ACS Pharmacology and Translational Science最新文献

{"title":"Neuropeptide Y Receptor Binding Profiles of Endogenous Ligands in the Presence and Absence of Sodium: A Panoramic View","authors":"Albert O. Gattor,&nbsp;Franziska Schettler,&nbsp;Julia Erl,&nbsp;Thomas Brunner,&nbsp;Joachim Wegener,&nbsp;Pierre Koch,&nbsp;Max Keller","doi":"10.1021/acsptsci.6c00127","DOIUrl":"https://doi.org/10.1021/acsptsci.6c00127","url":null,"abstract":"<p>Neuropeptide Y (NPY)receptors (YRs) play a key regulatoryrolein essential human physiological processes such as bone metabolism,feeding, anxiolysis, and pain modulation, making them potential therapeutictargets. Nonetheless, radiochemical ligand binding studies neededfor the development of therapeutics actings at YRs, have been conductedinconsistently in the presence or absence of sodium, the latter representinga nonphysiological-like condition that may lead to inaccurate interpretations.As such, this study aimed to provide an in-depth overview of the bindingaffinities of endogenous YR agonists, namely NPY, peptide YY (PYY),and pancreatic polypeptide (PP), to the various YR subtypes, Y₁R, Y₂R, Y₄R, and Y₅R, inthe presence and absence of sodium using recently developed tritium-labeledradioligands. Additionally, YR subtype-selective antagonists, BIBP3226(Y₁), JNJ31020028 and BIIE0246 (Y₂), UR-MK188(Y₄), and CGP71683A (Y₅), were studied. Significantdifferences in YR binding of the agonists, observed for Y₁R, Y₄R and Y₅R binding, were indicated by higherbinding affinities in the absence of sodium. The effect was most pronouncedfor Y₁R binding of PP (ca. 100-fold difference in bindingaffinity). While Y₂R binding of the Y₂R antagonistBIIE0246 and Y₄R binding of the putative Y₄Rantagonist UR-MK188 were not significantly influenced, a significantlydecreased binding affinity was observed for the antagonists BIBP3226(Y₁R) and CGP71683 (Y₅R) for binding under sodium-freeconditions compared to the sodium-containing buffer. Overall, thedetermined YR binding affinities were largely consistent with literaturedata. Findings from this study confirmed sodium’s allostericmodulation on YR agonist binding, although this modulatory effectwas shown to be dependent on the type of ligand bound.</p>","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"9 9","pages":"2497–2512"},"PeriodicalIF":3.7,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148950692","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Protease-Mediated TAR DNA-Binding Protein 43 (TDP-43) Pathogenesis: From Molecular Mechanisms to Therapeutic Opportunities","authors":"Joyal Xavier,&nbsp;Meenakshi Singh,&nbsp;Sampada Tamhankar,&nbsp;Kristine Griffett,&nbsp;Rajesh Amin","doi":"10.1021/acsptsci.6c00171","DOIUrl":"https://doi.org/10.1021/acsptsci.6c00171","url":null,"abstract":"<p>TDP-43 proteinopathyis the defining pathological featurein approximately50% of frontotemporal lobar degeneration (FTLD) cases, yet the precisemechanism or biochemical transition from nuclear proteostasis to cytoplasmictoxicity remains a critical knowledge gap. While its role in repressingnonconserved cryptic exons is well reported, this review highlightsand explores the synergy between site-specific proteolysis and post-translationalmodification (PTM)-induced phase transitions. We propose a mechanismwhere primary endoproteolytic cleavage by calpain, caspase, and asparaginylendopeptidase acts as a “protease switch” to generatea C-terminal fragment that disturbs the nuclear import ability ofTDP43. These fragments serve as preferred substrates for coordinatedhyperphosphorylation and SUMOylation, which drive widespread transcriptomeshutdown. We emphasize that synthesizing a small-molecule bridge betweenthese proteins and TDP-43 reduces aberrant protease-mediated fragmentationand delocalization of many proteins. Therefore, in this review, wehighlight several therapeutic drug discovery strategies to interceptTDP-43 at the preaggregation stage and restore its function, offeringdisease-modifying pathways.