Pub Date : 2024-10-03DOI: 10.1016/j.molcel.2024.09.013
Prakash Kharel, Pavel Ivanov
In this issue of Molecular Cell, Anastasakis et al. describe a novel function of the metabolic enzyme PKM2 as an RNA G-quadruplex binding protein, which could contribute to cancer biology.
{"title":"PKM2-G-quadruplex interactions conspire to regulate the cancer transcriptome","authors":"Prakash Kharel, Pavel Ivanov","doi":"10.1016/j.molcel.2024.09.013","DOIUrl":"https://doi.org/10.1016/j.molcel.2024.09.013","url":null,"abstract":"In this issue of <em>Molecular Cell</em>, Anastasakis et al. describe a novel function of the metabolic enzyme PKM2 as an RNA G-quadruplex binding protein, which could contribute to cancer biology.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"67 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142369136","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-03DOI: 10.1016/j.molcel.2024.09.014
Kfir B. Steinbuch, Yitzhak Tor
In a recent publication in Cell, Xie et al.1 report a sensitive and scalable method for the detection and characterization of native glycoRNAs and identify acp3U, an abundant modified nucleoside discovered 50 years ago in tRNAPhe, as one of the primary attachment sites for N-glycans.
{"title":"50 years in the making: acp3U, an amino-acid-containing nucleoside, links N-glycans and RNA in glycoRNA","authors":"Kfir B. Steinbuch, Yitzhak Tor","doi":"10.1016/j.molcel.2024.09.014","DOIUrl":"https://doi.org/10.1016/j.molcel.2024.09.014","url":null,"abstract":"In a recent publication in <em>Cell</em>, Xie et al.<span><span><sup>1</sup></span></span> report a sensitive and scalable method for the detection and characterization of native glycoRNAs and identify acp<sup>3</sup>U, an abundant modified nucleoside discovered 50 years ago in tRNA<sup>Phe</sup>, as one of the primary attachment sites for N-glycans.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"112 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142369137","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-03DOI: 10.1016/j.molcel.2024.09.009
Adelina Ivanova, Peace Atakpa-Adaji, Shanlin Rao, Maria Marti-Solano, Colin W. Taylor
The spatial organization of inositol 1,4,5-trisphosphate (IP3)-evoked Ca2+ signals underlies their versatility. Low stimulus intensities evoke Ca2+ puffs, localized Ca2+ signals arising from a few IP3 receptors (IP3Rs) within a cluster tethered beneath the plasma membrane. More intense stimulation evokes global Ca2+ signals. Ca2+ signals propagate regeneratively as the Ca2+ released stimulates more IP3Rs. How is this potentially explosive mechanism constrained to allow local Ca2+ signaling? We developed methods that allow IP3 produced after G-protein coupled receptor (GPCR) activation to be intercepted and replaced by flash photolysis of a caged analog of IP3. We find that phosphatidylinositol 4,5-bisphosphate (PIP2) primes IP3Rs to respond by partially occupying their IP3-binding sites. As GPCRs stimulate IP3 formation, they also deplete PIP2, relieving the priming stimulus. Loss of PIP2 resets IP3R sensitivity and delays the transition from local to global Ca2+ signals. Dual regulation of IP3Rs by PIP2 and IP3 through GPCRs controls the transition from local to global Ca2+ signals.
{"title":"Dual regulation of IP3 receptors by IP3 and PIP2 controls the transition from local to global Ca2+ signals","authors":"Adelina Ivanova, Peace Atakpa-Adaji, Shanlin Rao, Maria Marti-Solano, Colin W. Taylor","doi":"10.1016/j.molcel.2024.09.009","DOIUrl":"https://doi.org/10.1016/j.molcel.2024.09.009","url":null,"abstract":"The spatial organization of inositol 1,4,5-trisphosphate (IP<sub>3</sub>)-evoked Ca<sup>2+</sup> signals underlies their versatility. Low stimulus intensities evoke Ca<sup>2+</sup> puffs, localized Ca<sup>2+</sup> signals arising from a few IP<sub>3</sub> receptors (IP<sub>3</sub>Rs) within a cluster tethered beneath the plasma membrane. More intense stimulation evokes global Ca<sup>2+</sup> signals. Ca<sup>2+</sup> signals propagate regeneratively as the Ca<sup>2+</sup> released stimulates more IP<sub>3</sub>Rs. How is this potentially explosive mechanism constrained to allow local Ca<sup>2+</sup> signaling? We developed methods that allow IP<sub>3</sub> produced after G-protein coupled receptor (GPCR) activation to be intercepted and replaced by flash photolysis of a caged analog of IP<sub>3</sub>. We find that phosphatidylinositol 4,5-bisphosphate (PIP<sub>2</sub>) primes IP<sub>3</sub>Rs to respond by partially occupying their IP<sub>3</sub>-binding sites. As GPCRs stimulate IP<sub>3</sub> formation, they also deplete PIP<sub>2</sub>, relieving the priming stimulus. Loss of PIP<sub>2</sub> resets IP<sub>3</sub>R sensitivity and delays the transition from local to global Ca<sup>2+</sup> signals. Dual regulation of IP<sub>3</sub>Rs by PIP<sub>2</sub> and IP<sub>3</sub> through GPCRs controls the transition from local to global Ca<sup>2+</sup> signals.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"145 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142369132","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-03DOI: 10.1016/j.molcel.2024.09.006
YongWoo Lee, Jeannie T. Lee
Here, we expound on the view that Xist RNA directly controls Polycomb repressive complex 2 (PRC2) recruitment, off-loading to chromatin, catalytic activity, and eviction from chromatin. RNA-PRC2 interactions also control RNA polymerase II transcription pausing. Dynamic RNA folding determines PRC2 activity. Disparate studies and interpretations abound but can be reconciled.
