Mutation Research/DNA Repair最新文献

{"title":"Increased DNA double strand breakage is responsible for sensitivity of the pso3-1 mutant of Saccharomyces cerevisiae to hydrogen peroxide","authors":"Jela Brozmanová ,&nbsp;Viera Vlčková ,&nbsp;Eva Farkašová ,&nbsp;Andrej Dudáš ,&nbsp;Danuša Vlasáková ,&nbsp;Miroslav Chovanec ,&nbsp;Žaneta Mikulovská ,&nbsp;Ivana Fridrichová ,&nbsp;Jenifer Saffi ,&nbsp;Joao A.P Henriques","doi":"10.1016/S0921-8777(01)00070-2","DOIUrl":"10.1016/S0921-8777(01)00070-2","url":null,"abstract":"<div><p><em>Escherichia coli</em><span> endonuclease III (endo III) is the key repair enzyme essential for removal of oxidized pyrimidines and abasic sites. Although two homologues of endo III, Ntg1 and Ntg2, were found in </span><span><em>Saccharomyces cerevisiae</em></span>, they do not significantly contribute to repair of oxidative DNA damage in vivo. This suggests that an additional activity(ies) or a regulatory pathway(s) involved in cellular response to oxidative DNA damage may exist in yeast. The <em>pso3-1</em> mutant of <em>S. cerevisiae</em> was previously shown to be specifically sensitive to toxic effects of hydrogen peroxide (H₂O₂<span>) and paraquat. Here, we show that increased DNA double strand breakage is very likely the basis of sensitivity of the </span><em>pso3-1</em><span> mutant cells to H</span>₂O₂<span>. Our results, thus, indicate an involvement of the Pso3 protein in protection of yeast cells from oxidative stress presumably through its ability to prevent DNA double strand breakage. Furthermore, complementation of the repair defects of the </span><em>pso3-1</em> mutant cells by <em>E. coli</em> endo III has been examined. It has been found that expression of the <em>nth</em> gene in the <em>pso3-1</em> mutant cells recovers survival, decreases mutability and protects yeast genomic DNA from breakage following H₂O₂ treatment. This might suggest some degree of functional similarity between Pso3 and Nth.</p></div>","PeriodicalId":100935,"journal":{"name":"Mutation Research/DNA Repair","volume":"485 4","pages":"Pages 345-355"},"PeriodicalIF":0.0,"publicationDate":"2001-05-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0921-8777(01)00070-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56179799","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":"Disparate effects of similar phenolic phytochemicals as inhibitors of oxidative damage to cellular DNA","authors":"Melissa R Kelly,&nbsp;Jing Xu,&nbsp;Karen E Alexander,&nbsp;George Loo","doi":"10.1016/S0921-8777(01)00066-0","DOIUrl":"10.1016/S0921-8777(01)00066-0","url":null,"abstract":"<div><p><span><span>Phenolic phytochemicals are natural plant substances whose cellular effects have not been completely determined. Nordihydroguaiaretic acid (NDGA) and curcumin are two phenolic phytochemicals with similar molecular structures, suggesting that they possess comparable chemical properties particularly in terms of </span>antioxidant activity. To examine this possibility in a cellular system, this study evaluated the capacities of NDGA and curcumin to function as antioxidants in inhibiting oxidative damage to DNA. Jurkat T-lymphocytes were pre-incubated for 30</span> <!-->min with 0–25<!--> <!-->μM of either NDGA or curcumin to allow for uptake. The phenolic phytochemical-treated cells were then oxidatively challenged with 25<!--> <!-->μM hydrogen peroxide (H₂O₂<span>). Afterwards, cells were subjected to alkaline micro-gel electrophoresis (i.e. comet assay) to assess the extent of single-strand breaks in DNA. In a concentration-dependent manner, NDGA inhibited H</span>₂O₂<span>-induced DNA damage, whereas curcumin did not. In fact, incubating Jurkat T-lymphocytes with curcumin alone actually induced DNA damage. This effect of curcumin on DNA did not appear to reflect the DNA fragmentation<span> associated with apoptosis because there was no proteolytic cleavage of poly-(ADP-ribose)-polymerase, which is considered an early marker of apoptosis. Curcumin-induced damage to DNA was prevented by pre-treatment of the cells with the lipophilic antioxidant, α-tocopherol, suggesting that curcumin damaged DNA through oxygen radicals. Therefore, it is concluded that NDGA has antioxidant activity but curcumin has prooxidant activity in cultured cells based on their opposite effects on DNA.