ACS Chemical Biology最新文献

{"title":"Thioester Bond Formation Catalyzed by CalO4: A β-Ketoacyl-ACP Synthase III-like Acyltransferase in Calicheamicin Biosynthesis","authors":"Fang Pang,&nbsp;Yu-Ju Peng,&nbsp;Srinivas Thadkapally,&nbsp;Craig A. Townsend","doi":"10.1021/acschembio.6c00389","DOIUrl":"10.1021/acschembio.6c00389","url":null,"abstract":"<p>β-Ketoacyl-ACP synthase (KAS) III enzymes play central roles in fatty acid biosynthesis and the production of various natural products. While their canonical function involves catalyzing C–C bond formation between acetyl-CoA and malonyl acyl-carrier-proteins (ACPs), an increasing number of non-canonical activities have been reported among KAS III homologues, including C–O and C–N bond formation. Here, we describe a KAS III family enzyme, CalO4, that catalyzes C–S bond formation during the biosynthesis of the potent antitumor agent calicheamicin. We successfully reconstituted its transacylation activities, demonstrated C–S bond formation, and assessed its substrate selectivity. Furthermore, X-ray crystallography combined with molecular docking and mutational analysis identified key residues likely involved in substrate selection and catalysis. This work not only expands the functional diversity of the KAS III family but also provides a potential biocatalyst for hindered C–S bond formation and a target for engineering novel calicheamicin-like or other bioactive compounds.</p>","PeriodicalId":11,"journal":{"name":"ACS Chemical Biology","volume":"21 9","pages":"2224–2231"},"PeriodicalIF":3.6,"publicationDate":"2026-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148785342","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mitochondrial Lipids in Cellular Adaptation","authors":"Mária Balážová,&nbsp;Lili Jiang,&nbsp;Cunqi Ye","doi":"10.1021/acschembio.6c00615","DOIUrl":"10.1021/acschembio.6c00615","url":null,"abstract":"<p>Mitochondria serve as central hubs of cellular bioenergetics and signaling, yet the dynamic role of their lipid composition in cellular adaptation remains underappreciated. Unlike most organelles, mitochondria possess a unique dual-bilayer membrane architecture shaped by lipid transport and de novo synthesis. The mitochondrial lipidome, dominated by phosphatidylcholine, phosphatidylethanolamine, and the signature phospholipid cardiolipin, influences cristae organization, oxidative phosphorylation capacity, and metabolite transport, collectively determining whether mitochondria undergo stabilization, remodeling, or degradation. In this review, we explore how mitochondrial lipid dynamics sustain organelle-wide homeostasis while coordinating cellular adaptation across multiple temporal scales and how failure of lipid homeostasis drives rare monogenic disorders and complex pathologies. We propose that environmental shifts transiently disrupt the balance between phospholipid biosynthesis and utilization, generating changes in mitochondrial lipid homeostasis that promote cellular adaptation through complementary biophysical and biochemical signaling mechanisms. Specifically, membrane lipid remodeling rapidly alters membrane biophysical properties to regulate membrane protein activity, whereas bioactive phospholipid intermediates and side-products support long-term adaptive reprogramming. Mitochondrial lipids therefore function not merely as passive structural components but as active regulatory nodes that drive cellular plasticity, positioning lipid dynamics at the nexus of metabolic adaptation and human disease.</p>","PeriodicalId":11,"journal":{"name":"ACS Chemical Biology","volume":"21 9","pages":"2097–2111"},"PeriodicalIF":3.6,"publicationDate":"2026-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148862609","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of Collimonin Biosynthesis in the Fungus-Feeding Bacterium Collimonas fungivorans Ter331","authors":"Naoka Katayama,&nbsp;Kotone Kume,&nbsp;Rina Terada,&nbsp;Tatsuya Goi,&nbsp;Kenji Kai","doi":"10.1021/acschembio.6c00065","DOIUrl":"https://doi.org/10.1021/acschembio.6c00065","url":null,"abstract":"<p>Collimonins A–D are bacterial polyynes produced by the fungus-feeding bacterium <em>Collimonas fungivorans</em> Ter331. The <em>col</em> biosynthetic gene cluster (BGC) is implicated in collimonin biosynthesis, but their gene functions remain unclear. In this study, the biosynthetic pathway of collimonins in <em>C. fungivorans</em> Ter331 was elucidated through genetic and chemical characterization of each <em>col</em> gene’s function. The biosynthetic intermediates (namely, CBIs-1–4) were isolated from gene-deletion mutants (or with gene overexpression), and their structures were elucidated by spectroscopic analyses. The conversion of these intermediates to other intermediates or collimonins was analyzed by mutant coculturing, gene overexpression, and feeding experiments. CBI-1, which is the first detectable intermediate, was converted into collimonins A–D through desaturation, oxidation, and lactonization. Results indicated that the Rieske oxygenase ColK, the fatty acid desaturase ColJ, the possible cyclase ColM, and the flavin-dependent monooxygenase ColI were involved in the conversion of CBI-1 to collimonins A and B, whereas only ColK was responsible for its conversion to collimonins C and D. The <em>mas</em> BGC of <em>Massilia armeniaca</em> ZMN-3, which has a similar gene set to the <em>col</em> BGC but lacks a homologue of <em>colI</em>, can produce collimonins A–D when coexpressed with <em>colI</em>. A comparison of the antifungal activity between Ter331 and its <em>col</em> mutants suggested the importance of the latter lactonization in collimonin biosynthesis for the activity. This study represents the first comprehensive description of the biosynthetic pathway for collimonins and establishes an important basis for future biochemical analyses of each conversion step.</p>","PeriodicalId":11,"journal":{"name":"ACS Chemical Biology","volume":"21 9","pages":"2143–2156"},"PeriodicalIF":3.6,"publicationDate":"2026-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148985187","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Substrate Mimicry by Inhibitors of the Mycobacterium tuberculosis 20S Proteasome and Their Activity against Mycobacteria In Vitro and in Macrophages","authors":"Xilin Gu,&nbsp;Peter J. Rowheder,&nbsp;Zanlin Yu,&nbsp;Alexander Mohapatra,&nbsp;Shichun Lun,&nbsp;Xiuju Jiang,&nbsp;Daqiang Li,&nbsp;Nicholas L. Yan,&nbsp;Tyler C. Detomasi,&nbsp;Daniel F. Torres Pomares,&nbsp;Yifei Chen,&nbsp;Jason E. Gestwicki,&nbsp;Gang Lin,&nbsp;William R. Bishai,&nbsp;Joel D. Ernst,&nbsp;Yifan Cheng,&nbsp;Charles S. Craik,&nbsp;Jason K. Sello","doi":"10.1021/acschembio.6c00448","DOIUrl":"https://doi.org/10.1021/acschembio.6c00448","url":null,"abstract":"<p>The remarkable and problematic capacity of <em><em>Mycobacterium tuberculosis</em></em> to persist in the host is dependent on a functional 20S proteasome that is structurally and functionally analogous to its mammalian counterpart. It has been proposed that this enzyme is critical for the bacterium’s adaptive response to a variety of stressors in the host. Here, we report the structure of a rationally designed and species-selective inhibitor of the <em>Mtb</em> 20S proteasome in complex with the enzyme. The inhibitor was inspired by the syringolin natural products—covalent proteasome inhibitors that mimic a substrate. Structure elucidation of the <em>Mtb</em> 20S proteasome-inhibitor adduct via cryo-electron microscopy revealed that the inhibitor mimics a substrate yet engages the active site in a different fashion than the syringolin natural products. Corroboration of this model via the synthesis of hypothetical inhibitors led to the discovery of a more potent inhibitor, as evidenced in kinetic assays for enzyme inhibition. Both inhibitors are permeable to and active in <em><em>M. tuberculosis</em></em>. They sensitize the bacterium to chemically and pharmacologically induced nitrosative stress <em>in vitro</em>. Importantly, they suppress the persistence of live mycobacteria in murine and human macrophages.