RNAPub Date : 2026-05-08DOI: 10.1261/rna.081079.126
Pavla Linhartova, Jaclyn Quin, Tomas Loja, Janka Melicherova, Qiupei Du, Anna Cherian, Dragana Vukic, David Modry, Marie Tomandlova, Barbora Cervena, Helena Stribrnah, Ann-Kristin Ostlund Farrants, Andrea Knight, Liam Peter Keegan, Mary A O'Connell
{"title":"Reconfigured immunity in Adar heterozygous and Adar Mavs Eif2ak2 (PKR) triple mutant mice.","authors":"Pavla Linhartova, Jaclyn Quin, Tomas Loja, Janka Melicherova, Qiupei Du, Anna Cherian, Dragana Vukic, David Modry, Marie Tomandlova, Barbora Cervena, Helena Stribrnah, Ann-Kristin Ostlund Farrants, Andrea Knight, Liam Peter Keegan, Mary A O'Connell","doi":"10.1261/rna.081079.126","DOIUrl":"https://doi.org/10.1261/rna.081079.126","url":null,"abstract":"<p><p>Adenosine deaminase acting on RNA 1 (ADAR1) deaminates adenosine to inosine in dsRNA. ADAR1 RNA editing marks cellular dsRNA as self, preventing aberrant activation of the antiviral dsRNA sensor MDA5. Adar Ifih1 (MDA5) or Adar Mavs double mutant pups escape Adar mutant aberrant interferon induction but die early. Here, we show that long-lived Adar Mavs Eif2ak2 (PKR) mice display a new residual defect: failure to maintain blood CD8+ T cells due to loss of an editing-independent function of ADAR1. Further dsRNA sensor-stripping in Adar Mavs Eif2ak2 Zbp1 mutants shows that loss of blood CD8+ T cells is not prevented. Challenging Adar+/- heterozygous or Adar Mavs Eif2ak2 mice with blood stage Plasmodium yoelii infection led to reduced parasitemia in Adar+/- mice by increased basal interferon. Unexpected reduced parasitemia in Adar Mavs Eif2ak2 mice is also likely due to interferon-related defects specific to hemopoietic cells, leading to altered populations of γδ T cells and other immune cells. The defects observed in this partially dsRNA sensor-stripped mouse suggest that different antiviral dsRNA sensors normally complement each other.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":5.0,"publicationDate":"2026-05-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147857086","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2026-05-05DOI: 10.1261/rna.080909.125
Nina M Krause, Julia Wirmer-Bartoschek, Christian Richter, Matthias S Leisegang, Ralf P Brandes, Harald Schwalbe
{"title":"RNA•DNA:DNA Triplex Formation Modulates Individual Base Pair Stabilities in the DNA Target Duplex.","authors":"Nina M Krause, Julia Wirmer-Bartoschek, Christian Richter, Matthias S Leisegang, Ralf P Brandes, Harald Schwalbe","doi":"10.1261/rna.080909.125","DOIUrl":"https://doi.org/10.1261/rna.080909.125","url":null,"abstract":"<p><p>Long non-coding RNAs (lncRNAs) play key roles in gene regulation. One potential regulation mechanism involves the formation of RNA•DNA:DNA triplexes. In these triplexes, the lncRNA binds in the major groove of a target DNA via Hoogsteen base pair formation. Here, we investigated the impact of the underlying RNA binding on the on the stability of the DNA duplex target to gain insights into the triplex stability at base pair resolution. Quantification of the temperature-dependent exchange of imino hydrogen atoms with solvent of the target DNA duplex allows determination of the changes of the stability of individual DNA duplex base pairs upon triplex formation. The data shown here investigates an antiparallel triplex, formed between the lncRNA hypoxia-inducible factor 1-alpha Antisense RNA 1 (HIF1α-AS1) and the DNA target Adrenomedullin (ADM), important in cardiovascular diseases. Triplex formation alters DNA structure and stability by affecting both hydrogen bonding strength and nucleobase-stacking interactions. These thermodynamic insights support bioinformatic methods to predict triplex stability and enhance our understanding of RNA•DNA:DNA triplex formation.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":5.0,"publicationDate":"2026-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147842257","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2026-04-28DOI: 10.1261/rna.081025.126
Natalie Bao Ying Lim, Maya Jeitany, Peter Droge, Kah Wai Lim, Anh Tuan Phan
