Cell Chemical Biology最新文献

{"title":"GLP-1R and GIPR crosstalk modulates insulinotropic signaling pathways","authors":"Peter Lindquist, Luuk R. Hoegen Dijkhof, Anna K. Drzazga, Pierre Sabatier, Tomasz M. Stepniewski, Louise Granlund, Maico Y. Lechner, Yi Zhong, Lærke S. Gasbjerg, Bolette Hartmann, Volker M. Lauschke, Jens J. Holst, Jesper V. Olsen, Olle Korsgren, Jana Selent, Shane C. Wright, Alexander S. Hauser, Mette M. Rosenkilde","doi":"10.1016/j.chembiol.2026.06.003","DOIUrl":"10.1016/j.chembiol.2026.06.003","url":null,"abstract":"<div><ul><li><span>•</span><span><div>GLP-1 and semaglutide (but not exendin 4 or GIP) induce GLP-1R-GIPR heterodimerization</div></span></li><li><span>•</span><span><div>GLP-1R/GIPR crosstalk rewires receptor trafficking and signaling</div></span></li><li><span>•</span><span><div>GLP-1R boosts GIPR signaling β-arrestin-dependently, while GIPR dampens GLP-1R</div></span></li><li><span>•</span><span><div>GIPR expression associates with adiposity and diabetes-related human phenotypes</div></span></li></ul></div><div>Drugs targeting the GLP-1R and GIPR have transformed the treatment of type 2 diabetes and obesity, but their combined mechanisms are not fully understood. We discovered ligand-dependent heterodimerization between GLP-1R and GIPR, which alters their signaling. Structurally, the dimerization occurs between TM4 of GLP-1R and TM1 and TM2 of GIPR. We found that different GLP-1R agonists promote receptor dimerization in various ways, unlike GIPR agonists, resulting in different signaling outcomes in human pancreatic islets. Additionally, GLP-1R-GIPR heterodimers co-internalize upon GLP-1R activation, affecting GIPR’s intracellular localization. Receptor stoichiometry influences signaling modulation: Higher GLP-1R levels enhance GIPR responses β-arrestin dependently, while higher GIPR levels reduce GLP-1R activity. Notably, changes in GIPR expression are associated with adiposity and diabetic traits. These interactions influence receptor signaling, trafficking, drug responses, and metabolic phenotypes. Our research redefines incretin receptor pharmacology by highlighting heterodimerization and receptor balance as key to signaling regulation. It offers a framework for designing new therapeutics that leverage receptor crosstalk and expression dynamics for better metabolic health.</div><div><div>Drugs targeting glucagon-like peptide-1 and glucose-dependent insulinotropic polypeptide receptors (GLP-1R and GIPR) show strong clinical effects in type 2 diabetes and obesity. Both GIPR agonism and antagonism enhance GLP-1R agonist efficacy, indicating important incretin receptor crosstalk. We show that GLP-1 and semaglutide, but not exendin-4, promote heterodimerization between GLP-1R and GIPR through interactions between TM4 of GLP-1R and TM1/2 of GIPR. Phosphoproteomics and molecular dynamics reveal that dimerizing and non-dimerizing agonists differentially influence GLP-1R, activating divergent signaling pathways in human pancreatic islets. Moreover, semaglutide and exenatide display distinct patterns in their FDA-reported safety profiles. When co-expressed, GLP-1R enhances GIPR signaling in a β-arrestin-dependent manner, while increasing GIPR levels decreases GLP-1R signaling. Additionally, we show that changes in <em>GIPR</em> expression are clinically associated with adiposity and diabetic phenotypes. These findings highlight heterodimerization and receptor expression as key modulators of GLP-1R/GIPR signaling, offering mechanistic insights, and ","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 9","pages":"Pages 1284-1299.e8"},"PeriodicalIF":9.0,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148409937","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":"N-acetyltransferase 10 regulates chemokine expression in keratinocytes and promotes atopic dermatitis","authors":"Jinjin Shao, Linying Wang, Zhichao Ye, Kexin Wang, Zeren Shen, Ziyi Hong, Ruimin Sun, Lili Zhang, Fang Liu, Siming Zhang, Yunxiang Chen, Zhiqi Xie, Lijiang Zhang","doi":"10.1016/j.chembiol.2026.06.012","DOIUrl":"10.1016/j.chembiol.2026.06.012","url":null,"abstract":"<div><ul><li><span>•</span><span><div>NAT10 