Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression最新文献

{"title":"Functional characterization of the promoter of human kinetochore protein HEC1: Novel link between regulation of the cell cycle protein and CREB family transcription factors","authors":"Liansheng Cheng,&nbsp;Liangwei Li,&nbsp;Xinxian Qiao,&nbsp;Jing Liu,&nbsp;Xuebiao Yao","doi":"10.1016/j.bbaexp.2007.07.005","DOIUrl":"10.1016/j.bbaexp.2007.07.005","url":null,"abstract":"<div><p>HEC1 (highly expressed in cancer), which localizes to kinetochore in cell mitosis, plays an essential role in chromosome segregation for M phase progression. To clarify the mechanism of its transcriptional regulation, we searched out and isolated its 5′-flanking region. Mapping of this region identified that it is a TATA-less promoter and contains several putative binding sites for different transcription factors. The results from HeLa cells transfected with pGL3 luciferase reporter vectors containing progressive deletion of the <em>HEC1</em> 5′-flanking region demonstrated that two elements containing binding sites for cAMP responsive element binding (CREB) protein and activating transcription factor 4 (ATF4 or CREB2) are critical for transcriptional activity. Mutation of the two elements, not downstream E2F box, resulted in a significant reduction of the promoter activity. Gel shift and supershift assays also demonstrated specific binding of transcription factors to their putative binding sites. Furthermore, overexpression of either CREB or ATF4 enhanced the activation of the <em>HEC1</em> promoter and overexpression of both of them had an additive effect on the activation of the <em>HEC1</em> transcription. Conversely, overexpression of dominant negative mutants of either CREB or ATF4 resulted in downregulation of <em>HEC1</em> mRNA significantly. Our study provided a new insight into a potential mechanism of how transcription factors of CREB family are involved in the regulation of kinetochore protein HEC1 in cancer-related cells.</p></div>","PeriodicalId":100161,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression","volume":"1769 9","pages":"Pages 593-602"},"PeriodicalIF":0.0,"publicationDate":"2007-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bbaexp.2007.07.005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27004948","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":"The Popdc gene family in the rat: Molecular cloning, characterization and expression analysis in the heart and cultured cardiomyocytes","authors":"Doris Parnes ,&nbsp;Vered Jacoby ,&nbsp;Avital Sharabi ,&nbsp;Hadassa Schlesinger ,&nbsp;Thomas Brand ,&nbsp;Gania Kessler-Icekson","doi":"10.1016/j.bbaexp.2007.06.001","DOIUrl":"10.1016/j.bbaexp.2007.06.001","url":null,"abstract":"<div><p>Three Popeye domain-containing (<em>Popdc 1–3</em>) family-members are known in vertebrates. Their exact function is as yet unknown although involvement in cell adhesion has been suggested. We report herein sequencing of the rat <em>Popdc 1–3</em> cDNAs that show high homology to other vertebrate orthologs and are expressed primarily in the heart and skeletal muscles. <em>Popdc2</em> splice variants were identified, with <em>Popdc2C</em> showing a distinctive age-dependent decline. In isolated cardiomyocytes, <em>Popdc</em> genes were negatively regulated by serum, an effect that was reversed by EGFR-kinase inhibition, suggesting an EGFR-dependent modulation of <em>Popdc</em> gene expression.</p></div>","PeriodicalId":100161,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression","volume":"1769 9","pages":"Pages 586-592"},"PeriodicalIF":0.0,"publicationDate":"2007-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bbaexp.2007.06.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26857471","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":"The identification and sequence analysis of a new Reg3gamma and Reg2 in the Syrian golden hamster","authors":"Mauro L. Castellarin,&nbsp;Maria Petropavlovskaia,&nbsp;Mark A. Lipsett,&nbsp;Lawrence Rosenberg","doi":"10.1016/j.bbaexp.2007.06.002","DOIUrl":"10.1016/j.bbaexp.2007.06.002","url":null,"abstract":"<div><p>The regenerating (<em>Reg</em>) genes are associated with tissue repair and have been directly implicated in pancreatic β-cell regeneration. <em>A hamster Reg3, Islet neogenesis associated protein</em> (INGAP), has been shown to possess anti-diabetic properties in rodent models. Although several <em>Reg3</em> proteins have been identified in other species, INGAP is the only <em>Reg3</em> found in hamsters. To identify new <em>Reg3</em> genes in the hamster pancreas we employed homology reverse transcription polymerase chain reaction (RT-PCR) using degenerate <em>Reg3</em> primers, followed by rapid amplification of cDNA ends (RACE). We report here the discovery of a new hamster <em>Reg3</em> gene of 765 nucleotides (nt) that encodes a 174-amino acid (aa) protein. This protein sequence was identified as a novel hamster <em>Reg3</em>γ with 78% and 75% identity to the rat <em>Reg3</em>γ and mouse <em>Reg3</em>γ protein, respectively. We also fully sequenced the previously reported partial sequence of the hamster <em>Reg1</em> gene coding region using RACE to yield a 756-nt transcript that encodes a deduced 173 aa protein. This protein was identified as hamster <em>Reg2</em>, rather than <em>Reg1</em> as was initially reported, with an 81% identity to mouse <em>Reg2</em>. The spatial gene expression patterns of the hamster Reg genes, analyzed by RT-PCR, were similarly distributed with low level expression being found globally throughout the body. Mice and hamsters are the only species known to carry either of the functional <em>INGAP</em> or <em>Reg2</em> genes. It remains to be determined whether these genes bestow mice and hamsters with special regenerative abilities in the pancreas.</p></div>","PeriodicalId":100161,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression","volume":"1769 9","pages":"Pages 579-585"},"PeriodicalIF":0.0,"publicationDate":"2007-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bbaexp.2007.06.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26866599","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":"YB-1 binds to the MMP-13 promoter sequence and represses MMP-13 transactivation via the AP-1 site","authors":"Shaija Samuel ,&nbsp;Katherine K. Beifuss ,&nbsp;Lori R. Bernstein","doi":"10.1016/j.bbaexp.2007.07.003","DOIUrl":"10.1016/j.bbaexp.2007.07.003","url":null,"abstract":"<div><p>Matrix metalloproteinases (MMPs) are key enzymes that implement degradation of the extracellular matrix during cellular invasion in development, tissue remodeling, and pathogenic disease states. MMP-13 has pivotal roles in the pathogenesis of invasive cancers and arthritis. Here we report the identification of Y-box binding protein-1 (YB-1) as a new repressor of MMP-13 transactivation. YB-1 binds in vitro in DNA affinity chromatography to the activator protein-1 (AP-1) DNA sequence within the MMP-13 promoter. Chromatin immunoprecipitation assays reveal that YB-1 binds in living cells to the MMP-13 gene promoter to a region of the MMP-13 promoter containing the AP-1 site. YB-1 represses tumor promoter-induced MMP-13 promoter transactivation at the AP-1 site. This is the first report demonstrating YB-1 binding in vitro and in living cells to a mammalian AP-1 target gene, and the first report of YB-1 regulation of the MMP-13 promoter.</p></div>","PeriodicalId":100161,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression","volume":"1769 9","pages":"Pages 525-531"},"PeriodicalIF":0.0,"publicationDate":"2007-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bbaexp.2007.07.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27004951","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":"HDAC1 bound to the Cyp1a1 promoter blocks histone acetylation associated with Ah receptor-mediated trans-activation","authors":"Michael Schnekenburger,&nbsp;Li Peng,&nbsp;Alvaro Puga","doi":"10.1016/j.bbaexp.2007.07.002","DOIUrl":"10.1016/j.bbaexp.2007.07.002","url":null,"abstract":"<div><p>Metabolic bioactivation of polycyclic aromatic hydrocarbons, such as the environmental procarcinogen benzo[<em>a</em>]pyrene, is catalyzed by a cytochrome <em>P450</em> monooxygenase encoded by the substrate-inducible <em>Cyp1a1</em> gene. <em>Cyp1a1</em> induction requires <em>trans</em>-activation by the heterodimeric transcriptional complex formed by the liganded Ah receptor (AHR) and its partner, ARNT. Previously, we showed that constitutively bound HDAC1 dissociates from <em>Cyp1a1</em> promoter chromatin after ligand-mediated induction, concomitantly with the recruitment of AHR/ARNT complexes and p300. Here, we investigated the hypothesis that HDAC1 binding maintains the <em>Cyp1a1</em> gene in a silenced state in uninduced cells. We find that <em>Cyp1a1</em> induction by the AHR/ARNT is associated with modification of specific chromatin marks, including hyperacetylation of histone H3K14 and H4K16, trimethylation of histone H3K4, and phosphorylation of H3S10. HDAC1 and DNMT1 form complexes on the <em>Cyp1a1</em> promoter of uninduced cells but HDAC1 inhibition alone is not sufficient to induce <em>Cyp1a1</em> expression, although it allows for the hyperacetylation of H3K14 and H4K16 to levels similar to those found in B[<em>a</em>]P-induced cells. These results show that by blocking the modification of histone marks, HDAC1 plays a central role in <em>Cyp1a1</em> expression and that its removal is a necessary but not sufficient condition for <em>Cyp1a1</em> induction, underscoring the requirement for a concerted series of chromatin-remodeling events to complete the initial steps of gene <em>trans</em>-activation by the Ah receptor.</p></div>","PeriodicalId":100161,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression","volume":"1769 9","pages":"Pages 569-578"},"PeriodicalIF":0.0,"publicationDate":"2007-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bbaexp.2007.07.