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The human AQP4 gene : Definition of the locus encoding two water channel polypeptides in brain
LU, MINGOI,LEE, M.DOUGLAS,SMITH, BARBARA L.,JUNG, JIN SUP,AGRE, PETER,VERDUK, MARIAN A.J.,MERKX, GERARD,RUSS, JOHAN P.L.,DEEN, PETER M.T. 부산대학교 유전공학연구소 1996 분자생물학 연구보 Vol.12 No.-
The aquaporin family of membrane water transport proteins are expressed in diverse tissues, and in brain the predominant water channel protein is AQP4. Here we report the isolation and characterization of the human AQP4 cDNAs and genomic DNA. Two cDNAs were isolated corresponding to the two initiating methionines (M1 in a 323-aa polypeptide and M23 in a 301-aa polypeptide) previously indentified in rat [Jung, J. S., Bhat, R. V., Preston, G. M., Guggino, W. B. & Agre, P. (1994) Proc. Natl. Acad. Sci. USA 91, 13052-13056]. Similar to other aquaporins, the AQP4 gene is composed of four exons encoding 127, 55, 27, and 92 amino acids separated by introns of 0.8, 0.3, and 5.2 kb. Unlike other aquaporins, an alternative coding initiation sequence (designated exon 0) was located 2.7 kb upstream of exon 1. When spliced together, M1 and the subsequent 10 amino acids are encoded by exon 0; the next 11 amino acids and M23 are encoded by exon 1. Transcription initiation sites have been mapped in the proximal promoters of exons 0 and 1. RNase protection revealed distinct transcripts corresponding to M1 and M23 mRNAs, and AQP4 immunoblots of cerebellum demonstrated reactive polypeptides of 31 and 34 kDa. Using a P1 and a λEMBL subclone, the chromosomal site of the human AQP4 gene was mapped to chromosome 18 at the junction of q11.2 and q12.1 by fluorescence in situ hybridization. These studies may now permit molecular characterization of AQP4 during human development and in clinical disorders.
Molecular characterization of swine leucocyte antigen class I genes in outbred pig populations
Ho, C.-S.,Lunney, J. K.,Franzo-Romain, M. H.,Martens, G. W.,Lee, Y.-J.,Lee, J.-H.,Wysocki, M.,Rowland, R. R. R.,Smith, D. M. Blackwell Publishing Ltd 2009 Animal genetics Vol.40 No.4
<P>Summary</P><P>The highly polymorphic <I>swine leucocyte antigen</I> (<I>SLA</I>) genes are one of the most important determinants in swine immune responses to infectious diseases, vaccines, and in transplantation success. Study of SLA influence requires accurate and effective typing methods. We developed a simple and rapid method to type alleles at the three classical SLA class I loci (<I>SLA-1</I>, <I>SLA-3</I> and <I>SLA-2</I>) using the PCR-sequence-specific primer (PCR-SSP) strategy. This typing system relies on 47 discriminatory PCR primer pairs designed to amplify the SLA class I alleles by groups that have similar sequence motifs. We applied this low-resolution group-specific typing method to characterize the SLA class I alleles present in three outbred pig populations (<I>n = </I>202). Alleles from 24 class I allele groups corresponding to 56 class I genotypes were detected. We also identified 23 low-resolution SLA class I haplotypes in these pigs and found haplotypes Lr-1.0 (<I>SLA-1</I>*01XX-<I>SLA-3</I>*01XX-<I>SLA-2</I>*01XX) and Lr-4.0 (<I>SLA-1</I>*04XX-<I>SLA-3</I>*04XX-<I>SLA-2</I>*04XX) in all three pig populations with a high prevalence. Over 80% of the pigs examined (<I>n </I>=<I> </I>162) were found to bear at least one of these haplotypes, resulting in a combined haplotype frequency of nearly 50%. This PCR-SSP-based typing system demonstrates a reliable and unambiguous detection of SLA class I alleles, and can be used to effectively investigate the SLA diversity in outbred pig populations. It will help to identify the role of SLA antigens in disease-resistant pigs and may facilitate the development of effective vaccines.</P>
