Biochemical Journal最新文献

{"title":"Nuclear Translocation of Mitochondrial Ferredoxin Reductase Is Regulated by AKT-Mediated Phosphorylation.","authors":"Jin Zhang,Ken-Ichi Nakajima,Shakur Mohibi,Xinbin Chen","doi":"10.1042/bcj20250303","DOIUrl":"https://doi.org/10.1042/bcj20250303","url":null,"abstract":"Ferredoxin reductase (FDXR) is the sole ferredoxin reductase in humans and plays an essential role for steroidogenesis and biosynthesis of heme and iron sulfur cluster (ISC) by transferring electrons from NADPH to ISC-containing ferredoxin 1 (FDX1) and FDX2. In this study, we found that while FDXR is classified as a mitochondria-localized flavoprotein, it can be translocated into the nucleus, especially in response to various stress signals. Next, we identified a bipartite NLS within amino acids 271-299 of FDXR, the disruption of which impairs its nuclear translocation. Further, we found that AKT can phosphorylate threonine 277 adjacent to the NLS in FDXR and subsequently enhances its nuclear translocation. Consistent with this, mutant FDXR(T277A), in which threonine 277 was substituted with alanine, impaired FDXR nuclear translocation. Together, our data provide evidence that the mitochondrial FDXR can be translocated to the nucleus, which is regulated by AKT-mediated phosphorylation, especially in response to cellular stress. Our data suggest that FDXR plays a role in the mitochondria-nucleus communication and stress responses.","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"27 1","pages":""},"PeriodicalIF":4.1,"publicationDate":"2026-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147483632","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Modulating backbone flexibility in hydroxamate siderophores for improved iron chelation and peptide nucleic acid (PNA) delivery into bacteria.","authors":"Uladzislava Tsylents,Piotr Maj,Mateusz Wdowiak,Jan Stadnicki,Adam Mieczkowski,Monika Wojciechowska,Joanna Trylska","doi":"10.1042/bcj20253458","DOIUrl":"https://doi.org/10.1042/bcj20253458","url":null,"abstract":"The development of effective delivery systems for peptide nucleic acids (PNAs) into bacterial cells remains a critical challenge in antisense therapeutics. We report the design and evaluation of hydroxamate siderophore-PNA conjugates that exploit bacterial iron uptake pathways for targeted delivery. We demonstrate that modulating the backbone flexibility of hydroxamate siderophores, through glycine or alanine spacers, enhances iron(III) binding affinity and PNA delivery efficiency into Escherichia coli cells. Molecular dynamics simulations revealed that glycine insertion increases backbone flexibility, enabling optimal coordination of all three hydroxamate groups to iron(III). Circular dichroism spectroscopy and iron(III) competition assays confirmed that the siderophores form stable Λ-configured ferric complexes, with the flexible siderophore showing superior iron(III)-binding affinity compared to the less flexible analog. Growth recovery experiments using E. coli mutants deficient in several transporters indicated recognition and internalization of the siderophores via the TonB-dependent hydroxamate pathway. Molecular docking demonstrated the affinity of these siderophores for E. coli hydroxamate receptors, with binding scores comparable to those of natural siderophores. All three siderophore carriers successfully delivered functional PNA targeting the mrfp reporter gene into bacterial cells, achieving sequence-specific gene silencing as confirmed by fluorescence measurements and confocal microscopy. Additionally, bacteriostatic activity was observed for the best-performing siderophore mimic conjugated with a PNA targeting the essential acpP gene.","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"119 1","pages":""},"PeriodicalIF":4.1,"publicationDate":"2026-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147471648","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Inducing TRIB2 Targeted Protein Degradation to Reverse Chemoresistance in Acute Myeloid Leukaemia.","authors":"Evie Rigby,Francesca Fasanella Masci,Akshara Narayanan,Elzbieta Kania,John A Harris,Jamie Williams,Binghua Zhang,Lijun Liu,Laura Richmond,Fengtao Zhou,Ke Ding,Ruaidhrí J Carmody,Patrick A Eyers,Karen Keeshan","doi":"10.1042/bcj20253463","DOIUrl":"https://doi.org/10.1042/bcj20253463","url":null,"abstract":"The