Cell Chemical Biology最新文献

{"title":"Understanding protein ISGylation, a multifaceted posttranslational modification","authors":"David Joseph Shirley,&nbsp;Euna Yoo","doi":"10.1016/j.chembiol.2026.06.006","DOIUrl":"10.1016/j.chembiol.2026.06.006","url":null,"abstract":"<div><div>ISG15 represents a key ubiquitin-like modifier induced primarily by interferon signaling. ISG15 is synthesized as a precursor, processed to a mature form, and covalently conjugated to substrates through a dedicated E1-E2-E3 enzymatic cascade involving UBE1L, UBE2L6, and E3 ligases such as HERC5, TRIM25, and ARIH1. This modification is reversed by deISGylases, particularly the highly specific protease USP18, which also negatively regulates interferon signaling. ISGylation impacts diverse molecular and cellular processes, including protein stability and function, protein-protein interaction, autophagy, transcription/translation, DNA damage response, and innate immunity. Advances in chemical biology and mass spectrometry-based proteomics have enabled the characterization of enzymes involved in (de)ISGylation and mapping of ISGylated proteins and sites. Dysregulated ISGylation is implicated in cancer, infection, neurodegenerative disorders, and inflammatory diseases, underscoring its broad pathophysiological relevance.</div></div><div>ISG15 represents a key ubiquitin-like modifier induced primarily by interferon signaling. ISG15 is synthesized as a precursor, processed to a mature form, and covalently conjugated to substrates through a dedicated E1-E2-E3 enzymatic cascade involving UBE1L, UBE2L6, and E3 ligases such as HERC5, TRIM25, and ARIH1. This modification is reversed by deISGylases, particularly the highly specific protease USP18, which also negatively regulates interferon signaling. ISGylation impacts diverse molecular and cellular processes, including protein stability and function, protein-protein interaction, autophagy, transcription/translation, DNA damage response, and innate immunity. Advances in chemical biology and mass spectrometry-based proteomics have enabled the characterization of enzymes involved in (de)ISGylation and mapping of ISGylated proteins and sites. Dysregulated ISGylation is implicated in cancer, infection, neurodegenerative disorders, and inflammatory diseases, underscoring its broad pathophysiological relevance.</div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (101KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div>","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 10","pages":"Pages 1459-1481"},"PeriodicalIF":9.0,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13372206/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148434433","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Meet the authors: Song-Iee Han and Akiyoshi Fukamizu","authors":"","doi":"10.1016/j.chembiol.2026.09.015","DOIUrl":"10.1016/j.chembiol.2026.09.015","url":null,"abstract":"<div><div>In an interview with Samantha Nelson, a scientific editor of <em>Cell Chemical Biology</em>, the authors of the review entitled “Arginine methylation in immunoregulation: mechanisms and therapeutic targeting” reflect on advances in their field, their scientific journeys, and the experiences that have shaped their research.</div></div><div>In an interview with Samantha Nelson, a scientific editor of <em>Cell Chemical Biology</em>, the authors of the review entitled “Arginine methylation in immunoregulation: mechanisms and therapeutic targeting” reflect on advances in their field, their scientific journeys, and the experiences that have shaped their research.</div>","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 10","pages":"Pages 1346-1347"},"PeriodicalIF":9.0,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149173074","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Non-enzymatic protein modifications at the interface of metabolism and immunity","authors":"Nicole S. Walker,&nbsp;James J. Galligan,&nbsp;Yael David,&nbsp;Anna Knörlein","doi":"10.1016/j.chembiol.2026.09.005","DOIUrl":"10.1016/j.chembiol.2026.09.005","url":null,"abstract":"<div><div>Immune cells are highly metabolically active throughout their life cycle, leading to elevated levels of a variety of reactive metabolites including reactive oxygen species, sugars, and lipid peroxidation products. These molecules covalently modify proteins, resulting in post-translational non-enzymatic covalent modifications (NECMs). Similar to their enzymatic counterparts, NECMs impact proteins’ structure, stability, localization, function, and interactome, thereby shaping cellular behavior, providing an additional layer of regulation to leukocyte function. With increasing evidence linking metabolic dysregulation to dysfunction of immune cells, it is becoming critical to understand the role NECMs play in regulating immune cell fate. This review highlights recent advances in our understanding of NECMs in immune cell function, including their roles in inflammation and immune responses. We further discuss emerging chemical biology technologies to detect, interrogate, and manipulate these modifications while outlining key challenges that will shape future studies of non-enzymatic protein modifications in immune regulation.