</p>","PeriodicalId":11,"journal":{"name":"ACS Chemical Biology","volume":"21 9","pages":"2275–2285"},"PeriodicalIF":3.6,"publicationDate":"2026-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148985189","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Copper Nanoparticles Enable Multi-Compartment Cuproenzyme Metalation in Cellular Models of Copper Deficiency","authors":"Harman Kaur,&nbsp;John Soukar,&nbsp;Nikita Gudekar,&nbsp;Vinit C. Shanbhag,&nbsp;Michael J. Petris,&nbsp;Akhilesh K. Gaharwar,&nbsp;Vishal M. Gohil","doi":"10.1021/acschembio.6c00564","DOIUrl":"https://doi.org/10.1021/acschembio.6c00564","url":null,"abstract":"<p>Copper (Cu) is an essential trace element that serves as a cofactor for enzymes involved in diverse metabolic pathways and processes across multiple subcellular compartments. Mutations that cause systemic or subcellular Cu deficiency result in fatal pediatric disorders, including Menkes disease and related mitochondrial disorders. Treatment of these disorders requires pharmacological agents that can transport Cu across membranes; however, the only approved drug, Cu histidinate, shows limited efficacy. Using genetic models of Menkes disease, we recently demonstrated that the Cu ionophore elesclomol (ES) efficiently restores the activity of mitochondrial and cytosolic cuproenzymes, but its ability to metalate cuproenzymes within secretory compartments is low. To overcome this limitation, we investigated Cu nanoparticles (Cu-NPs) as a facile means of delivering Cu to multiple subcellular compartments simultaneously. Cu-NPs were synthesized by chemical reduction to produce spherical nanoparticles with an average size of 80 nm. Biophysical characterization of Cu-NPs revealed zero-valent Cu and a neutral zeta potential, compatible with biological interactions and in vivo circulation. In cellular models of Cu deficiency, Cu-NPs were shown to internalize via clathrin-mediated endocytosis and restore the activity of cuproenzymes in mitochondrial, cytosolic, and secretory compartments. Importantly, biomarkers of Cu toxicity were not activated under these conditions, indicating a favorable therapeutic index. Overall, these findings highlight Cu-NPs as versatile Cu delivery agents with therapeutic potential for Cu deficiency disorders.</p>","PeriodicalId":11,"journal":{"name":"ACS Chemical Biology","volume":"21 9","pages":"2441–2450"},"PeriodicalIF":3.6,"publicationDate":"2026-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148985191","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Systematic Virtual Screening of Heparan Sulfate Oligosaccharides and Mechanistic Insights into Heparanase Inhibition","authors":"Binjie Li,&nbsp;Siran Zhao,&nbsp;Zonglin Lan,&nbsp;Marco Maccarana,&nbsp;Xiao Zhang,&nbsp;Vito Ferro,&nbsp;Hui Cao,&nbsp;Tianji Zhang,&nbsp;Mingjia Yu,&nbsp;Jin-Ping Li","doi":"10.1021/acschembio.6c00454","DOIUrl":"https://doi.org/10.1021/acschembio.6c00454","url":null,"abstract":"<p>Heparanase (Hpse) is an endo-β-glucuronidase that specifically cleaves heparan sulfate (HS) and plays critical roles in the pathogenesis of multiple diseases, making it a well-validated therapeutic target. To identify novel Hpse inhibitors, we developed a rule-based computational pipeline to construct a rigorously curated database of HS oligosaccharides ranging from disaccharides to hexasaccharides. This database systematically encompasses all possible sulfation patterns and stereochemical configurations of the three monosaccharide species in HS. Using a multistage virtual screening strategy against Hpse, we prioritized high-affinity HS oligosaccharides for detailed analysis. Structural motif profiling of the top-ranking candidates revealed that even-numbered oligosaccharides preferentially retain the iduronic acid (IdoA)-<em>N</em>-acetyl-3-<em>O</em>-sulfated glucosamine (GlcNAc3S) motif, whereas odd-numbered species are enriched with IdoA2S and 3,6-<em>O</em>-sulfated glucosamine (GlcN3S6S) motifs. Systematic desulfation of the lead compound, HP-dp5R1, found that removal of 2-<em>O</em>- or 3-<em>O</em>-sulfate groups resulted in substantially larger penalties to binding-free energy compared with removal of 6-<em>O</em>- or <em>N</em>-sulfates, indicating a dominant role for 2-<em>O</em>/3-<em>O</em> sulfation in Hpse recognition. Molecular dynamics simulations and binding-free energy calculations further revealed that longer oligosaccharides form extensive interactions with the heparin-binding domains (HBD1 and HBD2) flanking the catalytic cleft, leading to reduced conformational fluctuation. Together with preliminary experimental results using selected octasaccharides that resemble the structural features of the top-hit oligosaccharides identified from virtual screening, we demonstrate that the integrated computational platform provides a robust foundation for the rational design of HS-based Hpse inhibitors. More broadly, the virtual HS oligosaccharide database described here is expected to serve as a powerful resource for screening other HS-binding proteins and for the discovery of novel agonists or antagonists.