</p>","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"9 8","pages":"2076–2091"},"PeriodicalIF":3.7,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729651","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Kinetic Benefit(s) of Allosteric Receptor Blockade by Positive Allosteric Modulator Antagonists","authors":"Georges Vauquellin,&nbsp;Terry Kenakin","doi":"10.1021/acsptsci.6c00324","DOIUrl":"https://doi.org/10.1021/acsptsci.6c00324","url":null,"abstract":"<p>Thispaper discusses how targeted pharmacologic experiments canelucidate the mechanism of allosteric receptor inhibitors (NAMs) toidentify NAMs that may have exceptionally useful properties and targetresidence times in vivo. Specifically, experiments can be done toidentify positive allosteric modulator (PAM) antagonists, NAMs thatincrease the affinity of the receptor for the agonist but decreaseagonist efficacy. These molecules would be predicted to have longreceptor offset times in vivo (in the presence of ambient concentrationsof agonist) and favorable receptor residence times for therapy andalso selectively target agonist prebound receptors. Flux analysisis used to demonstrate the salient properties of PAM antagonists andtheir favorable pharmacodynamic effects for blocking physiologicalsignals.</p>","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"9 8","pages":"1994–2007"},"PeriodicalIF":3.7,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729783","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development of pH-Sensitive β-Adrenergic Receptor Antagonists","authors":"Tobias Braun,&nbsp;Theresa Pröll,&nbsp;Nils Weißing,&nbsp;Harald Hübner,&nbsp;Peter Gmeiner","doi":"10.1021/acsptsci.6c00296","DOIUrl":"https://doi.org/10.1021/acsptsci.6c00296","url":null,"abstract":"<p>G protein-coupledreceptors (GPCRs) can trigger distinct signalingpathways depending on their localization. Because their appearanceis not restricted, GPCRs can signal not only from the plasma membranebut also from internalized compartments. The pH of endosomes is significantlylower compared to the extracellular environment, and thus, location-biasedligands can be developed by carefully adjusting their physicochemicalproperties. This work describes the development of pH-sensitive β-adrenergicreceptor antagonists with weak basicity, conferring enrichment inacidic compartments. Starting from FDA-approved β-blockers includingbisoprolol, metoprolol, propranolol, and nebivolol, chemical synthesis,physicochemical studies, in vitro pharmacological investigations,and structure–activity relationship studies led to ligandswith considerably higher potency at representative acidic pH valuesof 6 and 6.5 compared to a pH of 7.4, which is typical for ligandbinding at the plasma membrane. Bis-fluorination in the beta positionof nitrogen substituents was the most effective and led to pH-sensitiveanalogs of bisoprolol, metoprolol, and propranolol with 10- to 12-foldhigher potencies at endosome-specific pH values. Because endosomalβ-adrenergic receptors are suggested to be associated with hearthypertrophy and cardiac dysfunction, the newly developed ligands mayserve as lead compounds for the development of powerful and safe cardioprotectivedrugs.</p>","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"9 8","pages":"2291–2303"},"PeriodicalIF":3.7,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729430","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Discovery of Cyclic Peptides Targeting the BRAF Dimer Interface as Dual Inhibitors","authors":"Kai Zhang,&nbsp;Wen-Wen Zhang,&nbsp;Peng Dong,&nbsp;Guangyao Wang,&nbsp;Conghao Gai,&nbsp;Xiaoyun Chai,&nbsp;Xiaobin Zhuo,&nbsp;Yuxin Xiao,&nbsp;Kaixuan Hu,&nbsp;Jing Li,&nbsp;Pei-Chao Zhang,&nbsp;Qingjie Zhao,&nbsp;Yan Zou","doi":"10.1021/acsptsci.6c00158","DOIUrl":"https://doi.org/10.1021/acsptsci.6c00158","url":null,"abstract":"<p>RAFdimerization is crucial for oncogenic signaling in RAS mutanttumors, contributing to resistance to mitogen-activated