</span></span></p></div>","PeriodicalId":100935,"journal":{"name":"Mutation Research/DNA Repair","volume":"485 4","pages":"Pages 309-318"},"PeriodicalIF":0.0,"publicationDate":"2001-05-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0921-8777(01)00066-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56179760","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 major human abasic endonuclease: formation, consequences and repair of abasic lesions in DNA","authors":"David M Wilson III,&nbsp;Daniel Barsky","doi":"10.1016/S0921-8777(01)00063-5","DOIUrl":"10.1016/S0921-8777(01)00063-5","url":null,"abstract":"<div><p>DNA continuously suffers the loss of its constituent bases, and thereby, a loss of potentially vital genetic information. Sites of missing bases — termed abasic or apurinic/apyrimidinic (AP) sites — form spontaneously, through damage-induced hydrolytic base release, or by enzyme-catalyzed removal of modified or mismatched bases during base excision repair (BER). In this review, we discuss the structural and biological consequences of abasic lesions in DNA, as well as the multiple repair pathways for such damage, while emphasizing the mechanistic operation of the multi-functional human abasic endonuclease APE1 (or REF-1) and its potential relationship to disease.</p></div>","PeriodicalId":100935,"journal":{"name":"Mutation Research/DNA Repair","volume":"485 4","pages":"Pages 283-307"},"PeriodicalIF":0.0,"publicationDate":"2001-05-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0921-8777(01)00063-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56179731","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":"Characterization of functional interactions among the Escherichia coli mismatch repair proteins using a bacterial two-hybrid assay","authors":"Catherine A Mansour,&nbsp;Kathy M.J Doiron,&nbsp;Claire G Cupples","doi":"10.1016/S0921-8777(01)00071-4","DOIUrl":"10.1016/S0921-8777(01)00071-4","url":null,"abstract":"<div><p>Vsr mediates very short patch repair in <em>Escherichia coli</em><span>, correcting T/G mismatches caused by deamination<span> of 5-methylcytosine to thymine<span>. MutS and MutL, part of the post-replication mismatch repair<span> system, stimulate VSP repair. In this study, we use a bacterial two-hybrid assay to show that MutL interacts with Vsr. We also show that interaction between Vsr and MutL inhibits the ability of MutL to dimerize, to interact with MutS and MutH and to mediate a previously unknown interaction between MutS and MutH. This inhibition may explain why high levels of Vsr are mutagenic in vivo. In addition, we show that the Mut fusion proteins are repair proficient in the bacterial two-hybrid assay, making it possible to study their interactions in various genetic backgrounds, or in the presence of DNA damaging agents.</span></span></span></span></p></div>","PeriodicalId":100935,"journal":{"name":"Mutation Research/DNA Repair","volume":"485 4","pages":"Pages 331-338"},"PeriodicalIF":0.0,"publicationDate":"2001-05-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0921-8777(01)00071-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56179809","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":"Diversity of the damage recognition step in the global genomic nucleotide excision repair in vitro","authors":"Rika Kusumoto ,&nbsp;Chikahide Masutani ,&nbsp;Kaoru Sugasawa ,&nbsp;Shigenori Iwai ,&nbsp;Marito Araki ,&nbsp;Akio Uchida ,&nbsp;Toshimi Mizukoshi ,&nbsp;Fumio Hanaoka","doi":"10.1016/S0921-8777(00)00082-3","DOIUrl":"10.1016/S0921-8777(00)00082-3","url":null,"abstract":"<div><p><span><span><span>The XPC–HR23B