</div></div><div>Immune cells are highly metabolically active throughout their life cycle, leading to elevated levels of a variety of reactive metabolites including reactive oxygen species, sugars, and lipid peroxidation products. These molecules covalently modify proteins, resulting in post-translational non-enzymatic covalent modifications (NECMs). Similar to their enzymatic counterparts, NECMs impact proteins’ structure, stability, localization, function, and interactome, thereby shaping cellular behavior, providing an additional layer of regulation to leukocyte function. With increasing evidence linking metabolic dysregulation to dysfunction of immune cells, it is becoming critical to understand the role NECMs play in regulating immune cell fate. This review highlights recent advances in our understanding of NECMs in immune cell function, including their roles in inflammation and immune responses. We further discuss emerging chemical biology technologies to detect, interrogate, and manipulate these modifications while outlining key challenges that will shape future studies of non-enzymatic protein modifications in immune regulation.</div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (141KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div>","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 10","pages":"Pages 1482-1500"},"PeriodicalIF":9.0,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149092129","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}

{"title":"Chemoproteomic profiling of itaconate-derived protein modifications","authors":"Youjia Wang,&nbsp;Chu Wang","doi":"10.1016/j.chembiol.2026.08.016","DOIUrl":"10.1016/j.chembiol.2026.08.016","url":null,"abstract":"<div><div>Itaconate is an emerging immunomodulatory metabolite produced in macrophages upon inflammatory activation and exhibits both immunoregulatory and bacterial-regulatory properties. Structurally, itaconate is a reactive α,β-unsaturated carboxylic acid that undergoes Michael addition with nucleophilic cysteine residues in proteins, generating a unique type of covalent post-translational modification termed itaconation. Here, we review recent progress in the systematic identification of itaconation by chemoproteomic methods. These studies have identified an expanding repertoire of itaconation targets in both host cells and pathogens, providing mechanistic insight into how itaconate regulates immune responses and modulates pathogen tolerance. We further highlight the recent discovery of lysine itaconylation, a novel acylation mediated by itaconate, and briefly review chemoproteomic studies that have globally profiled the non-covalent targets of this immunoregulatory metabolite. Collectively, these chemoproteomic efforts provide rich resources to guide future functional studies and deepen our understanding of the multifaceted roles of itaconate in host-pathogen interactions.</div></div><div>Itaconate is an emerging immunomodulatory metabolite produced in macrophages upon inflammatory activation and exhibits both immunoregulatory and bacterial-regulatory properties. Structurally, itaconate is a reactive α,β-unsaturated carboxylic acid that undergoes Michael addition with nucleophilic cysteine residues in proteins, generating a unique type of covalent post-translational modification termed itaconation. Here, we review recent progress in the systematic identification of itaconation by chemoproteomic methods. These studies have identified an expanding repertoire of itaconation targets in both host cells and pathogens, providing mechanistic insight into how itaconate regulates immune responses and modulates pathogen tolerance. We further highlight the recent discovery of lysine itaconylation, a novel acylation mediated by itaconate, and briefly review chemoproteomic studies that have globally profiled the non-covalent targets of this immunoregulatory metabolite. Collectively, these chemoproteomic efforts provide rich resources to guide future functional studies and deepen our understanding of the multifaceted roles of itaconate in host-pathogen interactions.</div>","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 10","pages":"Pages 1501-1516"},"PeriodicalIF":9.0,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149019681","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Post-translational modifications in bacteria: From identification to function","authors":"Ashleigh L. Dale,&nbsp;Melanie Y. White,&nbsp;Stuart J. Cordwell","doi":"10.1016/j.chembiol.2026.08.018","DOIUrl":"10.1016/j.chembiol.2026.08.018","url":null,"abstract":"<div><div>Post-translational modifications (PTMs) provide molecular variety beyond the gene or amino acid codes. Diversity stems from a vast number of chemical species or physical changes that are regulated either enzymatically or non-enzymatically to provide transient or prolonged alterations to protein structure and function. Bacteria are wrongly considered “simple” due to their relatively small genomes; however, application of high-resolution methods in enrichment, identification, and quantitation by mass spectrometry (MS) has unleashed a plethora of site-specific PTM data unequivocally demonstrating that bacteria can undertake almost all modifications seen in eukaryotes, while also maintaining novel PTMs that occur specifically in these organisms. Despite this, our ability to exploit omics-level PTM data has not been comparable; determining site stoichiometry, understanding the roles conferred by PTMs, and characterizing the functions of identified PTM sites remain to be routinely achievable at scale. This review examines major PTMs and their importance in generating functional variations in bacterial proteins.