{"title":"PRC2-RNA interactions: Viewpoint from YongWoo Lee and Jeannie T. Lee","authors":"YongWoo Lee, Jeannie T. Lee","doi":"10.1016/j.molcel.2024.09.006","DOIUrl":"https://doi.org/10.1016/j.molcel.2024.09.006","url":null,"abstract":"Here, we expound on the view that Xist RNA directly controls Polycomb repressive complex 2 (PRC2) recruitment, off-loading to chromatin, catalytic activity, and eviction from chromatin. RNA-PRC2 interactions also control RNA polymerase II transcription pausing. Dynamic RNA folding determines PRC2 activity. Disparate studies and interpretations abound but can be reconciled.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"33 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142369139","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-03DOI: 10.1016/j.molcel.2024.08.024
William Garland, Torben Heick Jensen
Mammalian genomes produce an abundance of short RNA. This is, to a large extent, due to the genome-wide and spurious activity of RNA polymerase II (RNAPII). However, it is also because the vast majority of initiating RNAPII, regardless of the transcribed DNA unit, terminates within a ∼3-kb early “pausing zone.” Given that the resultant RNAs constitute both functional and non-functional species, their proper sorting is critical. One way to think about such quality control (QC) is that transcripts, from their first emergence, are relentlessly targeted by decay factors, which may only be avoided by engaging protective processing pathways. In a molecular materialization of this concept, recent progress has found that both “destructive” and “productive” RNA effectors assemble at the 5′ end of capped RNA, orchestrated by the essential arsenite resistance protein 2 (ARS2) protein. Based on this principle, we here discuss early QC mechanisms and how these might sort short RNAs to their final fates.
{"title":"Nuclear sorting of short RNA polymerase II transcripts","authors":"William Garland, Torben Heick Jensen","doi":"10.1016/j.molcel.2024.08.024","DOIUrl":"https://doi.org/10.1016/j.molcel.2024.08.024","url":null,"abstract":"Mammalian genomes produce an abundance of short RNA. This is, to a large extent, due to the genome-wide and spurious activity of RNA polymerase II (RNAPII). However, it is also because the vast majority of initiating RNAPII, regardless of the transcribed DNA unit, terminates within a ∼3-kb early “pausing zone.” Given that the resultant RNAs constitute both functional and non-functional species, their proper sorting is critical. One way to think about such quality control (QC) is that transcripts, from their first emergence, are relentlessly targeted by decay factors, which may only be avoided by engaging protective processing pathways. In a molecular materialization of this concept, recent progress has found that both “destructive” and “productive” RNA effectors assemble at the 5′ end of capped RNA, orchestrated by the essential arsenite resistance protein 2 (ARS2) protein. Based on this principle, we here discuss early QC mechanisms and how these might sort short RNAs to their final fates.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"222 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142369144","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNA is a central molecule in RNA virus biology; however, the interactions that it establishes with the host cell are only starting to be elucidated. In recent years, a methodology revolution has dramatically expanded the scope of host-virus interactions involving the viral RNA (vRNA). A second wave of method development has enabled the precise study of these protein-vRNA interactions in a life cycle stage-dependent manner, as well as providing insights into the interactome of specific vRNA species. This review discusses these technical advances and describes the new regulatory mechanisms that have been identified through their use. Among these, we discuss the importance of vRNA in regulating protein function through a process known as riboregulation. We envision that the elucidation of vRNA interactomes will open new avenues of research, including pathways to the discovery of host factors with therapeutic potential against viruses.
