{"title":"Photocycloaddition of 6-chloro-1,3-dimethyluracil to benzene.","authors":"K. Seki, K. Ohkura, N. Sasaki","doi":"10.1002/CHIN.200024154","DOIUrl":"https://doi.org/10.1002/CHIN.200024154","url":null,"abstract":"","PeriodicalId":19394,"journal":{"name":"Nucleic acids symposium series","volume":"68 1","pages":"7-8"},"PeriodicalIF":0.0,"publicationDate":"2010-06-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86094047","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"mRNA stability and the control of gene expression.","authors":"S. Liebhaber","doi":"10.1002/9780470015902.A0005972.PUB2","DOIUrl":"https://doi.org/10.1002/9780470015902.A0005972.PUB2","url":null,"abstract":"The stability of an mRNA plays a major role in the determination of gene expression. The stability of an mRNA reflects its primary and higher-order structure, as well as its interactions with a variety of trans-acting RNA-binding proteins. Both of these parameters can control the function of the mRNA and its exposure to rate limiting nuclease digestion. The specific determinants of mRNA stability are now being worked out in well defined model systems. The unusual stability of globin mRNAs, necessitated by the prolonged posttranscriptional phase of erythroid differentiation, presents a potentially informative example of stability control.","PeriodicalId":19394,"journal":{"name":"Nucleic acids symposium series","volume":"32 1","pages":"29-32"},"PeriodicalIF":0.0,"publicationDate":"2007-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87390266","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Y. Sakamoto, N. Tanaka, T. Ichimiya, T. Kurihara, Kazuo T. Nakamura
{"title":"Three-dimensional structure of a cyclic-nucleotide phosphodiesterase from human brain.","authors":"Y. Sakamoto, N. Tanaka, T. Ichimiya, T. Kurihara, Kazuo T. Nakamura","doi":"10.5940/JCRSJ.47.403","DOIUrl":"https://doi.org/10.5940/JCRSJ.47.403","url":null,"abstract":"2',3'-Cyclic-nucleotide 3'-phosphodiesterase (CNP) is found mainly in the central nervous system of vertebrates and catalyzes the hydrolysis of 2',3'-cyclic nucleotides to produce 2'-nucleotides in vitro. Recently, CNP has been identified as a member of the 2H phosphoesterase superfamily. Here we have determined the crystal structure of the catalytic fragment of human CNP (hCNP-CF) at 1.3 A resolution.","PeriodicalId":19394,"journal":{"name":"Nucleic acids symposium series","volume":"8 1","pages":"157-8"},"PeriodicalIF":0.0,"publicationDate":"2005-12-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78814033","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Hitoshi Suzuki, H. Kaneko, N. Tamai, N. Miyano-kurosaki, K. Hashimoto, K. Shimotohno, H. Takaku
{"title":"Suppression of HCV RNA replication by baculovirus-mediated shRNA expression.","authors":"Hitoshi Suzuki, H. Kaneko, N. Tamai, N. Miyano-kurosaki, K. Hashimoto, K. Shimotohno, H. Takaku","doi":"10.1016/J.ANTIVIRAL.2008.01.099","DOIUrl":"https://doi.org/10.1016/J.ANTIVIRAL.2008.01.099","url":null,"abstract":"","PeriodicalId":19394,"journal":{"name":"Nucleic acids symposium series","volume":"16 1","pages":"339-40"},"PeriodicalIF":0.0,"publicationDate":"2005-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87042763","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cloning and sequencing of ftsZ homolog from extremely halophilic archaeon Haloarcula japonica strain TR-1.","authors":"O Kazumichi, R Yatsunami, S Nakamura","doi":"10.1093/nass/44.1.155","DOIUrl":"https://doi.org/10.1093/nass/44.1.155","url":null,"abstract":"<p><p>The gene encoding FtZ was cloned from triangular disc-shaped extremely halophilic archaeon Haloarcula japonica strain TR-1. Nucleotide sequencing analysis of the possible ftsZ gene revealed that the structural gene consisted of an open reading frame of 1,182 nucleotides encoding 394 amino acids. The deduced amino acid sequence of the Ha. japonica FtsZ showed high identities with those Halobacterium salinarom, Haloferax volcanii and Haloferax mediterranei FtsZs.</p>","PeriodicalId":19394,"journal":{"name":"Nucleic acids symposium series","volume":" 44","pages":"155-6"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/nass/44.1.155","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22517388","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Design and synthesis of curcumin-bioconjugates to improve systemic delivery.","authors":"S Kumar, K K Dubey, S Tripathi, M Fujii, K Misra","doi":"10.1093/nass/44.1.75","DOIUrl":"https://doi.org/10.1093/nass/44.1.75","url":null,"abstract":"<p><p>Di-O-glycinoyl curcumin (I), di-O-glycinoyl-C4-glycyl-curcumin (II), 5'-deoxy-5'-curcuminyl thymidine (5'-cur-T) (III) and 2'-deoxy-2'-curcuminyl uridine (2'-cur-U) (IV) have been synthesized and characeterised by elemental analysis & 1H NMR. The antibacterial activities of these four bioconjugates has been tested particularly for multiresistant micro-organisms. Best results are shown by I & IV. These bioconjugates serve dual purpose of systemic delivery as well as therapeutic agents against viral diseases.</p>","PeriodicalId":19394,"journal":{"name":"Nucleic acids symposium series","volume":" 44","pages":"75-6"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/nass/44.1.75","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22517649","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