complex, a mammalian factor specifically involved in global genomic nucleotide excision repair (NER) has been shown to bind various forms of damaged DNA and initiate DNA repair in cell-free reactions. To characterize the binding specificity of this factor in more detail, a method based on </span>immunoprecipitation was developed to assess the relative affinity of XPC–HR23B for defined lesions on DNA. Here we show that XPC–HR23B preferentially binds to UV-induced (6-4) photoproducts (6-4PPs) as well as to cholesterol, but not to the </span>cyclobutane pyrimidine dimer (CPD), 8-oxoguanine (8-oxo-G), </span><em>O</em>⁶-methylguanine (<em>O</em>⁶-Me-G), or a single mismatch. Human whole cell extracts could efficiently excise 6-4PPs and cholesterol in an XPC–HR23B-dependent manner, but not 8-oxo-G, <em>O</em>⁶<span>-Me-G or mismatches. Thus, there was good correlation between the binding specificity of XPC–HR23B for certain types of lesion and the ability of human cell extracts to excise these lesions, supporting the model that XPC–HR23B initiates global genomic NER. Although, XPC–HR23B does not preferentially bind to CPDs, the excision of CPDs in human whole cell extracts was found to be absolutely dependent on XPC–HR23B, in agreement with the in vivo observation that CPDs are not removed from the global genome in XP-C mutant cells. These results suggest that, in addition to the excision repair pathway initiated by XPC–HR23B, there exists another sub-pathway for the global genomic NER that still requires XPC–HR23B but is not initiated by XPC–HR23B. Possible mechanisms will be discussed.</span></p></div>","PeriodicalId":100935,"journal":{"name":"Mutation Research/DNA Repair","volume":"485 3","pages":"Pages 219-227"},"PeriodicalIF":0.0,"publicationDate":"2001-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0921-8777(00)00082-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56179690","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":"Complementation of chromosomal aberrations in AT/NBS hybrids: inadequacy of RDS as an endpoint in complementation studies with immortal NBS cells","authors":"Maria Kraakman-van der Zwet ,&nbsp;Wilhelmina J.I. Overkamp ,&nbsp;Nicolaas G.J. Jaspers ,&nbsp;Adayapalam T. Natarajan ,&nbsp;Paul H.M. Lohman ,&nbsp;Małgorzata Z. Zdzienicka","doi":"10.1016/S0921-8777(00)00078-1","DOIUrl":"10.1016/S0921-8777(00)00078-1","url":null,"abstract":"<div><p><span><span><span>Nijmegen breakage syndrome<span> (NBS) and ataxia telangiectasia (AT) are rare autosomal recessive hereditary disorders characterized by </span></span>radiosensitivity<span><span>, chromosomal instability, immunodeficiency and proneness to cancer. Although the clinical features of both syndromes are quite distinct, the cellular characteristics are very similar. Cells from both NBS and AT patients are hypersensitive to ionizing radiation (IR), show elevated levels of </span>chromosomal aberrations<span> and display radioresistant DNA synthesis (RDS). The proteins defective in NBS and AT, NBS1 and ATM, respectively, are involved in the same pathway, but their exact relationship is not yet fully understood. Stumm et al. (Am. J. Hum. Genet. 60 (1997) 1246) have reported that hybrids of AT and NBS </span></span></span>lymphoblasts<span> were not complemented for chromosomal aberrations. In contrast, we found that X-ray-induced cell killing as well as chromosomal aberrations were complemented in proliferating NBS-1LBI/AT5BIVA hybrids, comparable to that in NBS-1LBI cells after transfer of a single human chromosome 8 providing the </span></span><em>NBS1</em> gene. RDS observed in AT5BIVA cells was reduced in these hybrids to the level of that seen in immortal NBS-1LBI cells. However, the level of DNA synthesis, following ionizing radiation, in SV40 transformed wild-type cell lines was the same as in NBS-1LBI cells. Only primary wild-type cells showed stronger inhibition of DNA synthesis. In summary, these results clearly indicate that RDS cannot be used as an endpoint in functional complementation studies with immortal NBS-1LBI cells, whereas the cytogenetic assay is suitable for complementation studies with immortal AT and NBS cells.