{"title":"Exploring the expanding universe of host-virus interactions mediated by viral RNA","authors":"Alfredo Castello, Lucía Álvarez, Wael Kamel, Louisa Iselin, Janosch Hennig","doi":"10.1016/j.molcel.2024.08.027","DOIUrl":"https://doi.org/10.1016/j.molcel.2024.08.027","url":null,"abstract":"RNA is a central molecule in RNA virus biology; however, the interactions that it establishes with the host cell are only starting to be elucidated. In recent years, a methodology revolution has dramatically expanded the scope of host-virus interactions involving the viral RNA (vRNA). A second wave of method development has enabled the precise study of these protein-vRNA interactions in a life cycle stage-dependent manner, as well as providing insights into the interactome of specific vRNA species. This review discusses these technical advances and describes the new regulatory mechanisms that have been identified through their use. Among these, we discuss the importance of vRNA in regulating protein function through a process known as riboregulation. We envision that the elucidation of vRNA interactomes will open new avenues of research, including pathways to the discovery of host factors with therapeutic potential against viruses.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"33 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142369147","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-03DOI: 10.1016/j.molcel.2024.09.003
Blerta Xhemalçe, Kyle M. Miller, Natalia Gromak
Complex pathways involving the DNA damage response (DDR) contend with cell-intrinsic and -extrinsic sources of DNA damage. DDR mis-regulation results in genome instability that can contribute to aging and diseases including cancer and neurodegeneration. Recent studies have highlighted key roles for several RNA species in the DDR, including short RNAs and RNA/DNA hybrids (R-loops) at DNA break sites, all contributing to efficient DNA repair. RNAs can undergo more than 170 distinct chemical modifications. These RNA modifications have emerged as key orchestrators of the DDR. Here, we highlight the function of enzyme- and non-enzyme-induced RNA modifications in the DDR, with particular emphasis on m6A, m5C, and RNA editing. We also discuss stress-induced RNA damage, including RNA alkylation/oxidation, RNA-protein crosslinks, and UV-induced RNA damage. Uncovering molecular mechanisms that underpin the contribution of RNA modifications to DDR and genome stability will have direct application to disease and approaches for therapeutic intervention.
{"title":"Epitranscriptome in action: RNA modifications in the DNA damage response","authors":"Blerta Xhemalçe, Kyle M. Miller, Natalia Gromak","doi":"10.1016/j.molcel.2024.09.003","DOIUrl":"https://doi.org/10.1016/j.molcel.2024.09.003","url":null,"abstract":"Complex pathways involving the DNA damage response (DDR) contend with cell-intrinsic and -extrinsic sources of DNA damage. DDR mis-regulation results in genome instability that can contribute to aging and diseases including cancer and neurodegeneration. Recent studies have highlighted key roles for several RNA species in the DDR, including short RNAs and RNA/DNA hybrids (R-loops) at DNA break sites, all contributing to efficient DNA repair. RNAs can undergo more than 170 distinct chemical modifications. These RNA modifications have emerged as key orchestrators of the DDR. Here, we highlight the function of enzyme- and non-enzyme-induced RNA modifications in the DDR, with particular emphasis on m<sup>6</sup>A, m<sup>5</sup>C, and RNA editing. We also discuss stress-induced RNA damage, including RNA alkylation/oxidation, RNA-protein crosslinks, and UV-induced RNA damage. Uncovering molecular mechanisms that underpin the contribution of RNA modifications to DDR and genome stability will have direct application to disease and approaches for therapeutic intervention.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"57 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142369142","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-03DOI: 10.1016/j.molcel.2024.09.007
Jimmy K. Guo, Mario R. Blanco, Mitchell Guttman
Many reported PRC2-RNA interactions have been shown to be functionally dispensable, raising questions about whether they occur in vivo. Here, we lay out technical issues with existing evidence for direct binding and argue that there is currently a lack of biochemical or functional evidence for direct PRC2-RNA binding in vivo.
{"title":"PRC2-RNA interactions: Viewpoint from Jimmy K. Guo, Mario R. Blanco, and Mitchell Guttman","authors":"Jimmy K. Guo, Mario R. Blanco, Mitchell Guttman","doi":"10.1016/j.molcel.2024.09.007","DOIUrl":"https://doi.org/10.1016/j.molcel.2024.09.007","url":null,"abstract":"Many reported PRC2-RNA interactions have been shown to be functionally dispensable, raising questions about whether they occur <em>in vivo</em>. Here, we lay out technical issues with existing evidence for direct binding and argue that there is currently a lack of biochemical or functional evidence for direct PRC2-RNA binding <em>in vivo</em>.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"15 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142369138","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-03DOI: 10.1016/j.molcel.2024.08.036
Tucker J. Carrocci, Karla M. Neugebauer
Proper gene expression requires the collaborative effort of multiple macromolecular machines to produce functional messenger RNA. As RNA polymerase II (RNA Pol II) transcribes DNA, the nascent pre-messenger RNA is heavily modified by other complexes such as 5′ capping enzymes, the spliceosome, the cleavage, and polyadenylation machinery as well as RNA-modifying/editing enzymes. Recent evidence has demonstrated that pre-mRNA splicing and 3′ end cleavage can occur on similar timescales as transcription and significantly cross-regulate. In this review, we discuss recent advances in co-transcriptional processing and how it contributes to gene regulation. We highlight how emerging areas—including coordinated splicing events, physical interactions between the RNA synthesis and modifying machinery, rapid and delayed splicing, and nuclear organization—impact mRNA isoforms. Coordination among RNA-processing choices yields radically different mRNA and protein products, foreshadowing the likely regulatory importance of co-transcriptional RNA folding and co-transcriptional modifications that have yet to be characterized in detail.