{"title":"Differential human telomerase RNA knockdown by antisense oligonucleotides reveals the existence and potential function of a robust RNA domain.","authors":"Natalie Bao Ying Lim, Maya Jeitany, Peter Droge, Kah Wai Lim, Anh Tuan Phan","doi":"10.1261/rna.081025.126","DOIUrl":"https://doi.org/10.1261/rna.081025.126","url":null,"abstract":"<p><p>Telomere length governs replicative capacity and cellular fate. In most cancers, telomeres are maintained by telomerase, a holoenzyme comprising an RNA component (hTR), a protein component (hTERT), and associated accessory proteins. hTR contains two major domains: a 5' domain that associates with hTERT, and a 3' domain that binds core H/ACA proteins. Beyond telomere maintenance, hTR also exerts extra-telomeric roles. Here, we identified a potent antisense oligonucleotide (ASO) against hTR, which inhibited telomerase activity, leading to telomere shortening and cell growth impairment. Surprisingly, this ASO only mediated hTR degradation up to nucleotide 209, leaving the 3' domain intact. Profiling of hTR using ASO tiling also supported this observation: whereas 3'-targeting ASOs could deplete the whole molecule, 5'-targeting ASOs could selectively deplete only the 5' domain, leaving the 3' domain intact, or even increase in abundance. Furthermore, the 3' domain persisted at a steady state following prolonged treatment and was detected in untreated cells, suggesting its natural existence.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":5.0,"publicationDate":"2026-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147779716","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2026-04-28DOI: 10.1261/rna.080942.126
Yukitomo Arao, Jason G Williams, Wi S Lai
{"title":"CNOT10 is involved in TTP-mediated AU-rich element containing mRNA metabolism, independent of mRNA decay regulation.","authors":"Yukitomo Arao, Jason G Williams, Wi S Lai","doi":"10.1261/rna.080942.126","DOIUrl":"10.1261/rna.080942.126","url":null,"abstract":"<p><p>Tristetraprolin (TTP)/ ZFP36 is an RNA binding protein that is involved in the turnover regulation of target adenylate-uridylate-rich RNA element (ARE) containing mRNAs. AREs are present in the 3'-untranslated region of transcripts expressed from many immediate-early genes, including cytokines and chemokines. It has been demonstrated that TTP-mediated post-transcriptional mRNA decay regulation is crucial for modulating physiological control, particularly in response to inflammatory stimulation. TTP is associated with the CCR4-NOT deadenylation complex through the TTP C-terminus to promote mRNA decay. However, it is not fully understood whether there are additional sites within TTP that contribute to its function through interacting with other factors. We analyzed the functionality of the unique tryptophan residues located in the TTP N-terminus using a cell-based assay system that consists of a tetracycline-responsive CMV promoter-driven, intron-inserted luciferase (LUC). This system enabled us to analyze TTP activity during both the early phase and the steady-state phase of gene expression, as well as in the post-transcriptional mRNA decay following the treatment of tetracycline analogs. Meanwhile, we identified putative TTP associates using a proximity labeling method. We found that tryptophan residues in the TTP N-terminus together with CNOT10, a component of the CCR4-NOT complex, were involved specifically in the reduction of the ARE-containing LUC mRNA level during the early phase of gene expression. However, they were not involved in the decay of LUC mRNA in the steady-state phase. We propose a novel post-transcriptional TTP functionality in the reduction of ARE-containing mRNA level, which differs from the well-characterized mRNA decay activity.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":5.0,"publicationDate":"2026-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147779594","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2026-04-27DOI: 10.1261/rna.080657.125
Sierra S Schmidt, Alexandra R Farah, Aisling Macaraeg, Daniel Floyd, Hannah S Trautmann, Kathryn M Ramsey
