Biochemical Journal最新文献

{"title":"Modulation of Nur77-DNA interactions by the glucocorticoid receptor.","authors":"Laurens W H J Heling,Kristina Kovač,Carlie J M de Vries,Alireza Mashaghi","doi":"10.1042/bcj20250293","DOIUrl":"https://doi.org/10.1042/bcj20250293","url":null,"abstract":"Nuclear receptors (NRs) comprise a superfamily of (ligand-)regulated transcription factors that are pivotal in orchestrating gene networks essential for development, metabolism, and cellular homeostasis. Their activity is critical for normal physiology, and consequently, dysregulation of NR signalling is implicated in a wide array of human diseases. Within this superfamily, the orphan nuclear receptor Nur77 and the glucocorticoid receptor (GR) are key regulators that exhibit significant cross-talk, primarily antagonistic, which is crucial for modulating inflammatory and stress responses. Despite the recognised importance of their interplay, the precise molecular mechanisms by which GR modulates Nur77's engagement with DNA remain incompletely defined. The present study elucidates the direct impact of GR and its ligand, dexamethasone (Dex), on the DNA binding dynamics of Nur77. Single-molecule DNA tightrope assays revealed that Nur77 employs a three-dimensional diffusion-based search mechanism on non-specific DNA, characterised by transient interactions with two distinct dissociation kinetic profiles. GR significantly stabilises Nur77-DNA interactions, evidenced by a shift towards longer residence times, primarily achieved by slowing the dissociation of the more transiently interacting Nur77 population. Conversely, single-molecule analysis and biochemical assays demonstrated that Dex alone markedly reduces Nur77's overall DNA binding affinity kinetics and frequency in a sequence-dependent manner, to such an extent that accurate quantification was unfeasible. These findings delineate distinct modulatory effects of the GR protein and its ligand on Nur77-DNA interactions, providing crucial biophysical insights into their complex regulatory interplay and revealing a direct, GR-independent impact of Dex on Nur77's DNA engagement.","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"9 1","pages":"429-440"},"PeriodicalIF":4.1,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147471643","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":"Structural enzymology of a Fusarium graminearum aldehyde oxidase reveals a distinct active-site and reactivity versus its paralog galactose oxidase.","authors":"Jessica K Fong, Laura Mazo, Alison K Nairn, Rosa Lorizolla Cordeiro, Yann Mathieu, Yu Seby Chen, Carme Rovira, Paul H Walton, Filip Van Petegem, Harry Brumer","doi":"10.1042/BCJ20260010","DOIUrl":"10.1042/BCJ20260010","url":null,"abstract":"<p><p>Copper radical oxidases (CROs), which comprise Auxiliary Activity Family 5 (AA5) in the Carbohydrate-Active Enzymes (CAZy) classification, have a long history of study due to their unique catalytic mechanism and biotechnological applications. The majority of mechanistic and structural insights into CRO function have been obtained from studies on the galactose 6-oxidase from the fungal phytopathogen Fusarium graminearum (FgrGalOx) of AA5 subfamily 2 (AA5_2). In contrast, enzyme structure/function studies of CROs from subfamily 1, comprising glyoxal oxidases, are limited. Here, we report the biochemical characterisation of the individual AA5_1 members from F. graminearum and Colletotrichum graminicola, which exhibit predominant activities on aldehydes, such as methylglyoxal, and enantioselectivity for d-glyceraldehyde. Electron paramagnetic resonance indicated that the AA5_1 aldehyde oxidases possessed similar copper coordination geometry to AA5_2 CROs, including a canonical cross-linked Tyr-Cys residue. However, the X-ray crystal structure of the F. graminearum aldehyde oxidase-the first of a fungal AA5_1 CRO-strikingly revealed that a key radical-stabilising tryptophan side chain in the second coordination sphere is provided by a different position in the polypeptide chain and exists in a flipped orientation vis-à-vis AA5_2 members. Quantum mechanics/molecular mechanics (QM/MM) calculations demonstrated that, in contrast to the AA5_2 GalOx, the AA5_1 aldehyde oxidase does not delocalise spin density onto the second-sphere tryptophan as a consequence of this alternative active-site arrangement. Together, these data provide new molecular insight into catalytic selectivity among the distinct subfamilies of alcohol- and aldehyde-specific CROs, which will facilitate elucidation of their biological roles and inform their application as biocatalysts.