</p></div>","PeriodicalId":100935,"journal":{"name":"Mutation Research/DNA Repair","volume":"485 3","pages":"Pages 177-185"},"PeriodicalIF":0.0,"publicationDate":"2001-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0921-8777(00)00078-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56179639","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":"RAD9, RAD24, RAD16 and RAD26 are required for the inducible nucleotide excision repair of UV-induced cyclobutane pyrimidine dimers from the transcribed and non-transcribed regions of the Saccharomyces cerevisiae MFA2 gene","authors":"Shirong Yu ,&nbsp;Yumin Teng ,&nbsp;Noel F. Lowndes ,&nbsp;Raymond Waters","doi":"10.1016/S0921-8777(01)00061-1","DOIUrl":"10.1016/S0921-8777(01)00061-1","url":null,"abstract":"<div><p><span>In this study, the effect of a prior UV irradiation on the removal of cyclobutane pyrimidine dimers (CPDs) from the transcribed strand (TS) and non-transcribed strand (NTS) of the </span><em>MFA</em>2 gene in haploid <span><em>Saccharomyces</em><em> cerevisiae</em></span> (<em>S. cerevisiae</em>) cells was investigated. In NER competent cells, the pre-irradiation with a dose of 20<!--> <!-->J/m² enhances the removal of CPDs induced by a second UV dose of 100<!--> <!-->J/m² in the TS and the NTS of <em>MFA</em>2 gene except for the CPDs in the region +258 to +298 in the NTS, where the enhanced repair was absent. No inducible repair was observed in <em>rad9</em>, <em>rad24</em>, <em>rad16</em> and <em>rad26</em> cells, indicating two checkpoint genes <em>RAD</em>9 and <em>RAD</em>24, the global repair gene <em>RAD</em>16 and the transcription coupled repair gene <em>RAD</em>26 are essential for inducible NER.</p></div>","PeriodicalId":100935,"journal":{"name":"Mutation Research/DNA Repair","volume":"485 3","pages":"Pages 229-236"},"PeriodicalIF":0.0,"publicationDate":"2001-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0921-8777(01)00061-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56179712","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 relative contribution of adduct blockage and DNA repair on template utilization during replication of 1,N2-propanodeoxyguanosine and pyrimido[1,2-α]purin-10(3H)-one-adducted M13MB102 genomes","authors":"Stephen P. Fink ,&nbsp;Lawrence J. Marnett","doi":"10.1016/S0921-8777(01)00064-7","DOIUrl":"https://doi.org/10.1016/S0921-8777(01)00064-7","url":null,"abstract":"<div><p><span>The role of replication blockage by the exocyclic DNA adducts propanodeoxyguanosine (PdG) and pyrimido[1,2-α]purin-10(3</span><em>H</em>)-one (M₁G) was determined through the use of site-specifically adducted M13MB102 genomes containing a C:C-mismatch ∼3000 base-pairs from the site of adduct incorporation. Genomes containing either dG, PdG, or M₁G positioned at site 6256 of the (−)-strand were transformed into repair-proficient and repair-deficient <em>Escherichia coli</em> strains and the percent template utilization was determined by hybridization analysis. Unmodified genomes containing a C:C-mismatch resulted in a percent template utilization of approximately 60 and 40% for the (−)- and (+)-strands, respectively. Transformation of PdG- or M₁G-adducted genomes resulted in approximately a 60–40% and 50–50% (−)-strand to (+)-strand ratio, respectively, indicating that PdG and M₁G are negligible blocks to replication in repair-proficient <em>E. coli</em>. This is in contrast to previous studies using (PdG:T)- and (M₁<span>G:T)-mismatched M13MB102 genomes, which resulted in a majority of the replication events using the unadducted (+)-strand and suggested that both adducts were significant blocks to replication [J. Biol. Chem. 272 (1997) 11434; Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 8652]. The C:C-mismatch