</div></div><div>Post-translational modifications (PTMs) provide molecular variety beyond the gene or amino acid codes. Diversity stems from a vast number of chemical species or physical changes that are regulated either enzymatically or non-enzymatically to provide transient or prolonged alterations to protein structure and function. Bacteria are wrongly considered “simple” due to their relatively small genomes; however, application of high-resolution methods in enrichment, identification, and quantitation by mass spectrometry (MS) has unleashed a plethora of site-specific PTM data unequivocally demonstrating that bacteria can undertake almost all modifications seen in eukaryotes, while also maintaining novel PTMs that occur specifically in these organisms. Despite this, our ability to exploit omics-level PTM data has not been comparable; determining site stoichiometry, understanding the roles conferred by PTMs, and characterizing the functions of identified PTM sites remain to be routinely achievable at scale. This review examines major PTMs and their importance in generating functional variations in bacterial proteins.</div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (132KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div>","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 10","pages":"Pages 1517-1543"},"PeriodicalIF":9.0,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149070992","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Arginine methylation in immunoregulation: Mechanisms and therapeutic targeting","authors":"Song-Iee Han,&nbsp;Sachiko Toma-Fukai,&nbsp;Jun-Dal Kim,&nbsp;Koichiro Kako,&nbsp;Hiroaki Daitoku,&nbsp;Akiyoshi Fukamizu","doi":"10.1016/j.chembiol.2026.09.003","DOIUrl":"10.1016/j.chembiol.2026.09.003","url":null,"abstract":"<div><div>Post-translational modifications (PTMs) are central regulators of immune cell function, linking extracellular signals to the regulation of intracellular gene expression. Among these, protein arginine methylation, catalyzed by protein arginine methyltransferases (PRMTs), is a key mechanism that connects epigenetic control with signal transduction. PRMTs modify both histone and non-histone substrates, thereby regulating chromatin accessibility, transcriptional programs, and immune signaling pathways. Recent studies have shown that arginine methylation modulates immune cell activation, differentiation, and effector functions, whereas its dysregulation contributes to tumor immune evasion and chronic inflammation. Notably, alterations in PRMT activity have been increasingly suggested in age-associated immune remodeling and inflammaging. In this review, we integrate current evidence showing how PRMT-mediated arginine methylation coordinates chromatin regulation, RNA metabolism, and immune signaling, and examine how these mechanisms shape immune homeostasis, tumor immunity, inflammaging, and opportunities for therapeutic intervention.</div></div><div>Post-translational modifications (PTMs) are central regulators of immune cell function, linking extracellular signals to the regulation of intracellular gene expression. Among these, protein arginine methylation, catalyzed by protein arginine methyltransferases (PRMTs), is a key mechanism that connects epigenetic control with signal transduction. PRMTs modify both histone and non-histone substrates, thereby regulating chromatin accessibility, transcriptional programs, and immune signaling pathways. Recent studies have shown that arginine methylation modulates immune cell activation, differentiation, and effector functions, whereas its dysregulation contributes to tumor immune evasion and chronic inflammation. Notably, alterations in PRMT activity have been increasingly suggested in age-associated immune remodeling and inflammaging. In this review, we integrate current evidence showing how PRMT-mediated arginine methylation coordinates chromatin regulation, RNA metabolism, and immune signaling, and examine how these mechanisms shape immune homeostasis, tumor immunity, inflammaging, and opportunities for therapeutic intervention.</div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (198KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div>","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 10","pages":"Pages 1422-1442"},"PeriodicalIF":9.0,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149090235","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}

{"title":"Location, location, deUFMylation: Coordinating ribosome quality control at the ER","authors":"Alexander R. Mikesell,&nbsp;Zachary T. Campbell","doi":"10.1016/j.chembiol.2026.08.015","DOIUrl":"10.1016/j.chembiol.2026.08.015","url":null,"abstract":"<div><div>Endoplasmic-reticulum-associated ribosome quality control (ER-RQC) requires ubiquitin-fold modifier 1 (UFM1) for UFMylation of the ribosomal protein RPL26. In the August 6 issue of <em>Molecular Cell</em>, Mao et al.<span><span>¹</span></span> identify an ER-associated complex (UFSP2/ODR4) as critical for deUFMylation of RPL26 and uncover a critical physiologic role for UFSP2 in neuronal proteostasis.</div></div><div>Endoplasmic-reticulum-associated ribosome quality control (ER-RQC) requires ubiquitin-fold modifier 1 (UFM1) for UFMylation of the ribosomal protein RPL26. In the August 6 issue of <em>Molecular Cell</em>, Mao et al.<span><span>¹</span></span> identify an ER-associated complex (UFSP2/ODR4) as critical for deUFMylation of RPL26 and uncover a critical physiologic role for UFSP2 in neuronal proteostasis.</div>","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 10","pages":"Pages 1353-1355"},"PeriodicalIF":9.0,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149173072","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}