</p>","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"483 4","pages":"493-509"},"PeriodicalIF":4.3,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13094651/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147509107","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":"Artemether and Euphorbia factor L9 suppress kynurenine production through distinct effects on tryptophan metabolism.","authors":"Alina L Capatina, Tomasz Czechowski, Charlotte Plunkett-Jones, Thierry Tonon, Ioannis Kourtzelis, Benjamin R Lichman, William J Brackenbury, Ian A Graham, Dimitris Lagos","doi":"10.1042/BCJ20253246","DOIUrl":"10.1042/BCJ20253246","url":null,"abstract":"<p><p>l-Tryptophan (Trp) is an essential amino acid catabolised through the kynurenine pathway, which is mediated by the enzymes indoleamine-2,3-dioxygenase 1 (IDO1), IDO2, or Trp-2,3-deoxygenase. In cancer, IDO1 acts as an immune checkpoint, suppressing effector T cell function. Yet, direct inhibition of IDO1 has had limited success in clinical trials. Therefore, alternative approaches to Trp metabolism therapeutic targeting are needed. We screened a library of 597 natural products (NPs) or NP derivatives for their effect on kynurenine production in triple-negative breast cancer cells. This revealed 24 candidate inhibitors of kynurenine production. Among them, artemether, a member of the artemisinin family of anti-malarial drugs, suppressed kynurenine production, likely via an endoperoxide bridge-dependent mechanism. The Euphorbia factor L9 (EFL9) inhibited kynurenine production, likely via a C7-benzoylation-dependent mechanism. Neither artemether nor EFL9 affected JAK/STAT signalling or IDO1 levels. Targeted metabolomics and molecular docking analyses demonstrated that artemether suppressed kynurenine production through heme sequestration and potential interactions with the IDO1 heme-binding pocket A. EFL9 affected Trp metabolism through heme-independent mechanisms and resulted in changes in purine and amino acid metabolism and the cellular redox balance. Notably, ouabain, a regulator of IDO1 levels, and linrodostat, a clinically approved IDO1 inhibitor, revealed distinct metabolic profiles, with ouabain and EFL9 showing the largest overlap. Importantly, the kynurenine-suppressing activities of artemether and EFL9 were observed in non-transformed primary mammary epithelial cells and also lung cancer cells. Overall, our findings set the foundation for future studies exploring the use of artemether or EFL9 as novel Trp metabolism-targeting therapeutics.</p>","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":" ","pages":"541-564"},"PeriodicalIF":4.3,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13094657/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147442268","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":"Excretory-secretory products of the fish-borne parasite Anisakis simplex L3 larvae possess allergens and unusual glycan modifications.","authors":"Isabella Adduci, Xiaoxu Wang, Katharina Paschinger, Iain B H Wilson, Guofeng Cheng, Shi Yan","doi":"10.1042/BCJ20253281","DOIUrl":"10.1042/BCJ20253281","url":null,"abstract":"<p><p>Anisakis simplex is a parasitic aquatic nematode, which may cause mild-to-severe gastrointestinal allergic reactions (anisakiasis) with clinical symptoms, such as rhinitis and urticaria, in humans who accidentally consume raw or undercooked marine products contaminated with infective L3 Anisakis larvae. Several Anisakis excretory-secretory (E/S) products and somatic proteins are known to be involved in IgE-mediated allergic reactions. In comparison with vertebrates, nematodes have a distinct machinery to glycosylate their proteins, and unusual glycan structures have been reported previously, many of which play immunogenic and immunomodulatory roles in host-parasite interactions. While an early study indicated that O-glycans participate in the cross-reactivity of antibodies in allergy patients to A. simplex somatic antigens, the N-glycosylation