Pub Date : 2026-01-09DOI: 10.1038/s41589-025-02130-9
Catherine A. Musselman, Tatiana G. Kutateladze
{"title":"Targeting epigenetic readers","authors":"Catherine A. Musselman, Tatiana G. Kutateladze","doi":"10.1038/s41589-025-02130-9","DOIUrl":"https://doi.org/10.1038/s41589-025-02130-9","url":null,"abstract":"","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"47 1","pages":""},"PeriodicalIF":14.8,"publicationDate":"2026-01-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145938278","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 : 2026-01-09DOI: 10.1038/s41589-025-02128-3
Yuefeng Ma,Leshan Yang,Yantong Chen,Michael W Chen,Wen Yu,Yifan Dai
Engineering synthetic intrinsically disordered proteins (synIDPs) enables regulation of biomolecular condensation and protein solubility. However, limited understanding of how sequence-dependent interaction cooperativity relates to the fitness impacts of synIDPs on endogenous cellular processes constrains our design capability. Here, to circumvent this design challenge, we present a systematic directed evolution method for the evolution of synIDPs capable of mediating diverse phase behaviors in living cells. The selection methods allow us to evolve a toolbox of synIDPs with distinct phase behaviors and thermoresponsive features in living cells, leading to the evolution of synthetic condensates. The reverse-selection method further allows us to select synIDPs as solubility tags. We demonstrate the applications of the evolved synIDPs in protein circuits to (1) regulate intracellular protein activity and (2) reverse antibiotic resistance. Our systematic evolution and selection strategies provide a versatile platform for developing synIDPs for broad applications in synthetic biology and biotechnology.
{"title":"Directed evolution of functional intrinsically disordered proteins.","authors":"Yuefeng Ma,Leshan Yang,Yantong Chen,Michael W Chen,Wen Yu,Yifan Dai","doi":"10.1038/s41589-025-02128-3","DOIUrl":"https://doi.org/10.1038/s41589-025-02128-3","url":null,"abstract":"Engineering synthetic intrinsically disordered proteins (synIDPs) enables regulation of biomolecular condensation and protein solubility. However, limited understanding of how sequence-dependent interaction cooperativity relates to the fitness impacts of synIDPs on endogenous cellular processes constrains our design capability. Here, to circumvent this design challenge, we present a systematic directed evolution method for the evolution of synIDPs capable of mediating diverse phase behaviors in living cells. The selection methods allow us to evolve a toolbox of synIDPs with distinct phase behaviors and thermoresponsive features in living cells, leading to the evolution of synthetic condensates. The reverse-selection method further allows us to select synIDPs as solubility tags. We demonstrate the applications of the evolved synIDPs in protein circuits to (1) regulate intracellular protein activity and (2) reverse antibiotic resistance. Our systematic evolution and selection strategies provide a versatile platform for developing synIDPs for broad applications in synthetic biology and biotechnology.","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"124 12 1","pages":""},"PeriodicalIF":14.8,"publicationDate":"2026-01-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145937891","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 : 2026-01-09DOI: 10.1038/s41589-025-02121-w
Meng Yang,Chunping Sun,Yonglin He,Hongwu Qian
Lipid phosphate phosphatases (LPPs) catalyze the dephosphorylation of a broad range of bioactive lipid phosphates, including lysophosphatidic acid and sphingosine-1-phosphate, playing essential roles in embryonic vasculogenesis, cell differentiation and inflammation. Here we present the cryo-electron microscopic structure of human LPP1 as a tetramer with C4 symmetry. We capture the phosphohistidine intermediate state by using vanadate as a phosphate analog, where vanadate is coordinated by positively charged residues from three conserved motifs (C1, C2 and C3). Structural investigations of LPP1 variants with mutations in two catalytic histidine residues confirm that the histidine in the C2 motif facilitates phosphate bond cleavage. Enzymatic assays validate our structural observations. Additionally, a phosphatidylinositol 4,5-bisphosphate (PIP2) molecule was discovered in the LPP1 structure, underscoring a potential regulatory role for PIP2 in the catalytic activity of LPP1.