protein kinasepathway inhibitors by promoting dysregulated BRAF dimerization. Thismakes it a promising target for overcoming resistance caused by paradoxicalextracellular signal-regulated kinase (ERK) signaling activation resultingfrom BRAF mutations (e.g., BRAF^V600E) and inhibitors likevemurafenib and dabrafenib. Peptide inhibitors such as Braftide (TRHVNILLFM)block BRAF dimerization but lack cell permeability and biologicalactivity within cells. A promising solution is conjugating cell-penetratingpeptides (CPPs). However, this approach involves a trade-off: it producesa larger molecule and increases the level of off-target cytotoxicity.On the basis of the crystal structure of the BRAF homodimer, we developeda series of linear and cyclic peptides derived from Braftide. Amongthese peptides, CBF-2-2 crosses the cell membrane without the aidof CPPs and significantly inhibits tumor cell growth, exhibiting greaterserum stability than Braftide. Moreover, the composite peptide SCBF-2-2,which contains an anti-invasion sequence, disrupts BRAF dimers, effectivelyinhibits cancer cell proliferation and invasion, reduces ERK phosphorylation,and suppresses tumor growth in the A549 mouse xenograft model. SCBF-2-2offers a new starting point for developing dual-function antitumorpeptides that target the BRAF dimer.</p>","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"9 8","pages":"2266–2281"},"PeriodicalIF":3.7,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729686","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Decoding Immunometabolic Dynamics of Adipose Tissue in Obesity: Evolving Evidence and Way Forward","authors":"Kajal Kumari,&nbsp;Kanika Verma,&nbsp;Richa Yadav,&nbsp;Jaya Dwivedi,&nbsp;Sarvesh Paliwal,&nbsp;Swapnil Sharma","doi":"10.1021/acsptsci.6c00071","DOIUrl":"https://doi.org/10.1021/acsptsci.6c00071","url":null,"abstract":"<p>Obesityis a prevalent global health condition associated withan increased risk of cardiovascular and metabolic diseases. Despitethe transformative impact of GLP-1 receptor agonists and dual or tripleincretin agonists in obesity management, a significant subset of patientsdevelops therapeutic resistance, exhibits no weight loss, or experiencesweight regain after treatment discontinuation. These limitations underscorecritical gaps in understanding the biological mechanisms underlyingthe heterogeneity in drug responsiveness. Growing evidence indicatesthat adipose tissue is a dynamic immunometabolic organ in which chroniclow-grade inflammation perturbs metabolic homeostasis and modulatesthe therapeutic responsiveness. This Review integrates emerging mechanistic,translational, and multiomics evidence on obesity-induced remodelingof adipose immune-cell niches. It also delineates the effects of thesealterations, including impaired lipolysis, insulin resistance, defectivethermogenesis, and resistance to weight loss. Overall, this Reviewhighlights adipose tissue immunometabolism as a central yet oftenunderappreciated contributor to therapeutic responsiveness and a promisingtarget for future obesity therapies.</p>","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"9 8","pages":"2024–2043"},"PeriodicalIF":3.7,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729656","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Conformationally Constrained Phosphonate Backbone Linkages Enhance CpG Oligonucleotide Activation of Toll-Like Receptor 9","authors":"Ivana Kóšiová,&nbsp;Ivan Štěpánek,&nbsp;Ondřej Šimák,&nbsp;Ondřej Kostov,&nbsp;Magdalena Petrová,&nbsp;Ondřej Páv,&nbsp;Dominik Rejman,&nbsp;Radek Liboska,&nbsp;Miloš Buděšínský,&nbsp;Šárka Rosenbergová,&nbsp;Gabriel Birkuš,&nbsp;Ivan Rosenberg","doi":"10.1021/acsptsci.6c00326","DOIUrl":"https://doi.org/10.1021/acsptsci.6c00326","url":null,"abstract":"<p>The effect of flexibleversus conformationally constrained phosphonateinternucleotide linkages on CpG-mediated TLR9 activation was investigated.Sixteen analogues of the CpG oligonucleotide <strong>ODN 