</p>","PeriodicalId":11,"journal":{"name":"ACS Chemical Biology","volume":"21 9","pages":"2286–2297"},"PeriodicalIF":3.6,"publicationDate":"2026-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148985218","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bacterial Display of Genetically Encoded Macrocyclic Peptide Libraries Using Cysteine-Reactive Unnatural Amino Acids","authors":"Olabode Dawodu,&nbsp;Jeffery M. Tharp","doi":"10.1021/acschembio.6c00634","DOIUrl":"https://doi.org/10.1021/acschembio.6c00634","url":null,"abstract":"<p>Cyclic peptides are powerful scaffolds for modulating protein–protein interactions; however, methods for constructing cyclic peptide libraries for cell-surface display applications remain limited. Here, we present a bacterial surface display platform that enables site-specific incorporation of diverse unnatural amino acids (uAAs) into peptides displayed on the surface of <em>Escherichia coli</em>. These uAAs include several cysteine-reactive residues that undergo spontaneous intramolecular reactions with cysteine to generate macrocyclic peptides directly on the bacterial outer membrane. Using high-resolution mass spectrometry, we show that peptide cyclization proceeds efficiently and selectively with no detectable off-target reactions. Further, we demonstrate that this platform supports simultaneous incorporation of two distinct uAAs, enabling the surface display of chemically diverse, drug-like macrocycles. To demonstrate the utility of this platform, we constructed and screened a naïve macrocyclic peptide library against a model target, yielding de novo ligands with conserved sequence motifs and binding affinities similar to those previously identified by phage display. Together, these results establish a robust approach for generating diverse cyclic peptide libraries, thereby expanding the scope of cell-surface display for research and drug discovery.</p>","PeriodicalId":11,"journal":{"name":"ACS Chemical Biology","volume":"21 9","pages":"2488–2503"},"PeriodicalIF":3.6,"publicationDate":"2026-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148985220","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"m6A-ARTR-DBiT for Spatial Mapping of m6A Epitranscriptome","authors":"Kun Xu,&nbsp;Xiang Huan,&nbsp;Yu Xiao","doi":"10.1021/acschembio.6c00603","DOIUrl":"10.1021/acschembio.6c00603","url":null,"abstract":"<p><em>N</em>⁶-methyladenosine (m⁶A) is a widespread RNA modification that regulates RNA metabolism and gene expression, yet most sequencing methods rely on isolated RNA and therefore lose its spatial context. This In Focus article surveys methodological advances in transcriptome-wide m⁶A detection and highlights m⁶A-ARTR-DBiT, a spatial m⁶A profiling assay that leverages reverse-transcription-based detection and deterministic barcoding in tissue to map transcriptome-wide m⁶A distribution while preserving native tissue context. This platform enables researchers to investigate how m⁶A patterns vary across distinct tissue regions, developmental structures, and local gene regulatory networks, bridging the gap between spatially patterned epitranscriptomic deposition and gene regulation.