myeloid oncogene TRIB2 is a key driver of acute myeloid leukaemia (AML) pathogenesis, promoting chemoresistance and blocking differentiation through ubiquitin-mediated degradation of the C/EBPα transcription factor. Despite its stable and sometimes elevated expression across AML subtypes, TRIB2 remains a clinically-untargeted vulnerability. Here, we present a comprehensive investigation into TRIB2 degradation mechanisms using multimodal approaches, including CRISPR knockout, mutational protein stability, small molecule TRIB2 engagement and evaluation of a novel targeted protein degrader (TRIB2-PROTAC). We identify Afatinib, a multi-ERBB covalent inhibitor, as a rapid inducer of TRIB2 degradation, triggering AML cell death potentially via signalling pathways distinct from ERBB. Importantly, TRIB2 degradation synergized with cytarabine, the frontline AML chemotherapy, amplifying therapeutic efficacy. Mapping of TRIB2 ubiquitination sites revealed Lys-63 as critical for its own proteolytic turnover, and a Lys to Arg degradation-resistant mutant (KallR) conferred enhanced chemoresistance and increased leukaemic engraftment in vivo. CRISPR-mediated TRIB2 knockout validated an essential role in AML cell survival. Consistently, the novel TRIB2-PROTAC (compound 5K) achieved robust TRIB2 degradation and AML cell killing at low micromolar concentrations. These findings establish TRIB2 as a compelling therapeutic target in AML and demonstrate that leveraging the ubiquitin-proteasome system to degrade TRIB2 offers a promising strategy to overcome chemoresistance. This work provides strong preclinical rationale for the development of TRIB2-targeting therapies in AML.","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"26 1","pages":""},"PeriodicalIF":4.1,"publicationDate":"2026-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147439570","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Modulation of Ube2R1 activity by a nanobody that binds near its N-terminus.","authors":"Charlotte Wijne, Pavana Suresh, Richard Dela Rosa, Luc van Oss, Sabine Normann, William McKibben, Florian I Schmidt, Hidde Ploegh","doi":"10.1042/BCJ20250271","DOIUrl":"10.1042/BCJ20250271","url":null,"abstract":"<p><p>Ube2R1 (Cdc34) is a K48-ubiquitin chain-specific ubiquitin-conjugating (E2) enzyme central to proteasomal degradation, yet the regulatory potential of its unique structural elements remains underexplored. Here, we report the isolation and biochemical characterization of a nanobody, VHH12R1, that binds selectively to the N-terminal extension of Ube2R1 with no detectable cross-reactivity to its paralog Ube2R2 or other E2s. Engagement of this N-terminal region by VHH12R1 transiently delays ubiquitin charging, promotes accumulation of stable mono-ubiquitin Ube2R1 conjugates, and markedly reduces self-directed polyubiquitination chain formation by Ube2R1 without impairing di-ubiquitin synthesis. Although Ube2R1 can catalyze ubiquitination of VHH12R1 in the absence of an E3 ligase, this modification occurs independently of stable nanobody binding and is not required for modulation of Ube2R1 activity. Together, these findings support a model in which VHH12R1 selectively restricts processive self-elongation by Ube2R1 through engagement of its N-terminal extension, without broadly inhibiting ubiquitin transfer reactions. Our results reveal an unappreciates regulatory role for the Ube2R1 N-terminus in controlling catalytic outcomes and highlight nanobody-based approaches as precise tools to dissect E2 enzyme function.</p>","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"483 3","pages":"345-363"},"PeriodicalIF":3.9,"publicationDate":"2026-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146217928","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Post-translational modifications of triosephosphate isomerase reveal metabolic vulnerabilities in T-ALL: effect of combining dichloroacetic acid and the PPI rabeprazole.","authors":"Yoalli Martínez-Pérez, Ignacio De la Mora-De la Mora, Gloria Hernández-Alcántara, Gabriela López-Herrera, Itzhel García-Torres, Saúl Gómez-Manzo, Alberto Olaya-Vargas, Gloria León-Avila, José Manuel Hernández-Hernandez, Fernando González-Rubio, C Yusiel Flores-Braulio, Luis A Flores-López, Sergio