pattern of Anisakis and the potential role of N-glycans in allergic reactions remained unknown. The aim of the present study was to characterise N-glycans and the associated glycoproteins from Anisakis E/S products using mass spectrometry. We collected E/S products from larvae culture and released N-glycans from trypsinised proteins using PNGase Ar. Native glycans were pyridylaminated prior to HPLC separation and MALDI-TOF-MS/MS analysis. In addition, hydrofluoric acid and glycosidase digestions were performed to aid structural characterisation. MS data of 5 h and 24 h E/S products indicated the presence of pauci-mannose and core fucosylated N-glycans as major species; tri-fucosylated and methylated glycans as well as complex-type and phosphorylcholine-substituted glycans were also detected. In addition, E/S products were subject to proteomics analysis, which revealed a set of proteins with conserved domains associated with allergens. Our study provides the first insight into the N-glycosylation machinery of Anisakis and highlights the need for investigating whether and which N-glycans are indubitably involved in the modulation of allergic responses.</p>","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":" ","pages":"391-408"},"PeriodicalIF":4.3,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147289074","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":"Towards broad-spectrum antiviral drugs: inhibition of transmembrane serine proteases.","authors":"Victoria Banas,Michael P Mannino,James W Janetka","doi":"10.1042/bcj20250335","DOIUrl":"https://doi.org/10.1042/bcj20250335","url":null,"abstract":"Proteases are important for the pathogenesis of many viruses. These proteolytic enzymes cleave one or more amide bonds of viral proteins. This protein processing is required for viral entry and replication. The most widely utilized for this purpose are serine proteases, the majority of which are host cell transmembrane, or membrane associated serine proteases such as matriptase, TMPRSS2, TMPRSS11D, and TMPRSS13. Several host cysteine proteases like members of the Cathepsin family (e.g. Cathepsin L) are also highjacked by viruses to process viral proteins to infect their hosts. To target these proteases as antiviral drugs, many inhibitors, both competitive and covalent, have been developed but none have been advanced to clinical evaluation to date. Herein, we review these proteases, their viral protein substrates, pathogenesis, and their inhibitors.","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"12 1","pages":"441-478"},"PeriodicalIF":4.1,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147471642","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":"Protein oxidation in crowded environments.","authors":"Eduardo Fuentes-Lemus","doi":"10.1042/BCJ20250150","DOIUrl":"10.1042/BCJ20250150","url":null,"abstract":"<p><p>Proteins are the most abundant macromolecules in biological systems. This high abundance and the presence of electron-rich side-chains make proteins a major target for biological oxidants. Protein oxidation encompasses a complex set of reactions that, depending on protein structure and the chemical properties of the oxidant, can trigger specific and reversible modifications, or can irreversibly damage multiple side-chains. Therefore, understanding protein oxidation from a mechanistic and kinetic perspective is important to illuminate the molecular basis of physiological (e.g. redox signaling) and pathological processes (e.g. cardiovascular disease and neurodegenerative diseases). However, an existing conundrum in the redox biochemistry field is whether (and how) intrinsic properties of biological environments, such as the crowded intracellular conditions resulting from the high abundance of macromolecules and protein confinement, modulate oxidation rates and pathways. These obvious, but often neglected, aspects of biological environments have begun to be systematically addressed, suggesting that the crowded intracellular conditions would be an important player in the oxidative biology of proteins. This review outlines the importance of protein oxidation in physiology and pathology. Then, thoroughly discusses the modulatory effect that crowding exerts on biochemical processes that involve proteins, particularly on the oxidative modification of proteins. Finally, evidence that illustrates the interplay that would exist between crowding, protein oxidation, and protein confinement by phase separation is discussed. The author proposes that the transition from using dilute in vitro studies to an experimental workflow that takes into account the crowded and heterogeneous conditions encountered is the cell is mandatory to rigorously investigate protein oxidation.