{"title":"Regulation of multiple paralogs of a small subunit ribosomal protein in <i>Francisella tularensis</i>.","authors":"Sierra S Schmidt, Alexandra R Farah, Aisling Macaraeg, Daniel Floyd, Hannah S Trautmann, Kathryn M Ramsey","doi":"10.1261/rna.080657.125","DOIUrl":"10.1261/rna.080657.125","url":null,"abstract":"<p><p>Francisella tularensis is a highly infectious human pathogen that must replicate inside macrophage to cause disease. The ribosomes of F. tularensis can incorporate one of three different paralogs for the small ribosomal subunit protein bS21. One of these paralogs positively impacts translation of key virulence genes and promotes intramacrophage replication. Although ribosomal bS21 content influences F. tularensis virulence, the factors that control bS21 paralog production are not well understood. Here, we reveal that all three bS21 proteins influence the transcript abundance of the paralog important for virulence, bS21-2. In contrast, the other bS21 paralogs (bS21-1 and bS21-3) do not affect their own production. We further determined that the leader sequence of the bS21-2 mRNA is sufficient for bS21-mediated repression of mRNA abundance, suggesting that bS21-2 is autogenously regulated. Counterintuitively, we found that in cells lacking bS21-2, the increase in bS21-2-encoding mRNA does not lead to significant increases in protein production. This reduction in translation efficiency suggests that translation of the bS21-2 mRNA is controlled by other factors. Finally, we determined that bS21-2 exerts at least some of its effects on the bS21-2 transcript by decreasing its stability. Together, our findings suggest that F. tularensis may integrate multiple signals into a regulatory network to control the appropriate production of each bS21 paralog, and particularly the paralog important for virulence, bS21-2. This raises the possibility of a regulatory network that can both control ribosome composition in F. tularensis as well as virulence.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":5.0,"publicationDate":"2026-04-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147779732","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2026-04-23DOI: 10.1261/rna.080990.126
Mert Cihan, Piyush More, Maximilian Sprang, Federico Marini, Miguel A Andrade-Navarro
{"title":"Target-site Dynamics Explain a Large Share of Apparent MicroRNA Differential Expression.","authors":"Mert Cihan, Piyush More, Maximilian Sprang, Federico Marini, Miguel A Andrade-Navarro","doi":"10.1261/rna.080990.126","DOIUrl":"https://doi.org/10.1261/rna.080990.126","url":null,"abstract":"<p><p>MicroRNA (miRNA) abundance reflects a dynamic balance between biogenesis, target engagement, and decay, yet differential expression analyses typically ignore changes in target-site availability driven by alternative polyadenylation (APA). We introduce MIRNAPEX, an expression-stratification-based machine learning framework that quantifies miRNA regulatory effect sizes from RNA-seq data by integrating target-gene expression with 3'UTR isoform usage to infer effective binding-site dosage. Using pan-cancer training sets, we train models that learn relationships between transcriptomic features and miRNA log-fold changes, with APA patterns providing context-dependent complementary information alongside gene expression. When applied to knockdowns of core APA regulators, MIRNAPEX captured widespread 3'UTR shortening and predicted miRNA-specific shifts whose direction was consistent with changes in the APA-associated 3'UTR landscapes of target genes. Analysis of target-directed miRNA degradation interactions further showed that loss of distal decay-trigger sites coincides with increased miRNA abundance, consistent with reduced TDMD-mediated decay. Together, these findings suggest that apparent miRNA differential expression can be associated with dynamic target-site landscapes in addition to altered miRNA transcription, and that neglecting this dimension can lead to misestimation of regulatory effect sizes.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":5.0,"publicationDate":"2026-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147779691","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2026-04-22DOI: 10.1261/rna.080781.125