results, though, indicate that the large strand bias detected in the earlier studies is due to repair of the adducts and resynthesis of the (−)-strand using the (+)-strand as a template for repair synthesis. Transformation of adducted C:C-mismatched genomes into </span><em>E. coli</em> strains deficient in nucleotide excision repair did result in an increased strand bias with only approximately 20 and 34% of the replication events using the (−)-strand for PdG- and M₁G-adducted genomes, respectively. The increased strand bias indicates the importance of nucleotide excision repair in the removal of PdG and M₁G.</p></div>","PeriodicalId":100935,"journal":{"name":"Mutation Research/DNA Repair","volume":"485 3","pages":"Pages 209-218"},"PeriodicalIF":0.0,"publicationDate":"2001-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0921-8777(01)00064-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72081761","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":"Isolation and genetic characterisation of the Drosophila homologue of (SCE)REV3, encoding the catalytic subunit of DNA polymerase ζ","authors":"J.C.J. Eeken ,&nbsp;R.J. Romeijn ,&nbsp;A.W.M. de Jong ,&nbsp;A. Pastink ,&nbsp;P.H.M. Lohman","doi":"10.1016/S0921-8777(01)00062-3","DOIUrl":"https://doi.org/10.1016/S0921-8777(01)00062-3","url":null,"abstract":"<div><p>In <em>Drosophila</em><span><span><span>, about 30 mutants are known that show hypersensitivity to the methylating agent methyl methane </span>sulfonate (MMS). Addition of this agent to the medium results in an increased larval mortality of the mutants. Using a P-insertion </span>mutagenesis screen, three MMS-sensitive mutants on chromosome II were isolated. One of these is allelic to the known EMS-induced </span><em>mus205</em><span> (mutagen sensitive) mutant. In the newly isolated mutant, a P-element is detected in region 43E by in situ hybridisation. The localisation of </span><em>mus205</em><span> to this region was confirmed by deficiency mapping. The gene was cloned and shows strong homology to the </span><span><em>Saccharomyces</em><em> cerevisiae REV3</em></span> gene. The <em>REV3</em><span> gene encodes the catalytic subunit of DNA polymerase </span><em>ζ</em>, involved in translesion synthesis. The P-element is inserted in the first exon of the <em>mus205</em> gene resulting in an aberrant mRNA, encoding a putative truncated protein containing only the first 13 of the 2130 aa native <em>Drosophila</em> protein. The <em>mus205</em><span> mutant is hypersensitive to alkylating agents and UV, but not to ionising radiation. In contrast to reported data, in germ cells, the mutant has no effect on mutability by X-rays, NQO and alkylating agents. In somatic cells, the mutant shows no effect on MMS-induced mutations and recombinations. This phenotype of the </span><em>Drosophila mus205</em> mutant is strikingly different from the phenotype of the yeast <em>rev3</em> mutant, which is hypomutable after UV, X-rays, NQO and alkylating agents.</p></div>","PeriodicalId":100935,"journal":{"name":"Mutation Research/DNA Repair","volume":"485 3","pages":"Pages 237-253"},"PeriodicalIF":0.0,"publicationDate":"2001-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0921-8777(01)00062-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72033947","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":"Erratum to ‘Three-dimensional structural views of damaged-DNA recognition: T4 endonuclease V, E. coli Vsr protein, and human nucleotide excision repair factor XPA’ ☆: [Mutation Res. 460 (2000) 257–275]","authors":"K. Morikawa, M. Shirakawa","doi":"10.1016/S0921-8777(01)00075-1","DOIUrl":"https://doi.org/10.1016/S0921-8777(01)00075-1","url":null,"abstract":"","PeriodicalId":100935,"journal":{"name":"Mutation Research/DNA Repair","volume":"7 1","pages":"267-268"},"PeriodicalIF":0.0,"publicationDate":"2001-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78998759","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}