Silicon nanoparticles–graphene paper composites for Li ion battery anodes
Lee, Jeong K.,Smith, Kurt B.,Hayner, Cary M.,Kung, Harold H. Royal Society of Chemistry 2010 Chemical communications Vol.46 No.12
<P>Composites of Si nanoparticles highly dispersed between graphene sheets, and supported by a 3-D network of graphite formed by reconstituting regions of graphene stacks exhibit high Li ion storage capacities and cycling stability. An electrode was prepared with a storage capacity >2200 mA h g<SUP>−1</SUP> after 50 cycles and >1500 mA h g<SUP>−1</SUP> after 200 cycles that decreased by <0.5% per cycle.</P> <P>Graphic Abstract</P><P>Composites of Si nanoparticles highly dispersed between graphene sheets, and supported by a 3-D network of graphite formed by reconstituting regions of graphene stacks exhibit high Li ion storage capacities and cycling stability. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=b919738a'> </P>
LEGACY EXTRAGALACTIC UV SURVEY (LEGUS) WITH THE<i>HUBBLE SPACE TELESCOPE</i>. I. SURVEY DESCRIPTION
Calzetti, D.,Lee, J. C.,Sabbi, E.,Adamo, A.,Smith, L. J.,Andrews, J. E.,Ubeda, L.,Bright, S. N.,Thilker, D.,Aloisi, A.,Brown, T. M.,Chandar, R.,Christian, C.,Cignoni, M.,Clayton, G. C.,Silva, R. da,Mi IOP Publishing 2015 The Astronomical journal Vol.149 No.2
NEUTRONICS MODELING AND SIMULATION OF SHARPFOR FAST REACTOR ANALYSIS
W. S. YANG,M. A. SMITH,C. H. LEE,A. WOLLABER,D. KAUSHIK,A. S. MOHAMED 한국원자력학회 2010 Nuclear Engineering and Technology Vol.42 No.5
This paper presents the neutronics modeling capabilities of the fast reactor simulation system SHARP, which ANL isdeveloping as part of theU.S. DOE’s NEAMS program. We discuss the three transport solvers (PN2ND, SN2ND, and MOCFE)implementedin the UNIC code along with the multigroup cross section generation code MC2-3. We describe the solution methodsand modelingcapabilities, and discuss the improvement needs for each solver, focusing on massively parallel computation.We present the performance test results against various benchmark problems and ZPR-6 and ZPPR critical experiments. We alsodiscuss weakand strong scalability results for the SN2ND solver on the ZPR-6 critical assembly benchmarks.
P2Y1 receptor signaling is controlled by interaction with the PDZ scaffold NHERF-2
Fam, S. R.,Paquet, M.,Castleberry, A. M.,Oller, H.,Lee, C. J.,Traynelis, S. F.,Smith, Y.,Yun, C. C.,Hall, R. A. Proceedings of the National Academy of Sciences 2005 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.102 No.22
<P>P2Y(1) purinergic receptors (P2Y(1)Rs) mediate rises in intracellular Ca(2+) in response to ATP, but the duration and characteristics of this Ca(2+) response are known to vary markedly in distinct cell types. We screened the P2Y(1)R carboxyl terminus against a recently created proteomic array of PDZ (PSD-95/Drosophila Discs large/ZO-1 homology) domains and identified a previously unrecognized, specific interaction with the second PDZ domain of the scaffold NHERF-2 (Na(+)/H(+) exchanger regulatory factor type 2). Furthermore, we found that P2Y(1)R and NHERF-2 associate in cells, allowing NHERF-2-mediated tethering of P2Y(1)R to key downstream effectors such as phospholipase Cbeta. Finally, we found that coexpression of P2Y(1)R with NHERF-2 in glial cells prolongs P2Y(1)R-mediated Ca(2+) signaling, whereas disruption of the P2Y(1)R-NHERF-2 interaction by point mutations attenuates the duration of P2Y(1)R-mediated Ca(2+) responses. These findings reveal that NHERF-2 is a key regulator of the cellular activity of P2Y(1)R and may therefore determine cell-specific differences in P2Y(1)R-mediated signaling.</P>