{"title":"Structural basis for the catalytic mechanism of human lipid phosphate phosphatases.","authors":"Meng Yang,Chunping Sun,Yonglin He,Hongwu Qian","doi":"10.1038/s41589-025-02121-w","DOIUrl":"https://doi.org/10.1038/s41589-025-02121-w","url":null,"abstract":"Lipid phosphate phosphatases (LPPs) catalyze the dephosphorylation of a broad range of bioactive lipid phosphates, including lysophosphatidic acid and sphingosine-1-phosphate, playing essential roles in embryonic vasculogenesis, cell differentiation and inflammation. Here we present the cryo-electron microscopic structure of human LPP1 as a tetramer with C4 symmetry. We capture the phosphohistidine intermediate state by using vanadate as a phosphate analog, where vanadate is coordinated by positively charged residues from three conserved motifs (C1, C2 and C3). Structural investigations of LPP1 variants with mutations in two catalytic histidine residues confirm that the histidine in the C2 motif facilitates phosphate bond cleavage. Enzymatic assays validate our structural observations. Additionally, a phosphatidylinositol 4,5-bisphosphate (PIP2) molecule was discovered in the LPP1 structure, underscoring a potential regulatory role for PIP2 in the catalytic activity of LPP1.","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"397 1","pages":""},"PeriodicalIF":14.8,"publicationDate":"2026-01-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145937896","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 : 2026-01-09DOI: 10.1038/s41589-025-02132-7
Sha Liu,Jinzhao Liu,Yinqiao Wu,Xinyi Yao,Xiang Li,Xinyu Dong,Qi Li,Hayden Jit Hei Cheung,Kwan Yuen Wong,Yuanyuan Li,Mu He,Chi-Leung Chiang,Jason Wing Hon Wong,Haitao Li,Weiping Wang,Xin Li,Xiang David Li
Histone acetyltransferases (HATs) modify chromatin to regulate gene expression. Instead of acting alone, HATs function in complexes with other proteins, leading to variations in substrate specificity, genomic localization and cellular function. To understand the complex-dependent roles of HATs, we present a chemical approach to specifically dissociate ATAC (Ada-two-A-containing) HAT complex from chromatin without perturbing other complexes. Rather than targeting the shared HAT enzyme, we developed chemical inhibitors for an ATAC-specific subunit, YEATS2. The most effective inhibitor, LS-170, specifically reduced the chromatin occupancy of the ATAC complex, decreased the ATAC-dependent histone acetylation level and downregulated the expression of ATAC-governed genes, leading to significantly suppressed tumor growth in a lung cancer mouse model. This study not only sheds light on the regulatory roles of the ATAC HAT complex in gene transcription but also provides evidence that the chemical inhibition of the ATAC complex can be a promising therapeutic strategy.
{"title":"Complex-specific inhibitors for interrogating ATAC histone acetyltransferase complex.","authors":"Sha Liu,Jinzhao Liu,Yinqiao Wu,Xinyi Yao,Xiang Li,Xinyu Dong,Qi Li,Hayden Jit Hei Cheung,Kwan Yuen Wong,Yuanyuan Li,Mu He,Chi-Leung Chiang,Jason Wing Hon Wong,Haitao Li,Weiping Wang,Xin Li,Xiang David Li","doi":"10.1038/s41589-025-02132-7","DOIUrl":"https://doi.org/10.1038/s41589-025-02132-7","url":null,"abstract":"Histone acetyltransferases (HATs) modify chromatin to regulate gene expression. Instead of acting alone, HATs function in complexes with other proteins, leading to variations in substrate specificity, genomic localization and cellular function. To understand the complex-dependent roles of HATs, we present a chemical approach to specifically dissociate ATAC (Ada-two-A-containing) HAT complex from chromatin without perturbing other complexes. Rather than targeting the shared HAT enzyme, we developed chemical inhibitors for an ATAC-specific subunit, YEATS2. The most effective inhibitor, LS-170, specifically reduced the chromatin occupancy of the ATAC complex, decreased the ATAC-dependent histone acetylation level and downregulated the expression of ATAC-governed genes, leading to significantly suppressed tumor growth in a lung cancer mouse model. This study not only sheds light on the regulatory roles of the ATAC HAT complex in gene transcription but also provides evidence that the chemical inhibition of the ATAC complex can be a promising therapeutic strategy.","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"112 