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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.

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        Non-radiative healing assessment techniques for fractured long bones and osseointegrated implant

        S. Lu,B. S. Vien,M. Russ,M. Fitzgerald,W. K. Chiu 대한의용생체공학회 2020 Biomedical Engineering Letters (BMEL) Vol.10 No.1

        The paper provides an overview of the fracture healing process of long bones, a review of work that proposed appropriatephysical parameters for the assessment of healing and highlights some recent work that reported on the development ofnon-radiative technique for healing assessment. An overview of the development and monitoring of osseointegration fortrans-femoral osseointegrated implant is also presented. The state of healing of a fractured long bone and the stability ofosseointegrated implants can be seen as engineering structural components where the mechanical properties are restored tofacilitate their desired function. To this end, this paper describes non-radiative techniques that are useful for healing assessmentand the stability assessment of osseointegrated implants. The achievement of non-radiative quantitative assessmentmethodologies to determine the state of healing of fractured long bones and to assess the stability of osseointegrated implantwill shorten the patient’s rehabilitation time, allowing earlier mobility and return to normal activities. Recent work on thedevelopment of assessment techniques supported by the Offi ce of Naval Research as part of the Monitoring of OsseointegratedImplant Prosthesis program is highlighted.

      • Subtle Chemical Shifts Explain the NMR Fingerprints of Oligomeric Proanthocyanidins with High Dentin Biomodification Potency

        ( Joo Won Nam ),( Rasika S Phansalkar ),( David C Lankin ),( Jonathan Bisson ),( James B Mcalpine ),( Ariene A Leme ),( Cristina M P Vidal ),( Benjamin Ramirez ),( Matthias Niemitz ),( Ana Bedran Russ 영남대학교 약품개발연구소 2016 영남대학교 약품개발연구소 연구업적집 Vol.26 No.-

        The ability of certain oligomeric proanthocya-nidins (OPACs) to enhance the biomechanical properties of dentin involves collagen cross-linking of the 1.3-4.5 nm wide space via protein-polyphenol interactions. A systematic interdisciplinary search for the bioactive principles of pine bark has yielded the trimeric PAC, ent-epicatechin-(4β →S)-epicatechin-(2β→0→7,4β→8)-catechin (3), representing the hitherto most potent single chemical entity capable of enhancing dentin stiffness. Building the case from two congeneric PAC dimers, a detailed structural analysis decoded the stereochemistry, spatial arrangement, and chemical properties of three dentin biomodifiers, Quantum-mechanics-driven <sup>1</sup>H iterative full spin analysis (QM-HiFSA) of NMR spectra distinguished previously unrecognized details such as higher order J coupling and provided valuable information about 3D structure. Detection and quantification of H/D-exchange effects by QM-HiFSA identified C-S and C-6 as (re) active sites, explain preferences in biosynthetic linkage, and suggest their involvement in dentin cross-linking activity. Mapping of these molecular properties underscored the significance of high 8 precision in both <sup>1</sup>H and <sup>13</sup>C NMR spectroscopy. Occurring at low- to subppb levels, these newly characterized chemical shift differences in ppb are small but diagnostic measures of dynamic processes inherent to the OPAC pharmacophores and can help augment our understanding of nanometer-scale intermolecular interactions in biomodified dentin macromolecules.

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