{"title":"Targeting protein arginine methyltransferases to enhance cancer immunotherapy","authors":"Nivine Srour,&nbsp;Chunxiao Zhao,&nbsp;Stéphane Richard","doi":"10.1016/j.chembiol.2026.09.010","DOIUrl":"10.1016/j.chembiol.2026.09.010","url":null,"abstract":"<div><div>Arginine methylation is a post-translational modification found on many proteins, including RNA-binding proteins, signaling molecules, histones, and heat shock proteins, where it can alter protein-protein and protein-nucleic acid interactions. Arginine methylation regulates many cellular pathways, including RNA metabolism, signal transduction, gene expression, cellular stress responses, DNA repair, and, more recently, innate immune sensing. Here, we discuss recent advances in innate immune sensing and the emerging role of arginine methylation in suppressing tumor immune visibility. We describe current knowledge of protein arginine methyltransferase (PRMT) inhibitors and degraders and their use from preclinical models to clinical trials, alone or in combination with other therapies, to reduce tumor progression and enhance the effectiveness of cancer immunotherapy.</div></div><div>Arginine methylation is a post-translational modification found on many proteins, including RNA-binding proteins, signaling molecules, histones, and heat shock proteins, where it can alter protein-protein and protein-nucleic acid interactions. Arginine methylation regulates many cellular pathways, including RNA metabolism, signal transduction, gene expression, cellular stress responses, DNA repair, and, more recently, innate immune sensing. Here, we discuss recent advances in innate immune sensing and the emerging role of arginine methylation in suppressing tumor immune visibility. We describe current knowledge of protein arginine methyltransferase (PRMT) inhibitors and degraders and their use from preclinical models to clinical trials, alone or in combination with other therapies, to reduce tumor progression and enhance the effectiveness of cancer immunotherapy.</div>","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 10","pages":"Pages 1443-1458"},"PeriodicalIF":9.0,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149173070","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}

{"title":"Voices: Emerging molecular mechanisms and open questions in post-translational modifications","authors":"Lauren V. Albrecht,&nbsp;Xiucong Bao,&nbsp;Philip A. Cole,&nbsp;Zhenyi Hu,&nbsp;Shan Li (李姗),&nbsp;Shixian Lin,&nbsp;Rebecca A. Scheck,&nbsp;Christopher Schofield,&nbsp;Amy Weeks,&nbsp;Qingfei Zheng","doi":"10.1016/j.chembiol.2026.09.017","DOIUrl":"10.1016/j.chembiol.2026.09.017","url":null,"abstract":"<div><div>Post-translational modifications expand the functional diversity of the proteome and provide dynamic control over protein activity, localization, interactions, and stability, making them fundamental regulators of cellular function. In this Voices piece accompanying a special issue on post-translational modifications in <em>Cell Chemical Biology</em>, we ask researchers from across the field: what recent advances in post-translational modification research are most exciting, what important challenges remain, and what are the next big questions for the field?</div></div><div>Post-translational modifications expand the functional diversity of the proteome and provide dynamic control over protein activity, localization, interactions, and stability, making them fundamental regulators of cellular function. In this Voices piece accompanying a special issue on post-translational modifications in <em>Cell Chemical Biology</em>, we ask researchers from across the field: what recent advances in post-translational modification research are most exciting, what important challenges remain, and what are the next big questions for the field?</div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (254KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div>","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 10","pages":"Pages 1348-1352"},"PeriodicalIF":9.0,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149173073","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}

{"title":"Meet the authors: Cameron Douglas and Ciaran Seath","authors":"Cameron Douglas,&nbsp;Ciaran Seath","doi":"10.1016/j.chembiol.2026.09.014","DOIUrl":"10.1016/j.chembiol.2026.09.014","url":null,"abstract":"<div><div>In an interview with Samantha Nelson, a scientific editor of <em>Cell Chemical Biology</em>, the authors of the review entitled “Chemical biology tools for studying histone post-translational modifications” share their perspectives on their field and life as scientists.</div></div><div>In an interview with Samantha Nelson, a scientific editor of <em>Cell Chemical Biology</em>, the authors of the review entitled “Chemical biology tools for studying histone post-translational modifications” share their perspectives on their field and life as scientists.</div><div><span><figure><span><img><ol><li><span><span>Download: <span>Download high-res image (247KB)</span></span></span></li><li><span><span>Download: <span>Download full-size image</span></span></span></li></ol></span></figure></span></div>","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 10","pages":"Pages 1344-1345"},"PeriodicalIF":9.0,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149173075","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}