1","pages":""},"PeriodicalIF":14.8,"publicationDate":"2026-01-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145937894","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 capped with dinucleoside polyphosphates has been discovered in bacteria and eukaryotes only recently. The likely mechanism of this specific capping involves direct incorporation of dinucleoside polyphosphates by RNA polymerase as noncanonical initiating nucleotides. However, how these compounds bind into the active site of RNA polymerase during transcription initiation is unknown. Here, we explored transcription initiation in vitro, using a series of DNA templates in combination with dinucleoside polyphosphates and model RNA polymerase from Thermus thermophilus. We observed that the transcription start site can vary on the basis of the compatibility of the specific template and dinucleoside polyphosphate. Cryo-electron microscopy structures of transcription initiation complexes with dinucleoside polyphosphates revealed that both nucleobase moieties can pair with the DNA template. The first encoded nucleotide pairs in a canonical Watson-Crick manner, whereas the second nucleobase pairs noncanonically in a reverse Watson-Crick manner. Our work provides a structural explanation of how dinucleoside polyphosphates initiate RNA transcription.
{"title":"Molecular insight into 5' RNA capping with NpnNs by bacterial RNA polymerase.","authors":"Valentina M Serianni,Jana Škerlová,Anna Knopp Dubánková,Anton Škríba,Hana Šváchová,Tereza Vučková,Anatolij Filimoněnko,Milan Fábry,Pavlína Řezáčová,Tomáš Kouba,Hana Cahova","doi":"10.1038/s41589-025-02134-5","DOIUrl":"https://doi.org/10.1038/s41589-025-02134-5","url":null,"abstract":"RNA capped with dinucleoside polyphosphates has been discovered in bacteria and eukaryotes only recently. The likely mechanism of this specific capping involves direct incorporation of dinucleoside polyphosphates by RNA polymerase as noncanonical initiating nucleotides. However, how these compounds bind into the active site of RNA polymerase during transcription initiation is unknown. Here, we explored transcription initiation in vitro, using a series of DNA templates in combination with dinucleoside polyphosphates and model RNA polymerase from Thermus thermophilus. We observed that the transcription start site can vary on the basis of the compatibility of the specific template and dinucleoside polyphosphate. Cryo-electron microscopy structures of transcription initiation complexes with dinucleoside polyphosphates revealed that both nucleobase moieties can pair with the DNA template. The first encoded nucleotide pairs in a canonical Watson-Crick manner, whereas the second nucleobase pairs noncanonically in a reverse Watson-Crick manner. Our work provides a structural explanation of how dinucleoside polyphosphates initiate RNA transcription.","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"4 1","pages":""},"PeriodicalIF":14.8,"publicationDate":"2026-01-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145937895","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 : 2026-01-08DOI: 10.1038/s41589-025-02099-5
F. Wieland Goetzke, Steffen M. Bernard, Cheng-Wei Ju, Jonathan Pollock, Kristen E. DeMeester, Jacob Gross, Gabriel M. Simon, Chuan He, Bruno Melillo, Benjamin F. Cravatt
Adaptors serve as hubs to regulate diverse protein complexes in cells. This multitude of functions can complicate the study of adaptors, as their genetic disruption may simultaneously impair the activities of several compositionally distinct complexes (or adaptor ‘complexoforms’). Here we describe the chemical proteomic discovery of bicyclopyrrolidine acrylamide stereoprobes that react with C100 of the methyltransferase (MT) adaptor TRMT112 in human cells. Curiously, the stereoprobes showed negligible reactivity with uncomplexed recombinant TRMT112 and we found that this interaction was restored exclusively in the presence of METTL5 but not other MTs. A cocrystal structure revealed stereoprobe binding to a composite pocket proximal to C100 of TRMT112 that is templated by METTL5 and absent in other TRMT112:MT complexes. Structural rearrangements promoted by stereoprobe binding in turn lead to allosteric agonism of METTL5, thus revealing how covalent ligands targeting a pleiotropic adaptor can confer partner-specific functional effects through reactivity with a single complexoform.