is upregulated in keratinocytes and drives skin inflammation in AD</div></span></li><li><span>•</span><span><div>NAT10-mediated ac4C modification enhances <em>RELB</em> mRNA stability</div></span></li><li><span>•</span><span><div>The NAT10/ac4C/RelB axis promotes neutrophil-dominant immune recruitment</div></span></li><li><span>•</span><span><div>Pharmacological inhibition of NAT10 by Remodelin alleviates AD pathology</div></span></li></ul></div><div>Chronic inflammatory skin disorders, such as atopic dermatitis (AD), affect hundreds of millions of individuals worldwide; yet, the molecular mechanisms bridging epithelial barrier dysfunction and subsequent immune activation remain incompletely understood. This study identifies an epitranscriptomic regulatory mechanism in skin immunity by demonstrating that NAT10-mediated RNA cytidine acetylation (ac4C) plays a key role in epithelial-driven inflammation. Rather than operating merely as a generic cellular maintenance factor, NAT10 contributes to the stabilization of specific inflammatory transcripts within barrier-forming keratinocytes, facilitating a pro-inflammatory microenvironment that promotes innate immune cell recruitment. Beyond characterizing this pathway in inflammatory biology, we demonstrate that pharmacological inhibition of this RNA-modifying enzyme mitigates clinical symptoms in preclinical models without apparent systemic toxicity. By connecting chemical RNA modifications to tissue-level immune crosstalk, these findings advance our understanding of tissue homeostasis and provide a conceptual framework for investigating epitranscriptome-targeted strategies in chronic barrier and inflammatory diseases.</div><div><div>Atopic dermatitis (AD) is a chronic relapsing inflammatory skin disorder with complex immunological underpinnings, yet the role of the RNA acetyltransferase NAT10 in its pathogenesis remains unclear. We investigated NAT10 function through cutaneous NAT10 knockdown (microneedle-delivered AAV-shRNA) and pharmacological inhibition (Remodelin), using 2,4-dinitrochlorobenzene- and ovalbumin-induced murine AD models combined with IFN-γ/TNF-α-stimulated HaCaT keratinocytes. Results showed elevated NAT10 expression and acetylcytidine modification in AD keratinocytes. NAT10 knockdown ameliorated skin pathology, reduced serum IgE, and selectively limited neutrophil infiltration by suppressing chemokines (CXCL8, CCL5, CXCL9, CXCL10, CCL2), whereas its overexpression promoted their expression. Mechanistically, NAT10 stabilized <em>RELB</em> mRNA via acetylcytidine modification, thereby activating NF-κB signaling. Remodelin suppressed keratinocyte chemokine production and neutrophil recruitment, improving skin lesions without toxicity. Collectively, NAT10 emerges as a central regulator of keratinocyte-driven inflammation and a viable therapeutic target in AD.</div></div><div>Atopic dermatitis (AD) is a chronic relapsing inflammatory skin disor","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 9","pages":"Pages 1237-1251.e7"},"PeriodicalIF":9.0,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148560244","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":"Rapamycin targetome mining identifies RBBP7 as a druggable epigenetic vulnerability in hepatocellular carcinoma","authors":"Zan Gao,Le Sun,Jianlong Li,Heng Lv,Yingnan You,Kun Wang,Nan Su,Lin Wang,Nan Liu,Junhao Hu,Hong Jiang,Bing Shan,Yaoyang Zhang","doi":"10.1016/j.chembiol.2026.08.012","DOIUrl":"https://doi.org/10.1016/j.chembiol.2026.08.012","url":null,"abstract":"Identifying therapeutic protein targets is challenging due to unpredictable druggability. Exploring multi-purpose drug targetomes, such as that of rapamycin, offers a valuable strategy for target discovery. Here, using chemical proteomics, we identified the histone-binding protein RBBP7 as a previously unrecognized target of rapamycin. Rapamycin disrupts the RBBP7-H4 interaction, leading to reduced histone H4 acetylation and downregulation of DNMT1. Based on this mechanism, we designed RBBP7-targeting peptides (RBBP7-TPs). RBBP7-TP4 exhibited potent anti-tumor activity in both cellular and xenograft mouse models of hepatocellular carcinoma (HCC). Furthermore, RBBP7-TP4 synergized with HDAC inhibitors to enhance epigenetic efficacy in HCC models, supporting a promising combination strategy. Collectively, our findings highlight the value of mining multi-purpose drug targetomes for therapeutic target discovery. RBBP7 is established as a druggable target in cancer, and RBBP7-TP4 represents a potential peptide-based therapeutic candidate.","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"16 1","pages":""},"PeriodicalIF":8.6,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148964443","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":"Neuronal translational control in physiology, infection, and inflammation","authors":"Felix Fischbach,Henrike K. Grosshans,Lars Binkle-Ladisch,Manuel A. Friese","doi":"10.1016/j.chembiol.2026.08.011","DOIUrl":"https://doi.org/10.1016/j.chembiol.2026.08.011","url":null,"abstract":"Neurons are highly specialized cells whose function depends on dynamic regulation of gene expression. With increasing subcellular compartmentalization, neuronal gene expression becomes less dependent on transcription in the perinuclear region and tends to be increasingly controlled by local translation. The integrated stress response is a central, evolutionarily conserved pathway of translational regulation that maintains neuronal homeostasis through precise control of protein synthesis. Transient cellular stress, such as neuronal infection, adaptively activates this pathway, whereas persistent dysregulation, as observed in neuroinflammation and neurodegeneration, promotes neuronal dysfunction and damage. Here, we summarize key neuron-specific mechanisms governing translational homeostasis and discuss adaptive and detrimental molecular processes associated with neurological disease. Understanding this tightly regulated pathway and its context-dependent effects provides a framework for identifying mechanisms of neuronal vulnerability and for developing therapeutic strategies that target translational control in neurological disorders, while preserving its essential adaptive functions under physiological and acute stress conditions.","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"33 1","pages":""},"PeriodicalIF":8.6,"publicationDate":"2026-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148957861","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":"DPP3 restrains the non-canonical inflammasome through PEBP1 cleavage","authors":"Mengqian Li,Jiajia Zheng,Chun Kong,Xiangyang Geng,Xiuli Sun,Ning Shen,Shuo Wang,Pengyan Xia","doi":"10.1016/j.chembiol.2026.08.010","DOIUrl":"https://doi.org/10.1016/j.chembiol.2026.08.010","url":null,"abstract":"The non-canonical inflammasome is a protein complex involved in bacterial infections, and its activation leads to excessive inflammatory responses during sepsis. The precise regulation of the non-canonical inflammasome in the body remains unclear. Here, we found that some chemicals that chelate zinc ions positively regulated the activation of the non-canonical inflammasome. These chemicals acted by inhibiting the activity of dipeptidyl peptidase 3 (DPP3). DPP3 cleaved phosphatidylethanolamine binding protein 1 (PEBP1) to generate an N-terminal fragment, which could bind to caspase-4/11 and inhibit the response intensity of the non-canonical inflammasome. PEBP1 N terminus appeared in the serum of mice and patients with sepsis. DPP3-deficient mice exhibited stronger inflammatory cytokine responses and had poor survival in the LPS-induced sepsis model. Promoting the activity of DPP3 effectively constrained the response intensity of sepsis in mice and increased their survival. Our findings provide a perspective for understanding the molecular regulatory process of the non-canonical inflammasome in sepsis.","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"31 1","pages":""},"PeriodicalIF":8.6,"publicationDate":"2026-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148908802","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":"Targeted