</p>","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"483 4","pages":"565-584"},"PeriodicalIF":4.3,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13094654/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147589605","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":"Dual targeting of SLC6A14 and autophagy/macropinocytosis enhances therapeutic efficacy in pancreatic ductal adenocarcinoma.","authors":"Yangzom D Bhutia, Mosharaf Mahmud Syed, Devaraja Rajasekaran, Souad R Sennoune, Tanima Sharker, Oscar Sanchez, Mary Katherine Jurek, Longfa Kou, Ruijie Chen, Vadivel Ganapathy","doi":"10.1042/BCJ20250155","DOIUrl":"https://doi.org/10.1042/BCJ20250155","url":null,"abstract":"<p><p>PDAC is highly desmoplastic and undergoes metabolic reprogramming to sustain their growth and proliferation. Our laboratory has identified SLC6A14, an amino acid transporter, as a novel drug target for PDAC. Genetic deletion of SLC6A14 or its pharmacological blockade with α-MLT attenuates PDAC growth by inducing amino acid deprivation. However, nutrient stress, particularly amino acid deprivation, can induce nutrient scavenging mechanisms like autophagy and macropinocytosis, thereby undermining the full anticancer potential of SLC6A14 blockade. To address this, the current work was conducted to test if SLC6A14 blockade induces autophagy and/or macropinocytosis and to further investigate if dual inhibition of SLC6A14 (α-MLT) and autophagy/macropinocytosis (HCQ) would yield a better therapeutic outcome in PDAC as opposed to targeting SLC6A14 alone. In vitro assays (MTT and colony formation) revealed that the combination treatment significantly reduced PDAC cell viability and clonogenic potential as opposed to monotherapy. Treatment model subcutaneous xenograft in athymic nude mice demonstrated a superior therapeutic outcome with the combination regimen. Collectively, our study demonstrates that the afore-described combination therapy creates a metabolic trap wherein α-MLT induces nutrient stress, while HCQ prevents autophagic and macropinocytosis compensation, thus culminating in a more potent tumor attenuation. This dual blockade represents a hitherto unexplored treatment strategy for PDAC.</p>","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":" ","pages":""},"PeriodicalIF":4.3,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147637958","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":"Understanding single stranded DNA gaps: from formation to fate.","authors":"Sonal Garg,George-Lucian Moldovan","doi":"10.1042/bcj20253455","DOIUrl":"https://doi.org/10.1042/bcj20253455","url":null,"abstract":"Single-stranded DNA gaps (ssDNA gaps) have emerged as a potential indicator of therapeutic response in cancer. Accumulation of ssDNA gaps is associated with increased sensitivity of cancer cells to genotoxic therapies like PARP inhibitors (PARPi) and cisplatin chemotherapy. However, efficient repair or suppression of ssDNA gap formation is associated with therapy resistance and treatment failure. Therefore, understanding how ssDNA gaps form and are repaired can help identify biomarkers that can guide new treatment strategies to overcome resistance. In this review, we discuss different sources of ssDNA gap formation and the repair mechanisms that have been characterized to date. We bring together current knowledge on how these gaps are processed and what their ultimate fate may be. Finally, we discuss how established drugs like PARPi, hydroxyurea, and platinum compounds, induce and/or exploit ssDNA gaps. Throughout this review, we highlight ssDNA gaps as a potential therapeutic vulnerability that can be used to advance personalized cancer therapy.","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"16 1","pages":"527-540"},"PeriodicalIF":4.1,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147578170","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":"Cold