基因的正常表达需要多种大分子机器的协同努力，才能产生功能性信使 RNA。当 RNA 聚合酶 II（RNA Pol II）转录 DNA 时，新生的前信使 RNA 会被其他复合体（如 5′封端酶、剪接体、裂解和多聚腺苷化机制以及 RNA 修饰/编辑酶）大量修饰。最近的证据表明，前 mRNA 剪接和 3′末端裂解可与转录发生在相似的时间尺度上，并具有显著的交叉调节作用。在这篇综述中，我们将讨论共转录处理的最新进展及其如何促进基因调控。我们强调了新出现的领域--包括协调剪接事件、RNA 合成和修饰机制之间的物理相互作用、快速和延迟剪接以及核组织--是如何影响 mRNA 同工型的。RNA加工选择之间的协调产生了截然不同的mRNA和蛋白质产物，这预示着共转录RNA折叠和共转录修饰可能具有重要的调控作用，而这些作用尚有待详细描述。
{"title":"Emerging and re-emerging themes in co-transcriptional pre-mRNA splicing","authors":"Tucker J. Carrocci, Karla M. Neugebauer","doi":"10.1016/j.molcel.2024.08.036","DOIUrl":"https://doi.org/10.1016/j.molcel.2024.08.036","url":null,"abstract":"Proper gene expression requires the collaborative effort of multiple macromolecular machines to produce functional messenger RNA. As RNA polymerase II (RNA Pol II) transcribes DNA, the nascent pre-messenger RNA is heavily modified by other complexes such as 5′ capping enzymes, the spliceosome, the cleavage, and polyadenylation machinery as well as RNA-modifying/editing enzymes. Recent evidence has demonstrated that pre-mRNA splicing and 3′ end cleavage can occur on similar timescales as transcription and significantly cross-regulate. In this review, we discuss recent advances in co-transcriptional processing and how it contributes to gene regulation. We highlight how emerging areas—including coordinated splicing events, physical interactions between the RNA synthesis and modifying machinery, rapid and delayed splicing, and nuclear organization—impact mRNA isoforms. Coordination among RNA-processing choices yields radically different mRNA and protein products, foreshadowing the likely regulatory importance of co-transcriptional RNA folding and co-transcriptional modifications that have yet to be characterized in detail.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"10 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142369145","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-03DOI: 10.1016/j.molcel.2024.08.028
Johanna Franziska Seidler, Katja Sträßer
Nuclear messenger RNA (mRNA) export is vital for cell survival under both physiological and stress conditions. To cope with stress, cells block bulk mRNA export while selectively exporting stress-specific mRNAs. Under physiological conditions, nuclear adaptor proteins recruit the mRNA exporter to the mRNA for export. By contrast, during stress conditions, the mRNA exporter is likely directly recruited to stress-specific mRNAs at their transcription sites to facilitate selective mRNA export. In this review, we summarize our current understanding of nuclear mRNA export. Importantly, we explore insights into the mechanisms that block bulk mRNA export and facilitate transcript-specific mRNA export under stress, highlighting the gaps that still need to be filled.
{"title":"Understanding nuclear mRNA export: Survival under stress","authors":"Johanna Franziska Seidler, Katja Sträßer","doi":"10.1016/j.molcel.2024.08.028","DOIUrl":"https://doi.org/10.1016/j.molcel.2024.08.028","url":null,"abstract":"Nuclear messenger RNA (mRNA) export is vital for cell survival under both physiological and stress conditions. To cope with stress, cells block bulk mRNA export while selectively exporting stress-specific mRNAs. Under physiological conditions, nuclear adaptor proteins recruit the mRNA exporter to the mRNA for export. By contrast, during stress conditions, the mRNA exporter is likely directly recruited to stress-specific mRNAs at their transcription sites to facilitate selective mRNA export. In this review, we summarize our current understanding of nuclear mRNA export. Importantly, we explore insights into the mechanisms that block bulk mRNA export and facilitate transcript-specific mRNA export under stress, highlighting the gaps that still need to be filled.","PeriodicalId":18950,"journal":{"name":"Molecular Cell","volume":"42 1","pages":""},"PeriodicalIF":16.0,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142369146","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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