O-GlcNAcylation enables functional rewiring of c-Myc","authors":"Tongyang Xu,Zhihao Guo,Khadija S. Khan,Yunpeng Huang,Bowen Ma,Shuhui Ji,Jialin Liu,Dean W. Felsher,Billy Wai-Lung Ng","doi":"10.1016/j.chembiol.2026.08.008","DOIUrl":"https://doi.org/10.1016/j.chembiol.2026.08.008","url":null,"abstract":"Chemically induced proximity has transformed targeted protein degradation but has been applied far less extensively to directly reprogram protein function through post-translational modification (PTM). Here, we develop an O-GlcNAcylation-targeting Chimera (OGTAC) that recruits O-GlcNAc transferase (OGT) to the oncogenic transcription factor c-Myc, enabling targeted O-GlcNAcylation in living cells without globally perturbing cellular O-GlcNAcylation. OGTAC suppresses HeLa cell proliferation, rewires c-Myc genomic occupancy, and reprograms expression of the downstream oncogene MALAT1 in an O-GlcNAcylation-dependent manner. By selectively modulating the regulatory state of c-Myc rather than its abundance, OGTAC establishes targeted O-GlcNAcylation as a chemically induced proximity strategy for functional rewiring of transcription factors. More broadly, this work expands proximity-induced protein regulation beyond degradation to programmable PTM.","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"34 1","pages":""},"PeriodicalIF":8.6,"publicationDate":"2026-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148877414","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":"A lysis-derived PMSF and orthovanadate oxidant defines a distinct cysteine-engagement profile","authors":"Bethany E. Schaffer,Jung Seung Nam,Ceci A. Cohen,Clementina Mesaros,Robert W. Myers,Leigh Baxt,Kathryn E. Wellen,Lewis C. Cantley,Noah Dephoure,Nathaniel W. Snyder,Iok In Christine Chio,John Blenis","doi":"10.1016/j.chembiol.2026.08.005","DOIUrl":"https://doi.org/10.1016/j.chembiol.2026.08.005","url":null,"abstract":"Reactive cysteines serve important functions in proteins, and characterizing their engagement by different electrophiles facilitates biological discovery and covalent drug development. Here, we show that the common lysis buffer components phenylmethylsulfonyl fluoride (PMSF) and orthovanadate generate a lysis-derived oxidant that engages cysteines during cell lysis. This oxidant sulfonylates N-acetyl-D-glucosamine kinase (NAGK) C217, producing a mobility shift on SDS-PAGE. C217 lies within the ATP-binding pocket, and a C217S mutant exhibits reduced ATP affinity and enzymatic activity. Competitive iodoacetamide-alkyne activity-based protein profiling (IAA-ABPP) chemoproteomics further showed that the PMSF/orthovanadate oxidant defines a cysteine-engagement profile that partially differs from that of pervanadate. These findings reveal an unrecognized source of chemical reactivity during protein extraction that expands the toolkit for cysteine-engagement profiling and underscores how sample preparation chemistry shapes chemoproteomic measurements.","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"39 1","pages":""},"PeriodicalIF":8.6,"publicationDate":"2026-08-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148858169","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":"A STING inhibitor suppresses ferroptosis through radical-trapping antioxidant activity","authors":"Songlin Yin,Yan Li,Ting Mei,Jiayao Li,Xueting Wang,Xiaoxiao Li,Liguo Yang,Junhong Lin,Weijie Ye,Fujia Lu,Weimin Wang","doi":"10.1016/j.chembiol.2026.08.004","DOIUrl":"https://doi.org/10.1016/j.chembiol.2026.08.004","url":null,"abstract":"Renal ischemia-reperfusion injury (IRI), a leading cause of acute kidney injury, is driven by coordinated inflammatory signaling and ferroptotic cell death, yet effective therapies remain limited. Here, we show that H-151, a covalent stimulator of interferon genes (STING) inhibitor, also suppresses ferroptosis through a STING-independent mechanism. H-151 functions as a broad-spectrum radical-trapping antioxidant that directly scavenges radicals generated during the Fenton reaction, thereby blocking lipid peroxidation. In a