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Engrailed protects mouse midbrain dopaminergic neurons against mitochondrial complex I insults
Alvarez-Fischer, Daniel,Fuchs, Julia,Castagner, Fran챌ois,Stettler, Olivier,Massiani-Beaudoin, Olivia,Moya, Kenneth L,Bouillot, Colette,Oertel, Wolfgang H,Lomb챔s, Anne,Faigle, Wolfgang,Joshi, Rajiv L,H Nature Publishing Group, a division of Macmillan P 2011 NATURE NEUROSCIENCE Vol.14 No.10
Mice heterozygous for the homeobox gene Engrailed-1 (En1) display progressive loss of mesencephalic dopaminergic (mDA) neurons. We report that exogenous Engrailed-1 and Engrailed-2 (collectively Engrailed) protect mDA neurons from 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), a mitochondrial complex I toxin used to model Parkinson's disease in animals. Engrailed enhances the translation of nuclearly encoded mRNAs for two key complex I subunits, Ndufs1 and Ndufs3, and increases complex I activity. Accordingly, in vivo protection against MPTP by Engrailed is antagonized by Ndufs1 small interfering RNA. An association between Engrailed and complex I is further confirmed by the reduced expression of Ndufs1 and Ndufs3 in the substantia nigra pars compacta of En1 heterozygous mice. Engrailed also confers in vivo protection against 6-hydroxydopamine and 慣-synuclein-A30P. Finally, the unilateral infusion of Engrailed into the midbrain increases striatal dopamine content, resulting in contralateral amphetamine-induced turning. Therefore, Engrailed is both a survival factor for adult mDA neurons and a regulator of their physiological activity.
Clustering Social Media Services and Messengers by Functionality
Fischer, Julia,Knapp, Daniel,Nguyen, Bich Chau,Richter, Daniel,Shutsko, Aliaksandra,Stoppe, Melanie,Williams, Kelly,Ilhan, Aylin,Stock, Wolfgang G. Korea Institute of Science and Technology Informat 2020 Journal of Information Science Theory and Practice Vol.8 No.4
The objective of this research is to analyze which functions make up web-based as well as mobile social media services and messengers. Services are clustered by their functionality. A total of 640 individual functions were identified, while investigating altogether 44 selected services in their web and mobile versions. Applying content analysis, functions were assigned to the services. The services were ranked by the number of implemented functions, and the functions were ranked by their occurrence in the services. Cluster analysis was applied to classify the services according to their functionality. Facebook and VKontakte were found to be the ones with the most functions; the most frequently implemented functions are support, profile, and account-related. Cluster analysis revealed six classes for mobile and seven classes for web applications. There is a noteworthy difference regarding the functionality scope between web and mobile applications of the same services. An example for this is Mendeley with 38 functions in the mobile and 91 functions in the web version. This is the first empirical attempt at clustering social media services based on their functionality.
Hubert Mecke,Reinhard Doebbelin,Wolfgang Fischer 전력전자학회 1998 ICPE(ISPE)논문집 Vol.- No.-
In recent years inverter power sources are more and more used for resistance welding processes. In this paper some results of investigation into the static and dynamic behavior of high-current rectifier diodes used in these inverter power sources will be discussed. By means of digital simulation, losses and efficiency have been determined depending on the power semiconductor parameters.<br/>
Ligand Binding Properties of the N-Terminal Domain of Riboflavin Synthase from Escherichia coli
( Chan Yong Lee ),( Boris Illarionov ),( Young Eun Woo ),( Kristina Kemter ),( Ryu Ryun Kim ),( Sabine Eberhardt ),( Mark Cushman ),( Wolfgang Eisenreich ),( Markus Fischer ),( Adelbert Bacher ) 생화학분자생물학회 2007 BMB Reports Vol.40 No.2
Ligand Binding Properties of the N-Terminal Domain of Riboflavin Synthase from Escherichia coli
Lee, Chan-Yong,Illarionov, Boris,Woo, Young-Eun,Kemter, Kristina,Kim, Ryu-Ryun,Eberhardt, Sabine,Cushman, Mark,Eisenreich, Wolfgang,Fischer, Markus,Bacher, Adelbert Korean Society for Biochemistry and Molecular Biol 2007 Journal of biochemistry and molecular biology Vol.40 No.2
Riboflavin synthase from Escherichia coli is a homotrimer of 23.4 kDa subunits and catalyzes the formation of one molecule each of riboflavin and 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione by the transfer of a 4-carbon moiety between two molecules of the substrate, 6,7- dimethyl-8-ribityllumazine. Each subunit comprises two closely similar folding domains. Recombinant expression of the N-terminal domain is known to provide a $C_2$-symmetric homodimer. In this study, the binding properties of wild type as well as two mutated proteins of N-terminal domain of riboflavin synthase with various ligands were tested. The replacement of the amino acid residue A43, located in the second shell of riboflavin synthase active center, in the recombinant N-terminal domain dimer reduces the affinity for 6,7-dimethyl-8-ribityllumazine. The mutation of the amino acid residue C48 forming part of activity cavity of the enzyme causes significant $^{19}F$ NMR chemical shift modulation of trifluoromethyl derivatives of 6,7-dimethyl-8-ribityllumazine in complex with the protein, while substitution of A43 results in smaller chemical shift changes.