Enríquez-Flores","doi":"10.1042/BCJ20253451","DOIUrl":"10.1042/BCJ20253451","url":null,"abstract":"<p><p>Acute lymphoblastic leukemia, particularly the T-cell subtype, remains associated with poor outcomes in relapsed and adult patients, highlighting the need for novel therapeutic strategies. Metabolic reprogramming, especially glycolytic dependence, represents a promising target. Triosephosphate isomerase (TPI), a key glycolytic enzyme, undergoes cancer-associated post-translational modifications (PTMs), including deamidation and phosphorylation. Here, we evaluated the potential of proton pump inhibitors (PPIs), particularly rabeprazole (Rbz), to selectively target PTM-bearing TPI isoforms in Jurkat cell model. Recombinant TPI variants engineered to mimic PTMs exhibited increased reactivity toward thiol-modifying agents and higher predicted binding affinities for PPI compared with wild-type TPI. Consistent with these properties, biochemical assays demonstrated preferential inhibition of the deamidation- and phosphorylation-mimicking proteins, with Rbz significantly reducing their enzymatic activity. Native gel electrophoresis of Jurkat cells protein extracts revealed drug-induced accumulation of acidic TPI isoforms, whereas normal T lymphocytes predominantly retained unmodified TPI. Rbz selectively impaired intracellular TPI activity and viability in Jurkat cells, effects enhanced by dichloroacetate (DCA) co-treatment. This inhibition correlated with marked accumulation of methylglyoxal and advanced glycation end products. Finally, combined DCA-Rbz treatment induced extensive apoptotic death in Jurkat cells while sparing normal lymphocytes. These findings identify PTM-bearing TPI isoforms as selective metabolic vulnerabilities in Jurkat cells and support the potential repurposing of thiol-modifying agents, particularly, Rbz, as targeted antileukemic strategies.</p>","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":" ","pages":"319-344"},"PeriodicalIF":3.9,"publicationDate":"2026-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13094655/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146103675","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural and mechanistic basis of mTORC2 activation of protein kinase AKT/PKB.","authors":"Nam Chu,Nhat Le,Ouada Nebie,Sammi Yang","doi":"10.1042/bcj20253108","DOIUrl":"https://doi.org/10.1042/bcj20253108","url":null,"abstract":"The PI3K/AKT/mTOR signaling pathway is crucial for regulating essential cellular processes such as growth, survival, metabolism, and protein synthesis. Dysregulation of this pathway is strongly associated with diseases like cancer, where it drives uncontrolled cell proliferation and survival. The mTOR kinase forms two multiprotein complexes, mTORC1 and mTORC2, which govern distinct signaling pathways. mTORC1, regulated by nutrients, controls protein synthesis, cell growth, and autophagy, while mTORC2 acts as a central node in phosphoinositide 3-kinase (PI3K) and Ras signaling, often disrupted in cancer and diabetes. AKT, recruited by PIP3 to the plasma membrane, is phosphorylated by PDK1 and mTORC2, enabling it to regulate various cellular functions. Notably, mTORC2 selectively phosphorylates AKT and PKC but no other closely related kinases targeted by mTORC1, reflecting a high degree of substrate specificity. This specificity is due to structural elements in AKT that interact with the mTORC2 subunit mSin1 as revealed by recent studies using semisynthetic probes, paving the way for the design of mTORC2-specific inhibitors. Given the pathway's significant role in disease progression, particularly cancer, targeting the AKT/mTOR axis holds considerable therapeutic promise. However, challenges remain due to the complex regulation and feedback mechanisms in this pathway. Emerging combination therapies show promise in overcoming these obstacles. This review highlights the intricate regulation of the AKT/mTOR pathway and its potential for developing targeted therapies.","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"71 1","pages":"375-389"},"PeriodicalIF":4.1,"publicationDate":"2026-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147329626","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Docking in the Abies grandis abietaenol synthase to investigate the mechanism underlying conifer resin acid diterpene synthase evolution.","authors":"Mark