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26898291","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":"The transcriptional repression by NIPP1 is mediated by Polycomb group proteins","authors":"Nivedita Roy,&nbsp;Aleyde Van Eynde,&nbsp;Lijs Beke,&nbsp;Mieke Nuytten,&nbsp;Mathieu Bollen","doi":"10.1016/j.bbaexp.2007.07.004","DOIUrl":"10.1016/j.bbaexp.2007.07.004","url":null,"abstract":"<div><p>NIPP1 is a ubiquitously expressed nuclear protein that represses the transcription of targeted genes. Here we show that the transcriptional repression by NIPP1 is alleviated by the RNAi-mediated knockdown of EED and EZH2, two core components of the Polycomb Repressive Complex 2 (PRC2), and by the overexpression of a catalytically dead mutant of the histone methyltransferase EZH2. NIPP1 is present in a complex with EED and EZH2 <em>in vivo</em> and has distinct binding sites for these proteins. These data disclose an essential role for the PRC2 complex in the transcriptional repression by NIPP1.</p></div>","PeriodicalId":100161,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression","volume":"1769 9","pages":"Pages 541-545"},"PeriodicalIF":0.0,"publicationDate":"2007-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bbaexp.2007.07.004","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26990155","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":"Translational regulation of human methionine synthase by upstream open reading frames","authors":"Bekir Col ,&nbsp;Sebastian Oltean,&nbsp;Ruma Banerjee","doi":"10.1016/j.bbaexp.2007.06.003","DOIUrl":"10.1016/j.bbaexp.2007.06.003","url":null,"abstract":"<div><p>Methionine synthase is a key enzyme poised at the intersection of folate and sulfur metabolism and functions to reclaim homocysteine to the methionine cycle. The 5′ leader sequence in human MS is 394 nucleotides long and harbors two open reading frames (uORFs). In this study, regulation of the main open reading frame by the uORFs has been elucidated. Both uORFs downregulate translation as demonstrated by mutation of the upstream AUG codons (uAUG) either singly or simultaneously. The uAUGs are capable of recruiting the 40S ribosomal complex as revealed by their ability to drive reporter expression in constructs in which the luciferase is fused to the uORFs. uORF2, which is predicted to encode a 30 amino acid long polypeptide, has a clustering of rare codons encoding arginine and proline. Mutation of a tandemly repeated rare codon for arginine at positions 3 and 4 in uORF2 to either common codons for the same amino acid or common codons for alanine results in complete alleviation of translation inhibition. This suggests a mechanism for ribosome stalling and demonstrates that the cis-effects on translation by uORF2 is dependent on the nucleotide sequence but is apparently independent of the sequence of the encoded peptide. This study reveals complex regulation of the essential housekeeping gene, methionine synthase, by the uORFs in its leader sequence.</p></div>","PeriodicalId":100161,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression","volume":"1769 9","pages":"Pages 532-540"},"PeriodicalIF":0.0,"publicationDate":"2007-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bbaexp.2007.06.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26875759","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":"Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori","authors":"Hiromitsu Tanaka ,&nbsp;Hiroyuki Matsuki ,&nbsp;Seiichi Furukawa ,&nbsp;Aki Sagisaka ,&nbsp;Eiji Kotani ,&nbsp;Hajime Mori ,&nbsp;Minoru Yamakawa","doi":"10.1016/j.bbaexp.2007.07.001","DOIUrl":"10.1016/j.bbaexp.2007.07.001","url":null,"abstract":"<div><p>Two cDNAs designated <em>BmRelish1</em> and <em>2</em>, that encode Relish homologs, were cloned from the silkworm, <em>Bombyx mori.</em> BmRelish1 had an IκB-like domain with 5 ankyrin repeats in addition to Rel homology domain (RHD), nuclear localization signal (NLS), and acidic and hydrophobic amino acids (AHAA) rich regions. On the other hand, BmRelish2 lacked the AHAA and ankyrin repeats (ANK). Knockdown of the <em>BmRelish</em> gene in transgenic silkworms resulted in failure of the activation of antimicrobial peptide genes by <em>Escherichia coli</em>, suggesting that BmRelish plays an important role in antimicrobial peptide gene expression. Functional analysis of BmRelish1 and 2 in mbn-2 cells showed that both Relish homologs do not activate promoters of <em>B. mori</em> antimicrobial peptide genes encoding cecropin B1, attacin, lebocin 3 and lebocin 4. However, a gene construct BmRelish1-d2 lacking the ANK strongly activated promoters of these genes. Another gene construct lacking AHAA and ANK failed to activate these genes, suggesting that BmRelish becomes active by removal of the ANK and that the AHAA-rich region is a transactivation domain. BmRelish2 was shown to repress activation of <em>Cecropin B1</em> gene expression by BmRelish1-d2, suggesting that BmRelish2 plays a role as a dominant negative factor against the BmRelish1 active form. Necessity of κB sites of <em>Cecropin B1</em>, <em>Attacin</em> and <em>Lebocin 4</em> genes for the full activation of these genes by BmRelish1-d2 was confirmed. The requirement of the mandatory κB sites for <em>Lebocin 4</em> gene expression was different between BmRelish1 active form and BmRelA, suggesting differential roles for κB sites in antimicrobial peptide gene activation by different transcription factors. The binding of the RHD portion of BmRelish1 fusion protein to the κB sites of <em>Cecropin B1</em> and <em>Attacin</em> genes was also confirmed.