F Nagatsugi, D Usui, T Kawasaki, M Maeda, S Sasaki
{"title":"Design and synthesis of the novel cross-linking reagents triggered by the triple helix formation.","authors":"F Nagatsugi, D Usui, T Kawasaki, M Maeda, S Sasaki","doi":"10.1093/nass/44.1.39","DOIUrl":"https://doi.org/10.1093/nass/44.1.39","url":null,"abstract":"<p><p>In our attempt to new nucleobase analogs capable of interstrand cross-linking, we developed 2-amino-6-vinyl purine analog (1). The oligonucleotides incorporating 1 showed efficient interstrand cross-linking with selectivity toward cytidine at a target site. In this paper, we describe the design of the new cross-linking reagents (2) bearing 2-amino-6-vinyl purine motif, and triplex-directed alkylation with 2 to double-stranded DNA.</p>","PeriodicalId":19394,"journal":{"name":"Nucleic acids symposium series","volume":" 44","pages":"39-40"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/nass/44.1.39","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22517735","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
T Sugiyama, A Kittaka, H Takayama, M Tomioka, Y Ida, R Kuroda
{"title":"Interaction of peptides derived from RecA with single-stranded oligonucleotides containing 5-formyl-2'-deoxyuridine.","authors":"T Sugiyama, A Kittaka, H Takayama, M Tomioka, Y Ida, R Kuroda","doi":"10.1093/nass/44.1.41","DOIUrl":"https://doi.org/10.1093/nass/44.1.41","url":null,"abstract":"<p><p>We report the first example of chemical cross-linking of 5-formyl-2'-deoxyuridine containing oligonucleotides with oligopeptides through a Schiff base formation. Twenty amino acid residue peptides investigated here were derived from the DNA binding site of RecA protein. We have demonstrated that the lysine residue placed at the 6th or 8th position from the N-terminus of the peptide directly contacts with DNA.</p>","PeriodicalId":19394,"journal":{"name":"Nucleic acids symposium series","volume":" 44","pages":"41-2"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/nass/44.1.41","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22517736","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Analysis of the RNase H activity by fluorescence resonance energy transfer.","authors":"H Miyashiro, T Kimura, M Tomiyama, M Hattori","doi":"10.1093/nass/44.1.55","DOIUrl":"https://doi.org/10.1093/nass/44.1.55","url":null,"abstract":"<p><p>The RNase H activity of HIV-1 reverse transcriptase was examined using chemically synthesized deoxyribo.ribo-oligonucleotide hybrid duplex labeled with the fluorescence donor at the 5'-end and with the fluorescence acceptor at the 3'-end of DNA strand as a substrate. Fluorescence resonance energy transfer (FRET) between these fluorescent dyes was used to analyze the rate of the enzymatic reaction. Under excitation of the donor dye, that is 6-carboxyfluorescein (6-FAM), at 490 nm, the increase of the fluorescence resulting from the acceptor dye, that is 6-carboxytetramethylrhodamine (TAMRA), at 578 nm, was observed depending on the degradation of DNA.RNA hybrid duplex. This method can be introduced into the high throughput screening of the inhibitors against the RNase H activity for anti-HIV drug.</p>","PeriodicalId":19394,"journal":{"name":"Nucleic acids symposium series","volume":" 44","pages":"55-6"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/nass/44.1.55","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22517743","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Synthesis and conformation control of peptide ribonucleic acid containing 5'-amino-5'-deoxyribopurinenucleosides.","authors":"H Sato, N Minamimoto, T Wada, Y Inoue","doi":"10.1093/nass/44.1.211","DOIUrl":"https://doi.org/10.1093/nass/44.1.211","url":null,"abstract":"<p><p>A novel nucleic acid model, i.e. peptide ribonucleic acid (PRNA), tethering 5'-amino-5'-deoxypyrimidine ribonucleoside as a recognition site for nucleic acids, has been designed and synthesized. We have demonstrated that the recognition behavior of PRNA with complementary oligopurinenucleotides can be controlled externally through the orientational switching of the pyrimidine nucleobase of PRNA induced by added borates. We extend this methodology of controlling the nucleobase orientation and recognition behavior of novel mono and oligomeric PRNAs containing 5'-amino-5'-deoxypyrimidine and/or purinenucleosides. In case of the PRNA oligomer containing pyrimidine-purine mixed sequence, efficient orientational switching of nucleobases induced by added borates was also observed.</p>","PeriodicalId":19394,"journal":{"name":"Nucleic acids symposium series","volume":" 44","pages":"211-2"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/nass/44.1.211","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22517745","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}