Schmidt-Dannert, Griffin Humphreys, Taylor Eich, Meirong Jia, Reuben J Peters","doi":"10.1042/BCJ20250294","DOIUrl":"10.1042/BCJ20250294","url":null,"abstract":"<p><p>The pine family (Pinaceae) produces oleoresins in which the diterpenoid resin acids contain tricyclic backbones of either the (iso)pimarane and/or rearranged abietane type. These are produced by closely related (class I) diterpene synthases, whose functional divergence is of significant interest, not least for mechanistic insights into the catalyzed complex carbocation-cascade reactions. The abietaenol synthase from Abies grandis (AgAS) has long served as a model for this enzymatic subfamily and was used here to examine key residues potentially involved in transitions from such ancestral activity to production of (iso)pimaradienes, which seems to have occurred independently at least three times in the Pinaceae. While the equivalent substitutions in AgAS led to production of some amount of isopimaradiene(s), based on the transition observed in the most closely related enzymes (i.e., those also from the Abies genus), the threonine substitution for an alanine was most impactful, with the resulting A723T variant producing almost entirely isopimara-7,15-diene. This prompted application of the TerDockin computational approach to investigate the underlying mechanism. Through iterative application, requiring placement and constraint of the reactant water from the native reaction (i.e., that added to yield the 13α-hydroxyl of the primary abietaenol epimer), it was found that the introduced threonine most likely acts directly as a catalytic base to short-circuit the native reaction by deprotonating the initially formed isopimara-13E-en-8-yl carbocation intermediate. These results not only provide mechanistic insight but also have some implications for such modeling of the complex reactions catalyzed by terpene synthases more generally, as discussed herein.</p>","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"483 3","pages":"365-374"},"PeriodicalIF":3.9,"publicationDate":"2026-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13089139/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147275573","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The role of linker length and composition in actin binding and bundling by palladin.","authors":"Rachel A Sargent, Colby W Bradford, Lauren M Hughes, Nathan H Ta, MarcArthur J Limpiado, Ravi Vattepu, Moriah R Beck","doi":"10.1042/BCJ20250187","DOIUrl":"10.1042/BCJ20250187","url":null,"abstract":"<p><p>Interdomain linkers in multidomain proteins influence spatial arrangement, flexibility, and cooperative binding, yet their functional roles remain underexplored. Palladin, an actin scaffold protein essential for cytoskeletal organization, contains tandem immunoglobulin domains (Ig3-4) separated by an unusually long (∼41-residue), arginine-rich, intrinsically disordered linker. While Ig3 mediates direct F-actin binding, the adjacent Ig4 domain and linker enhance binding and bundling, suggesting active roles beyond passive connection. Using targeted mutagenesis, actin co-sedimentation, bundling assays, and SAXS, we show that linker length, charge, and residue patterning are critical for activity. Shortening or replacing the 41-residue linker with the native Ig4-Ig5 linker reduced binding and abolished bundling, while small internal deletions decreased affinity but unexpectedly increased bundling efficiency. Neutralizing basic residues eliminated activity, while scrambling the sequence impaired both functions-demonstrating that electrostatic tuning and residue order, not just net charge, are essential. SAXS revealed that the native linker supports a broad, dynamic interdomain ensemble, enabling multiple binding-competent geometries. Shortened linkers restricted this conformational space, locking domains in extended orientations incompatible with efficient actin engagement. These results establish the Ig3-Ig4 linker as a finely tuned structural and electrostatic module that coordinates domain flexibility and filament crosslinking. More broadly, these findings highlight long, intrinsically disordered linkers as active determinants of cytoskeletal scaffold function, providing a general mechanism for modulating multivalent interactions in actin-binding proteins.