2006</strong>, a well-known TLR9 agonist, uniformly modified at all CpG motifs,were synthesized and evaluated in a human TLR9 (hTLR9) reporter cellline and peripheral blood mononuclear cells. Analogues bearing conformationallyconstrained 2′,3′-cytidine phosphonate modifications(<strong>ODN1</strong>–<strong>ODN10</strong>) generally exhibitedenhanced activity relative to <strong>ODN 2006</strong>, with <strong>ODN1</strong> (incorporating modification <strong>I</strong>) displaying ∼30-foldincreased potency. Analogues with flexible phosphonate linkages (<strong>ODN11</strong>, <strong>ODN13</strong>, <strong>ODN15</strong>, <strong>ODN16</strong>) showed comparable activity to that of the parent ODN, whereas additionalsugar modification abolished activity (<strong>ODN12</strong>, <strong>ODN14</strong>). A hexamer (<strong>ODN-B</strong>) incorporating the most potent modification <strong>I</strong>, when combined with CpG DNA, enhanced hTLR9 activation,consistent with interaction at the auxiliary 5′-xCx site. Thisstudy evaluates phosphonate internucleotide linkages in CpG oligonucleotidesand demonstrates that a conformationally constrained phosphonate backbonein <strong>ODN 2006</strong> analogues enhances hTLR9 activation, offeringa potential strategy for the development of potent immunostimulatoryoligonucleotides.</p>","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"9 8","pages":"2324–2332"},"PeriodicalIF":3.7,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729788","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Nutrient-Sensitive ZRF1-Dependent Secretory Network Involving S100A9 Contributes to Neutrophil Plasticity in Triple-Negative Breast Cancer","authors":"Aysegul Kaymak Ozdemir,&nbsp;Mahinur Basci,&nbsp;Minenur Kalyoncu,&nbsp;Ayse Caner,&nbsp;Serif Senturk","doi":"10.1021/acsptsci.6c00020","DOIUrl":"https://doi.org/10.1021/acsptsci.6c00020","url":null,"abstract":"<p>Zuotin-related factor 1 (ZRF1) is an essential chromatin-associatedregulator with established roles in transcription, differentiation,and cancer; however, its contribution to paracrine signaling withinthe tumor microenvironment (TME) remains unexplored. Here, we identifyZRF1 as a regulator of nutrient-sensitive tumor-derived paracrinesignaling in triple-negative breast cancer (TNBC). Across multiplebreast cancer subtypes, ZRF1 depletion altered the expression, secretion,and stress-associated protein patterns of the inflammatory mediatorS100A9. This regulation was influenced by metabolic status, wherenutrient deprivation selectively destabilized specific S100A9 proteoformsthrough proteasome-sensitive mechanisms. Bioinformatic analyses revealeda strong association between S100A9 expression and neutrophil infiltrationin breast tumors, prompting functional investigation of ZRF1-mediatedtumor–neutrophil communication using a multilayered experimentalframework. Conditioned medium from ZRF1-deficient tumor cells induceda nonbinary neutrophil activation spectrum rather than a fixed polarizationstate. This phenotypic remodeling was characterized by altered inflammatorysignaling and cytokine (IL-8) dynamics in both differentiated HL-60neutrophil-like cells and primary human neutrophils. Functionally,ZRF1-dependent paracrine cues regulated neutrophil transendothelialmigration over time. Reciprocal coculture platforms and real-timexCELLigence assays further demonstrated that ZRF1 loss sensitizestumor cells to neutrophil-derived signals, enhancing invasion anddriving state-dependent architectural remodeling in 3D tumor spheroids.Collectively, these findings support a model in which a nutrient-sensitiveZRF1-dependent secretory network involving S100A9 contributes to humanneutrophil plasticity under metabolic stress. Consequently, this studyhighlights S100A9 as one component of a broader ZRF1-regulated secretorynetwork and identifies nutrient-sensitive tumor–immune communicationas a potential therapeutic vulnerability in aggressive breast cancer.