Emma C Goguen, Kylie A Zawisza, David A Brow
{"title":"Direct RNA-seq provides evidence for an antiterminator function of the yeast Hrp1 protein on RNA polymerase II transcripts.","authors":"Emma C Goguen, Kylie A Zawisza, David A Brow","doi":"10.1261/rna.080781.125","DOIUrl":"10.1261/rna.080781.125","url":null,"abstract":"<p><p>Hrp1/Nab4 is an essential nuclear RNA-binding protein that was first identified in the yeast Saccharomyces cerevisiae as a cleavage and polyadenylation factor for mRNAs, CF1B, but was later shown to promote termination of some short, noncoding transcripts via the \"NNS\" termination pathway. Hrp1 binds (UA)n repeats found in both mRNA 3'-UTRs and short noncoding RNA terminators, but its function in 3'-end formation is not fully understood. Our past microarray transcriptome analysis of the heat-sensitive hrp1-7 allele suggested Hrp1 functions in antitermination of RNA polymerase II (RNAP II) on protein-coding genes. The hrp1-7 allele has four substitutions and one, M191T, was shown to be primarily responsible for NNS terminator readthrough. Here we show that Hrp1-7 protein has a three-fold and Hrp1-M191T a 1.5-fold decreased affinity for (UA)4 in vitro. We used nanopore direct RNA sequencing to assess the transcriptome-wide effects of hrp1-7 and hrp1-M191T, which identified new examples of Hrp1-dependent small nucleolar RNA terminators and mRNA attenuators (regulatory terminators in the 5'-UTR and ORF). For some genes, including HRP1, attenuated transcript reads outnumber the corresponding mRNA reads in exponentially growing wildtype cells. We also observed widespread changes in mRNA polyA site selection. In the hrp1-M191T strain the polyA site shifts are mostly downstream, while in the hrp1-7 strain upstream and downstream shifts are more similar in frequency. Our results are consistent with a model in which one or more of the four substitutions in hrp1-7 weaken the affinity of Hrp1 for the RNAP II elongation complex, promoting premature termination, while others interfere with its recognition of terminator sequences, promoting terminator readthrough.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":5.0,"publicationDate":"2026-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147779713","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2026-04-22DOI: 10.1261/rna.080915.125
Annika Ladwig, Melina Klostermann, Kathi Zarnack
{"title":"The impact of read depth and read length on RNA-seq splicing analysis.","authors":"Annika Ladwig, Melina Klostermann, Kathi Zarnack","doi":"10.1261/rna.080915.125","DOIUrl":"https://doi.org/10.1261/rna.080915.125","url":null,"abstract":"<p><p>Alternative splicing (AS) is a key layer of regulation in eukaryotic gene expression that is investigated in all areas of life sciences. Differences in AS between conditions can be quantified from transcriptome-wide short-read RNA sequencing (RNA-seq) data with designated computational tools. However, not all short-read RNA-seq data are equally suited for AS analysis. Here, we perform an exemplary AS analysis to showcase the impact of the RNA-seq library characteristics on the obtained results. Using two standard ENCODE data sets with widespread AS changes, we modulate read length and read depth and compare their influence on the detection, quantification and classification of AS events with the state-of-the-art AS algorithm MAJIQ. We find that both longer reads and higher read depth are effective measures to improve the sensitivity and precision of the AS analysis. Our results provide valuable insights to help researchers make informed decisions when choosing the short-read RNA-seq library specifications for AS analysis.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":5.0,"publicationDate":"2026-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147779655","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2026-04-21DOI: 10.1261/rna.080776.125
Ali Salman, Mikhail Loev, Tatiana Egorova, Alexey V Shuvalov, Anastasia Zharikova, Sergey Dmitriev, Ekaterina Shuvalova, Nikita Biziaev, Elena Alkalaeva
