying this disease, but more are needed, especially at the genetic and molecular levels. It is therefore interesting to establish the genetic and molecular profile of Moroccan patients with breast cancer. In this paper, we will highlight some pertinent hypotheses that may enhance breast cancer care in Moroccan patients. This review will give a precise description of breast cancer in Morocco and propose some new markers for detection and prediction of breast cancer prognosis.
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Promyelocytic Leukemia (PML) Gene Mutations may not Contribute to Gastric Adenocarcinoma Development
Imani-Saber, Zeinab,Yousefi-Razin, Ehsan,Javaheri, Mona,Mirfakhraie, Reza,Motalleb, Gholamreza,Ghafouri-Fard, Soudeh Asian Pacific Journal of Cancer Prevention 2015 Asian Pacific journal of cancer prevention Vol.16 No.8
Gastric cancer is the second most common cause of cancer death worldwide. Environmental as well as genetic factors have been shown to be involved in its genesis. Among genetic factors, loss of function of a tumor suppressive gene named promyelocytic leukemia (PML) has been demonstrated in gastric cancer. In order to cast light in the mechanism by which PML protein is under-expressed in gastric cancer cells, we analyzed all exons and intron-exon boundaries of PML gene in 50 formalin-fixed paraffin-embedded tissue blocks from gastric carcinoma tumors by means of PCR-SSCP and CSGE, with direct sequencing of abnormally shifted bands. We found a novel sequence variant of unknown significance localized in intron 5 in 3 samples (c.1398+84delA). We did not detect any deleterious mutations of the PML gene. This study shows that PML mutations may not contribute to gastric adenocarcinoma development. Post-translational modifications or protein degradation might be mechanisms by which PML is not expressed in gastric tumors.
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EFFECT OF CARBON NANOTUBES ON THE KINETICS OF IN SITU POLYMERIZATION OF METHYL METHACRYLATE
MEHDI SALAMI-KALAJAHI,VAHID HADDADI-ASL,FARID BEHBOODI-SADABAD,SAEID RAHIMI-RAZIN,HOSSEIN ROGHANI-MAMAQANI,MAHMOUD HEMMATI 성균관대학교(자연과학캠퍼스) 성균나노과학기술원 2012 NANO Vol.7 No.1
The effect of carbon nanotubes on the kinetics of free radical polymerization of methyl methacrylate (MMA) was investigated. To do this, pristine, acid treated, alcoholic and methacrylate-modified carbon nanotubes with different loadings were used and Conversion, molecular weight and polydispersity index (PDI) of all samples were monitored during polymerization. The results show that carbon nanotubes induce an induction time to polymerization system which is independent of modification system while decrease in monomer conversion can be improved by developing organic moieties on surface. Molecular weight and polydispersity index for free and attached-on-surface chains were studied separately and different kinetics behaviors were observed for them. Molecular weight of free chains was increased by adding carbon nanotubes while more modified nanotubes resulted in much increased molecular weight. On the other hand, more system stability of more modified nanotubes, which was tested using UV-Visible spectra, resulted in higher molecular weights. Adding more nanotubes in the case of MMA-modified nanotubes caused to determine an optimum loading value to reach maximum molecular weight of free chains which was ascribed to system stability according to UV-Visible results. In this optimum loading value, free chains had minimum PDI value. However, increasing carbon nanotubes content led to decreased molecular weight of attached chains while PDI values increased because of shielding effect as physical phenomenon.
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LysRS Serves as a Key Signaling Molecule in the Immune Response by Regulating Gene Expression
Yannay-Cohen, Nurit,Carmi-Levy, Irit,Kay, Gillian,Yang, Christopher Maolin,Han, Jung Min,Kemeny, D. Michael,Kim, Sunghoon,Nechushtan, Hovav,Razin, Ehud Elsevier 2009 Molecular cell Vol.34 No.5
<P><B>Summary</B></P><P>Lysyl-tRNA synthetase (LysRS) was found to produce diadenosine tetraphosphate (Ap<SUB>4</SUB>A) in vitro more than two decades ago. Here, we used LysRS silencing in mast cells in combination with transfected normal and mutated LysRS to demonstrate in vivo the critical role played by LysRS in the production of Ap<SUB>4</SUB>A in response to immunological challenge. Upon such challenge, LysRS was phosphorylated on serine 207 in a MAPK-dependent manner, released from the multisynthetase complex, and translocated into the nucleus. We previously demonstrated that LysRS forms a complex with MITF and its repressor Hint-1, which is released from the complex by its binding to Ap<SUB>4</SUB>A, enabling MITF to transcribe its target genes. Here, silencing LysRS led to reduced Ap<SUB>4</SUB>A production in immunologically activated cells, which resulted in a lower level of MITF inducible genes. Our data demonstrate that specific LysRS serine 207 phosphorylation regulates Ap<SUB>4</SUB>A production in immunologically stimulated mast cells, thus implying that LysRS is a key mediator in gene regulation.</P>
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Structural Switch of Lysyl-tRNA Synthetase between Translation and Transcription
Ofir-Birin, Y.,Fang, P.,Bennett, Steven P.,Zhang, H.M.,Wang, J.,Rachmin, I.,Shapiro, R.,Song, J.,Dagan, A.,Pozo, J.,Kim, S.,Marshall, Alan G.,Schimmel, P.,Yang, X.L.,Nechushtan, H.,Razin, E.,Guo, M. Cell Press 2013 Molecular Cell Vol.49 No.1
Lysyl-tRNA synthetase (LysRS), a component of the translation apparatus, is released from the cytoplasmic multi-tRNA synthetase complex (MSC) to activate the transcription factor MITF in stimulated mast cells through undefined mechanisms. Here we show that Ser207 phosphorylation provokes a new conformer of LysRS that inactivates its translational function but activates its transcriptional function. The crystal structure of an MSC subcomplex established that LysRS is held in the MSC by binding to the N terminus of the scaffold protein p38/AIMP2. Phosphorylation-created steric clashes at the LysRS domain interface disrupt its binding grooves for p38/AIMP2, releasing LysRS and provoking its nuclear translocation. This alteration also exposes the C-terminal domain of LysRS to bind to MITF and triggers LysRS-directed production of the second messenger Ap<SUB>4</SUB>A that activates MITF. Thus our results establish that a single conformational change triggered by phosphorylation leads to multiple effects driving an exclusive switch of LysRS function from translation to transcription.
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