</p>","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"9 8","pages":"2198–2224"},"PeriodicalIF":3.7,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729660","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Machine-Learning-Driven Optimization of Functional Excipients and Their Biointeractions in Drug Formulations","authors":"Xiaoyue Liu,&nbsp;Liulu Xie,&nbsp;Wei Chen","doi":"10.1021/acsptsci.6c00322","DOIUrl":"https://doi.org/10.1021/acsptsci.6c00322","url":null,"abstract":"<p>Functional excipients are increasingly recognized asactive componentsin drug formulations because they can influence drug stability, solubility,release behavior, delivery efficiency, biological barrier penetration,transporter activity, and metabolic clearance. Machine learning isbecoming useful in formulation research because it can connect scatteredformulation data to excipient selection, property prediction, andexperimental decision-making. In particular, machine learning modelscan help extract useful patterns from fragmented formulation data,prioritize candidate excipients, and guide formulation decisions beforeextensive experimental screening. This review summarizes recent advancesin machine-learning-driven optimization of functional excipients andtheir biointeractions in drug formulations. We first discuss the methodologicalfoundations of this field, including data acquisition, feature engineering,model architecture selection, optimization, and evaluation strategies.Representative application scenarios are then reviewed, includingthe identification of functional excipients related to drug effluxinhibition, formulation stability enhancement, biological barrierpenetration, and metabolic clearance reduction. This review also discussespractical barriers that still limit this field related to data quality,representation design, experimental feedback, computational cost,and deployability. These issues need to be addressed before artificialintelligence (AI)-assisted formulation systems can become reliabletools for routine pharmaceutical development.</p>","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"9 8","pages":"2137–2150"},"PeriodicalIF":3.7,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729364","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Strategies for Targeting Mitochondria in the Treatment of Breast Cancer","authors":"Kexin Wang,&nbsp;Xianyi Zheng,&nbsp;Yating Li,&nbsp;Chunyan Li,&nbsp;Xiaoyong Zhang,&nbsp;Qichuan Deng,&nbsp;Hao Yang,&nbsp;Xiaocui Shuai,&nbsp;Jinqi Li,&nbsp;Li Guo,&nbsp;Jianyou Shi,&nbsp;Lan Bai","doi":"10.1021/acsptsci.5c00823","DOIUrl":"https://doi.org/10.1021/acsptsci.5c00823","url":null,"abstract":"<p>Breast cancer is the most prevalent cancer among womenworldwide,with a complex pathogenesis and diverse treatment options. However,conventional treatments are often accompanied by large side effectsand limited efficacy. In recent years, mitochondria, as the core organellesof cellular energy metabolism, oxidative stress regulation, and apoptosisexecution, have played a key role in breast cancer development, progression,metastasis, and treatment resistance. Therefore, many researchershave turned their attention to mitochondria to open up new pathwaysfor the treatment of breast cancer. This review systematically outlinesthe relationship between mitochondrial energy metabolism, antiapoptoticproteins, mitochondrial fusion/fission, mitochondrial autophagy, andferroptosis and breast cancer cell proliferation, metastasis, anddrug resistance, summarizes and analyzes the inhibitory effects ofdrugs or therapeutics targeting mitochondria, and explores the strategiesof targeting mitochondria for the treatment of breast cancer to providenew ideas and methods for the treatment of breast cancer.</p>","PeriodicalId":36426,"journal":{"name":"ACS Pharmacology and Translational Science","volume":"9 8","pages":"2008–2023"},"PeriodicalIF":3.7,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148729397","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}