{"title":"Dual Role of 3' UTR Length in Modulating Translation Termination Efficiency.","authors":"Ali Salman, Mikhail Loev, Tatiana Egorova, Alexey V Shuvalov, Anastasia Zharikova, Sergey Dmitriev, Ekaterina Shuvalova, Nikita Biziaev, Elena Alkalaeva","doi":"10.1261/rna.080776.125","DOIUrl":"https://doi.org/10.1261/rna.080776.125","url":null,"abstract":"<p><p>The 3' untranslated region of mRNAs are involved in post-transcriptional control, influencing mRNA stability, localization, and translation efficiency through its interaction with various proteins and RNAs. While eukaryotic 3' UTRs are typically several hundred nucleotides long, certain protozoan species possess remarkably short 3' UTRs and have evolved alternative genetic codes where canonical stop codons are reassigned to sense codons. This suggests a potential link between 3' UTR architecture and the efficiency of translation termination. In this study, we investigate how the length and secondary structure of the 3' UTR modulate translation termination efficiency across different species. We demonstrate that shortening of structured 3' UTRs confer a translational advantage for mRNAs bearing UAA stop codons. Using purified pre-termination complexes, we show that 3' UTR secondary structures enhance the termination rate by facilitating the spatial proximity of PABP (bound to the poly(A) tail) to eRF3a on the ribosome. Furthermore, we found that the termination rate at UGA stop codons is highly sensitive to 3' UTR length when assayed with both human and ciliate release factors. Our investigation of stop codon reassignment underscores the primary role of release factor recognition efficiency in this process. Collectively, our findings reveal a dual regulatory mechanism: while long, structured 3' UTRs can sterically hinder stop codon recognition, they simultaneously promote eRF3a-PABP interactions that facilitate the recruitment of release factors to the ribosome. This work establishes 3' UTR length as a key cis-regulatory factor fine-tuning the fundamental process of translation termination.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":5.0,"publicationDate":"2026-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147779722","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2026-04-17DOI: 10.1261/rna.080976.126
Sivakumar Vadivel Gnanasundram, Lixiao Wang, Sa Chen, Ondrej Bonczek, Borivoj Vojtesek, Robin Fahraeus
{"title":"Cancer-associated synonymous mutations reveal stress signal-dependent mRNA folding that selectively modulates protein function.","authors":"Sivakumar Vadivel Gnanasundram, Lixiao Wang, Sa Chen, Ondrej Bonczek, Borivoj Vojtesek, Robin Fahraeus","doi":"10.1261/rna.080976.126","DOIUrl":"https://doi.org/10.1261/rna.080976.126","url":null,"abstract":"<p><p>Recent technical advances have facilitated studies on changes in mRNA structures in response to signaling pathways. However, if mRNA structures can affect the function of the encoded protein remains poorly understood. In-cell RNA structural probing (SHAPE-MaP) demonstrates how two cancer-associated synonymous mutations (CASMs) at proline codon 34 (c.102 C>A and c.102 C>G) prevent DNA damage-induced TP53 mRNA folding, whereas the non-cancer-associated c.102 C>U mutation does not. Transcript and chromatin immunoprecipitation (ChIP) analysis reveal that p53 expressed from CASM34 has reduced promoter binding and reduced induction of p53 downstream target genes PUMA and 14-3-3-σ, but not p21CDKN1A. Transcriptome analysis reveals a CASM34-mediated global attenuation of DNA damageresponsive gene expression. Together, the results demonstrate that CASM34 interferes with signal-induced p53 mRNA folding during DNA damage, leading to selective modulation of p53 protein activity. More broadly, our findings highlight a general concept by which cancer-associated synonymous mutations target signal-induced mRNA structures that influence the encoded protein.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":5.0,"publicationDate":"2026-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147717897","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}