murine renal IRI model, H-151 attenuated tissue damage and restored renal function through concurrent inhibition of STING signaling and ferroptosis. These findings establish radical-trapping antioxidant activity as an additional mechanism of H-151 and identify dual inhibition of inflammatory signaling and ferroptosis as a promising therapeutic strategy for IRI and related disorders.","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"54 1","pages":""},"PeriodicalIF":8.6,"publicationDate":"2026-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148821626","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":"Comparative protein engineering redirects the specificity of Clostridium botulinum proteases","authors":"Jason E. Garrido,Gabriela S. Salcedo,Max W. Strul,Shareen N. Ashby,Arjun S. Pamidi,Jaeho Cho,Katherine G. Waldvogel,Elizabeth L. Wiriadinata,Teodora Nedic,Natnicha Kaewtatip,Honoka Kato,Maya Chan,Rebekah P. Dyer,Gregory A. Weiss","doi":"10.1016/j.chembiol.2026.08.003","DOIUrl":"https://doi.org/10.1016/j.chembiol.2026.08.003","url":null,"abstract":"Botulinum neurotoxin serotypes A and E (BoNT/A and BoNT/E) cleave SNAP25 and are widely used in therapeutic applications. Redirecting the substrate specificity of their protease domains, LC/A and LC/E, could expand their utility to new therapeutic targets. Here, we report a comparative protein engineering strategy that integrates prior mutagenesis, bioinformatics, and structural insights to reprogram LC protease specificity. Directed evolution yielded a 14-mutation LC/A variant with 273-fold greater specificity for SNAP23 than a previously reported engineered protease. Insights from LC/A engineering then guided six rounds of directed evolution to generate an 8-mutation LC/E variant with a 26,000-fold increase in SNAP29 cleavage and no detectable activity toward SNAP25. Importantly, both engineered proteases retain their altered substrate preferences under physiologically relevant substrate and salt concentrations. Together, these findings establish comparative protein engineering as an effective framework for retargeting botulinum neurotoxin proteases.","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"26 1","pages":""},"PeriodicalIF":8.6,"publicationDate":"2026-08-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148821627","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":"Localized covalent targeting of NMDA receptors reprograms behavior","authors":"Daniel Bátora,Máté Varga,Sharad Kumar Suthar,András Málnási-Csizmadia","doi":"10.1016/j.chembiol.2026.08.001","DOIUrl":"https://doi.org/10.1016/j.chembiol.2026.08.001","url":null,"abstract":"Spatiotemporal control of neuronal activity has largely relied on genetically defined cell populations, limiting the ability to interrogate native biomolecules within intact circuits. Pharmacological approaches with high spatial precision are therefore needed to preserve physiological network architecture. Here, we demonstrate confined neuromodulation through two-photon molecular tattooing (sequential localized photocrosslinking). We introduce AL-701, an aryl azide derivatized photoreactive NMDA receptor antagonist that covalently binds receptors upon two-photon laser irradiation. In zebrafish larvae, molecular tattooing enabled spatially restricted inhibition of NMDA receptors in a hindbrain subregion regulating the acoustic startle reflex. This localized inhibition led to persistent suppression of NMDA receptor-dependent habituation, demonstrating that regionally restricted modulation of receptor function can alter behavior. Our results show the proof-of-concept for localized photocrosslinking within cell clusters in a vertebrate nervous system and thereby establish molecular tattooing as a robust chemical biology tool for circuit modulation and optically controlled reprogramming of behavior in vivo.","PeriodicalId":265,"journal":{"name":"Cell Chemical Biology","volume":"14 1","pages":""},"PeriodicalIF":8.6,"publicationDate":"2026-08-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148805870","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}