{"title":"Complexoform-restricted covalent TRMT112 ligands that allosterically agonize METTL5","authors":"F. Wieland Goetzke, Steffen M. Bernard, Cheng-Wei Ju, Jonathan Pollock, Kristen E. DeMeester, Jacob Gross, Gabriel M. Simon, Chuan He, Bruno Melillo, Benjamin F. Cravatt","doi":"10.1038/s41589-025-02099-5","DOIUrl":"https://doi.org/10.1038/s41589-025-02099-5","url":null,"abstract":"Adaptors serve as hubs to regulate diverse protein complexes in cells. This multitude of functions can complicate the study of adaptors, as their genetic disruption may simultaneously impair the activities of several compositionally distinct complexes (or adaptor ‘complexoforms’). Here we describe the chemical proteomic discovery of bicyclopyrrolidine acrylamide stereoprobes that react with C100 of the methyltransferase (MT) adaptor TRMT112 in human cells. Curiously, the stereoprobes showed negligible reactivity with uncomplexed recombinant TRMT112 and we found that this interaction was restored exclusively in the presence of METTL5 but not other MTs. A cocrystal structure revealed stereoprobe binding to a composite pocket proximal to C100 of TRMT112 that is templated by METTL5 and absent in other TRMT112:MT complexes. Structural rearrangements promoted by stereoprobe binding in turn lead to allosteric agonism of METTL5, thus revealing how covalent ligands targeting a pleiotropic adaptor can confer partner-specific functional effects through reactivity with a single complexoform.","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"84 1","pages":""},"PeriodicalIF":14.8,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145919888","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 : 2026-01-07DOI: 10.1038/s41589-025-02104-x
Reika Tei, Xiang-Ling Li, Lin Luan, Jeremy M. Baskin
{"title":"Membrane editing with proximity labeling reveals regulators of lipid homeostasis","authors":"Reika Tei, Xiang-Ling Li, Lin Luan, Jeremy M. Baskin","doi":"10.1038/s41589-025-02104-x","DOIUrl":"https://doi.org/10.1038/s41589-025-02104-x","url":null,"abstract":"","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"103 1","pages":""},"PeriodicalIF":14.8,"publicationDate":"2026-01-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145908187","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 : 2026-01-07DOI: 10.1038/s41589-025-02124-7
Esau L. Medina, Victoria A. Maola, Mohammad Hajjar, Grace K. Ko, Ethan J. Ho, Alexandria R. Horton, Nicholas Chim, John C. Chaput
{"title":"Rapid evolution of a highly efficient RNA polymerase by homologous recombination","authors":"Esau L. Medina, Victoria A. Maola, Mohammad Hajjar, Grace K. Ko, Ethan J. Ho, Alexandria R. Horton, Nicholas Chim, John C. Chaput","doi":"10.1038/s41589-025-02124-7","DOIUrl":"https://doi.org/10.1038/s41589-025-02124-7","url":null,"abstract":"","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"29 1","pages":""},"PeriodicalIF":14.8,"publicationDate":"2026-01-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145908186","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 : 2026-01-07DOI: 10.1038/s41589-025-02105-w
Damian L. Ludig, Xiaoxin Zhai, Alexander Rittner, Christian Gusenda, Maximilian Heinz, Svenja Berlage, Ning Gao, Adrian J. Jervis, Yongjin J. Zhou, Martin Grininger
Metazoan fatty acid (FA) synthases (mFASs) facilitate the de novo synthesis of C16- and C18-FAs through iterative extensions within the FA cycle and hydrolytic release. Here we re-engineer mFAS to fine-tune the interplay between FA extension and FA hydrolytic release for the targeted production of short- and medium-chain fatty acids. Single amino acid exchanges in the ketosynthase domain can redirect FA product profiles from predominantly C8 (G113W) to C8/C10 (G113F) and C12/C14 (G113M). Integration of a thioreductase domain enables the production of medium-chain fatty aldehydes and alcohols. We apply our approach for controlling chain length in FA biosynthesis to the microbial production of C10- and C12-FAs, translate it into a yeast cell factory and achieve C10/C12-FAs titers of 674 mg l −1 and 67% purity of total free FAs. Our work demonstrates a modular platform for programmable FA synthesis and paves the way toward sustainable bioproduction of valuable oleochemicals.