</p>","PeriodicalId":11,"journal":{"name":"ACS Chemical Biology","volume":"21 9","pages":"2093–2096"},"PeriodicalIF":3.6,"publicationDate":"2026-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148878643","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Novel Class I HDAC Inhibitors Sensitize Ovarian Cancer Cells for Cisplatin and Niraparib via an HDAC3-SLFN11 Axis","authors":"Julia M. Eichhorn,&nbsp;Jasmin Menning,&nbsp;Linda Schäker-Hübner,&nbsp;Finn K. Hansen,&nbsp;Philipp König,&nbsp;Gerd Bendas","doi":"10.1021/acschembio.6c00312","DOIUrl":"10.1021/acschembio.6c00312","url":null,"abstract":"<p>The DNA/RNA helicase Schlafen11 (SLFN11) is considered a sensitivity marker of various tumor cells for cytotoxic treatment with DNA damaging agents (DDA), such as cisplatin and PARP inhibitors (PARPi). Cells can epigenetically silence SLFN11 expression to gain chemoresistance, which can be targeted by HDAC inhibitors (HDACi). Here, we investigate the predictive value of SLFN11 expression for the response to three different PARPi in ovarian cancer cells. Furthermore, we target its epigenetic downregulation via HDACi for sensitization to cisplatin and PARPi. We show that HDAC3 plays a key role in SLFN11 silencing in W1 and W1CR ovarian cancer cells, confirmed by an HDAC3 knockdown approach. Therefore, addressing HDAC3 by novel class I HDACi <em>DS-103</em> and <em>FL-007</em> at non-toxic concentrations restored SLFN11 expression with various consequences for DDA treatment in W1, W1CR, and SKOV-3 cells. While <em>DS-103</em> and <em>FL-007</em> significantly sensitized cisplatin-resistant W1CR cells to cisplatin to the level of W1 cells, the response to various PARPi remains divergent. Whereas both HDACi induced significant sensitization in W1 and W1CR cells, and <em>DS-103</em> in SKOV-3 cells for niraparib cytotoxicity, cells remain unaffected in response to olaparib and rucaparib. Both compounds were also shown to be less dependent on, or independent of, SLFN11 in different ovarian cancer cells. In sum, the first time reported functional link of HDAC3 and SLFN11 appears an attractive co-treatment opportunity of DDA with HDACi. This is particularly promising for niraparib as it has a broader approval independent of BRCA status compared to other PARPi.</p>","PeriodicalId":11,"journal":{"name":"ACS Chemical Biology","volume":"21 9","pages":"2169–2178"},"PeriodicalIF":3.6,"publicationDate":"2026-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148785411","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Deubiquitinase-Targeting Chimera (DUBTAC)-Enhanced Mammalian Expression System for Efficient Recombinant Protein Expression","authors":"Ruhu Zheng,&nbsp;Xuan Zhao,&nbsp;Qiushuang Zhang,&nbsp;Yicong Dai,&nbsp;Xucong Teng,&nbsp;Jinghong Li","doi":"10.1021/acschembio.6c00465","DOIUrl":"https://doi.org/10.1021/acschembio.6c00465","url":null,"abstract":"<p>Overexpression of exogenous proteins in mammalian cells frequently saturates the endogenous folding and quality control machinery, resulting in their recognition as misfolded substrates, subsequent polyubiquitination, and rapid degradation by the 26S proteasome. This cellular bottleneck directly constrains recombinant protein yields and remains a major challenge in biopharmaceutical production. To address this limitation, we developed a deubiquitinase-targeting chimera (DUBTAC)-enhanced mammalian expression system designed to selectively stabilize recombinant proteins. In this platform, the target protein is genetically fused to cellular retinoic acid-binding protein 1 (CRABP1), while a SNAP-tagged deubiquitinase (UCHL1-SNAP) is co-expressed. Upon administration of the heterobifunctional small molecule BG-ATRA, which simultaneously engages the SNAP tag and CRABP1, the deubiquitinase is recruited in proximity to the target protein. This induced proximity enables the enzymatic removal of degradation-linked ubiquitin chains, thereby shielding the recombinant protein from proteasomal destruction and extending its intracellular half-life. We demonstrated that this system significantly increased the yields of three structurally and functionally diverse recombinant proteins─thrombopoietin (TPO), osteoprotegerin (OPG), and vitronectin (VN)─by 2.6- to 3.1-fold in HEK293F suspension cells. Importantly, the enhanced production was achieved without compromising the biological activity of the purified proteins. This DUBTAC-based approach thus offers a robust, generalizable platform for boosting recombinant protein production in mammalian expression systems.</p>","PeriodicalId":11,"journal":{"name":"ACS Chemical Biology","volume":"21 9","pages":"2298–2305"},"PeriodicalIF":3.6,"publicationDate":"2026-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148980746","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}