</p>","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":" ","pages":"301-318"},"PeriodicalIF":3.9,"publicationDate":"2026-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13137456/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146002922","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural basis for inhibition of SpyCas9 by the anti-CRISPR protein AcrIIA26.","authors":"Iris Zheng, Brian Learn, Scott Bailey","doi":"10.1042/BCJ20250364","DOIUrl":"10.1042/BCJ20250364","url":null,"abstract":"<p><p>CRISPR-Cas9 systems provide adaptive immunity in prokaryotes by targeting and cleaving invading phage DNA. In response, phages have evolved anti-CRISPR (Acr) proteins to inhibit Cas9 and evade this immune response. AcrIIA26 is a type II-A anti-CRISPR protein that inhibits Streptococcus pyogenes Cas9 (SpyCas9) DNA binding, but its molecular mechanism remains unclear. Here, we determined the 3.0 Å resolution cryo-EM structure of AcrIIA26 in complex with SpyCas9-single-guide RNA, revealing a dual inhibition mechanism. AcrIIA26 adopts a novel fold comprising a central β-sheet flanked by two α-helical bundles. The 5-helix bundle, which features a negatively charged surface whose shape mimics duplex DNA, occupies the same position as the protospacer adjacent motif (PAM) duplex in target-bound Cas9. This directly blocks PAM recognition by burying critical residues R1333 and R1335 in the PAM-interacting domain. Mutagenesis confirmed that residues E49 and D50 in AcrIIA26 are essential for this interaction. Simultaneously, the 4-helix bundle binds the Cas9 REC lobe and sterically prevents the conformational changes required for Cas9 activation, with mutation of AcrIIA26 F121 completely eliminating inhibitory activity. Structural comparisons reveal that despite diverse folds, multiple anti-CRISPRs convergently evolved to block PAM recognition, highlighting this as a critical vulnerability in Cas9 function. Our findings provide mechanistic insights into AcrIIA26 inhibition and offer a foundation for engineering improved Cas9 off-switches for genome editing applications.</p>","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":" ","pages":"289-300"},"PeriodicalIF":3.9,"publicationDate":"2026-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13089141/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146003010","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The future of Forkhead box O transcription factors.","authors":"Huanjie Huang, Tianshu Gui, Boudewijn Mt Burgering","doi":"10.1042/BCJ20253428","DOIUrl":"10.1042/BCJ20253428","url":null,"abstract":"<p><p>The Forkhead box O (FOXO) class of transcription factors is evolutionary conserved both structurally and at least in part also functionally. FOXO activation results in transcriptional programs that provide cellular resilience toward exogenous and endogenous challenges, especially challenges that provoke cellular oxidative stress. This FOXO-dependent mechanism of resilience explains by and large the observed longevity phenotype in model organisms where increased FOXO activity extends lifespan. This may even hold for human lifespan as genome-wide association studies show a strong linkage between FOXO3 and human lifespan. Despite decades of studies on FOXOs, there are still many unresolved questions. Here, we discuss some of these knowledge gaps, related to our general understanding of transcriptional control by FOXOs, the role of the intrinsically disordered regions that constitute over 50% of FOXOs sequence, the role of cellular context in determining isoform specificity, and finally, the importance of resilience in understanding FOXO function. The latter, we think, provides context to the evolutionary role of FOXOs. So, rather than providing an exhaustive summary of literature findings, we focus on some of the omissions in our knowledge of FOXO function. Resolving these outstanding questions, we think, will help to provide the necessary insight to know how and when to manipulate FOXO function in a manner that will contribute to healthy aging.</p>","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"483 2","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-02-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12905502/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146112001","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}