后生动物脂肪酸（FA）合成酶（mFASs）通过FA循环内的迭代延伸和水解释放促进C16-和C18-FAs的重新合成。在这里，我们重新设计了mFAS，以微调FA延伸和FA水解释放之间的相互作用，以实现短链和中链脂肪酸的目标生产。酮合酶结构域的单氨基酸交换可以将FA产物谱从主要的C8 （G113W）重定向到C8/C10 （G113F）和C12/C14 （G113M）。硫还原酶结构域的整合使中链脂肪醛和醇的生产成为可能。我们将控制FA生物合成链长度的方法应用于微生物生产C10-和C12-FAs，并将其转化为酵母细胞工厂，实现了C10/C12-FAs滴度为674 mg l - 1，总游离FAs纯度为67%。我们的工作展示了一个可编程FA合成的模块化平台，为有价值的油脂化学品的可持续生物生产铺平了道路。
{"title":"Engineering metazoan fatty acid synthase to control chain length applied in yeast","authors":"Damian L. Ludig, Xiaoxin Zhai, Alexander Rittner, Christian Gusenda, Maximilian Heinz, Svenja Berlage, Ning Gao, Adrian J. Jervis, Yongjin J. Zhou, Martin Grininger","doi":"10.1038/s41589-025-02105-w","DOIUrl":"https://doi.org/10.1038/s41589-025-02105-w","url":null,"abstract":"Metazoan fatty acid (FA) synthases (mFASs) facilitate the de novo synthesis of C16- and C18-FAs through iterative extensions within the FA cycle and hydrolytic release. Here we re-engineer mFAS to fine-tune the interplay between FA extension and FA hydrolytic release for the targeted production of short- and medium-chain fatty acids. Single amino acid exchanges in the ketosynthase domain can redirect FA product profiles from predominantly C8 (G113W) to C8/C10 (G113F) and C12/C14 (G113M). Integration of a thioreductase domain enables the production of medium-chain fatty aldehydes and alcohols. We apply our approach for controlling chain length in FA biosynthesis to the microbial production of C10- and C12-FAs, translate it into a yeast cell factory and achieve C10/C12-FAs titers of 674 mg l <jats:sup>−1</jats:sup> and 67% purity of total free FAs. Our work demonstrates a modular platform for programmable FA synthesis and paves the way toward sustainable bioproduction of valuable oleochemicals.","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"30 1","pages":""},"PeriodicalIF":14.8,"publicationDate":"2026-01-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145908189","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 : 2026-01-06DOI: 10.1038/s41589-025-02103-y
Jacob L. Capener, Martin P. Schwalm, James D. Vasta, Ani Michaud, Kelly A. Teske, William M. Marsiglia, Kilian V. M. Huber, Arvin C. Dar, Stefan Knapp, Alison D. Axtman, Matthew B. Robers
{"title":"Advances in BRET probes for intracellular target engagement studies","authors":"Jacob L. Capener, Martin P. Schwalm, James D. Vasta, Ani Michaud, Kelly A. Teske, William M. Marsiglia, Kilian V. M. Huber, Arvin C. Dar, Stefan Knapp, Alison D. Axtman, Matthew B. Robers","doi":"10.1038/s41589-025-02103-y","DOIUrl":"https://doi.org/10.1038/s41589-025-02103-y","url":null,"abstract":"","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"21 1","pages":""},"PeriodicalIF":14.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145903518","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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