</p></div>","PeriodicalId":100161,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression","volume":"1769 9","pages":"Pages 559-568"},"PeriodicalIF":0.0,"publicationDate":"2007-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bbaexp.2007.07.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26902431","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":"Transcriptional and epigenetic regulation of the integrin collagen receptor locus ITGA1-PELO-ITGA2","authors":"Yann Cheli ,&nbsp;Sachiko Kanaji ,&nbsp;Beatrice Jacquelin ,&nbsp;Mei Chang ,&nbsp;Diane J. Nugent ,&nbsp;Thomas J. Kunicki","doi":"10.1016/j.bbaexp.2007.06.004","DOIUrl":"10.1016/j.bbaexp.2007.06.004","url":null,"abstract":"<div><p>The integrin collagen receptor locus on human chromosome 5q11.2 includes the integrin genes <em>ITGA1</em> and <em>ITGA2,</em> and the cell cycle regulation gene <em>PELO,</em> embedded within <em>ITGA1</em> intron 1. <em>ITGA1</em> contains a CArG box that is bound by serum response factor (SRF), while <em>PELO</em> contains two Sp1 binding elements. A comparison of mRNA levels in megakaryocytic (MK) and non-megakaryocytic (non-MK) cell lines and an analysis of the transcriptional activity of promoter-LUC reporter gene constructs in transfected cells revealed that <em>ITGA1</em> is selectively suppressed in the MK lineage. Sodium bisulfite genomic sequencing established that a CpG-rich <em>ITGA1</em> promoter region (−<!--> <!-->209/+<!--> <!-->115) is fully methylated at 19 CpG sites in MK cells that do not express α1β1, but completely demethylated in expressing cells. <em>In vitro</em> methylation of <em>ITGA1</em> suppresses transcription, while treatment of megakaryocytic cells with 5-aza-2′-deoxycytidine, but not Trichostatin A, resulted in <em>de novo</em> expression of <em>ITGA1</em>. During thrombopoietin-induced <em>in vitro</em> differentiation of primary human cord blood mononuclear cells into megakaryocytes, we observed rapid, progressive CpG methylation of <em>ITGA1</em>, but not <em>PELO</em> or <em>ITGA2</em>. Thus, selective CpG methylation of the <em>ITGA1</em> promoter is a specific feature of α1β1 regulation that coincides with the initiation of megakaryocyte differentiation.</p></div>","PeriodicalId":100161,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression","volume":"1769 9","pages":"Pages 546-558"},"PeriodicalIF":0.0,"publicationDate":"2007-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bbaexp.2007.06.004","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26862908","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":"Flexible interaction of Drosophila Smad complexes with bipartite binding sites","authors":"Sheng Gao ,&nbsp;Allen Laughon","doi":"10.1016/j.bbaexp.2007.05.006","DOIUrl":"10.1016/j.bbaexp.2007.05.006","url":null,"abstract":"<div><p>A subset of BMP-responsive enhancer elements are characterized by pairing of a GC-rich Smad1 binding site and an SBE-type Smad4 binding site. Such paired, or bipartite, sites are in some cases just 5 bp apart and thus might be contacted by a single Smad1–Smad4 complex. Other potential pairings are separated as much as 60 bp but it is not known whether such longer distances can be spanned by a Smad1–Smad4 complex, indeed binding of native Smad1–Smad4 complexes to any of these bipartite elements has yet to be reported. Here we report that a complex of the homologous <em>Drosophila</em> Smad proteins, Mad and Medea, is capable of concerted binding to GC-rich and SBE sites separated by as much as 20 bp. The wider the separation, the more severely binding affinity was reduced by shortening of the linker region that tethers the DNA binding domain of Medea. In contrast, length of the Mad linker did not affect the allowed distance between paired sites, rather it contributes specifically to Mad contact with the GC-rich site. Finally, we show that Smad1 and Smad4 can participate in binding to bipartite sites.</p></div>","PeriodicalId":100161,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression","volume":"1769 7","pages":"Pages 484-496"},"PeriodicalIF":0.0,"publicationDate":"2007-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.bbaexp.2007.05.006","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26811798","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}