exposure remodels bile acid metabolism in a mouse strain- and tissue-specific manner.","authors":"Sarra Beji,Mathilde Mouchiroud,Bernie Efole,Yves Gélinas,Mélanie Verreault,Jocelyn Trottier,Andreanne Michaud,Olivier Barbier,Alexandre Caron","doi":"10.1042/bcj20260006","DOIUrl":"https://doi.org/10.1042/bcj20260006","url":null,"abstract":"Cold exposure remodels bile acid metabolism, but whether these changes are conserved across mouse strains and biological compartments is unclear. We profiled bile acid composition in C57BL/6J (C57) and C3H/HeJ (C3H) mice housed at 30°C or exposed to 10°C for 6h, 24h, or 72h. Total, conjugated, and unconjugated bile acids were quantified in liver, plasma, and feces. In liver, Cyp7a1 and Cyp8b1 increased after 24h of cold in both strains, and Cyp2c70 andCyp7b1 increased with higher levels in C3H. C57 showed decreases in taurine-conjugated muricholic acids (T-α-MCA, T-β-MCA, T-ω-MCA) after 72h of cold exposure whereas C3H maintained or increased hepatic TCA, TUDCA, and β-MCA. In plasma, C57 accumulated conjugated bile acids at 72h (TCA, TCDCA, TUDCA, THDCA), while C3H remained largely unchanged. In feces, total bile acids fell at 6h in both strains, and conjugated species were consistently higher in C3H across conditions. C57BL/6J mice showed hepatic depletion and systemic accumulation of conjugated bile acids, while C3H/HeJ maintained higher hepatic and fecal conjugates, consistent with enhanced excretory flux. These distinct profiles highlight TCA, TUDCA, β-MCA, and TCDCA as candidate bile acid species associated with cold-induced thermogenic adaptation. Together, our findings reveal that genetic background and temperature interact to shape bile acid handling and signaling, providing a framework to interpret variability in the metabolic outcomes of bile acid-based interventions.","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"147 1","pages":""},"PeriodicalIF":4.1,"publicationDate":"2026-03-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147502519","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":"Structural characterization of OsPDIL2-3, a rice protein disulfide isomerase involved in prolamin accumulation.","authors":"Zui Fujimoto,Kento Yonezawa,Mutsumi Sakurai,Naomi Kishine,Mitsuru Momma,Nobutaka Shimizu,Yasushi Kawagoe","doi":"10.1042/bcj20253474","DOIUrl":"https://doi.org/10.1042/bcj20253474","url":null,"abstract":"Protein disulfide isomerase-like 2-3 (OsPDIL2-3) is a rice endosperm-specific member of the PDI family that localizes to protein body-I and is essential for the accumulation of the cysteine‑rich 10-kDa prolamin crP10. OsPDIL2-3 comprises three thioredoxin-like domains (a0, a, and b). Here, we combined X-ray crystallography, size-exclusion chromatography-coupled small-angle X-ray scattering (SEC-SAXS), and ensemble optimization analysis to characterize the structural basis of OsPDIL2-3 function. Crystal structures of truncated constructs revealed that domain a0 forms a stable homodimer, whereas domain a mediates a weaker and labile dimeric interaction. SEC-SAXS analysis of the full-length protein demonstrated that OsPDIL2-3 predominantly exist as a flexible dimer in solution, populating a broad ensemble of conformational states rather than a single quaternary structure. This conformational heterogeneity arises from the flexible linker between the a0 and a domains, which acts as a molecular hinge permitting large-amplitude domain rearrangements. Structural prediction of OsPDIL2-3-crP10 complex suggested that domain a0 preferentially captures unfolded or partially folded crP10, whereas domain a promotes disulfide-bond rearrangement toward the native fold. These results support a model in which OsPDIL2-3 functions as a linker- mediated dynamic dimer, in which interdomain flexibility spatially coordinates substrate capture and oxidative refolding. Our results provide mechanistic insight into the specialized functions of plant PDIs and highlight their roles in the assembly of cereal seed storage protein complexes.","PeriodicalId":8825,"journal":{"name":"Biochemical Journal","volume":"2018 1","pages":""},"PeriodicalIF":4.1,"publicationDate":"2026-03-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147502521","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}