Toxins最新文献

{"title":"It's a Small World After All: The Remarkable but Overlooked Diversity of Venomous Organisms, with Candidates Among Plants, Fungi, Protists, Bacteria, and Viruses.","authors":"William K Hayes, Eric C K Gren, David R Nelsen, Aaron G Corbit, Allen M Cooper, Gerad A Fox, M Benjamin Streit","doi":"10.3390/toxins17030099","DOIUrl":"10.3390/toxins17030099","url":null,"abstract":"<p><p>Numerous organisms, including animals, plants, fungi, protists, and bacteria, rely on toxins to meet their needs. Biological toxins have been classified into three groups: poisons transferred passively without a delivery mechanism; toxungens delivered to the body surface without an accompanying wound; and venoms conveyed to internal tissues via the creation of a wound. The distinctions highlight the evolutionary pathways by which toxins acquire specialized functions. Heretofore, the term venom has been largely restricted to animals. However, careful consideration reveals a surprising diversity of organisms that deploy toxic secretions via strategies remarkably analogous to those of venomous animals. Numerous plants inject toxins and pathogenic microorganisms into animals through stinging trichomes, thorns, spines, prickles, raphides, and silica needles. Some plants protect themselves via ants as venomous symbionts. Certain fungi deliver toxins via hyphae into infected hosts for nutritional and/or defensive purposes. Fungi can possess penetration structures, sometimes independent of the hyphae, that create a wound to facilitate toxin delivery. Some protists discharge harpoon-like extrusomes (toxicysts and nematocysts) that penetrate their prey and deliver toxins. Many bacteria possess secretion systems or contractile injection systems that can introduce toxins into targets via wounds. Viruses, though not \"true\" organisms according to many, include a group (the bacteriophages) which can inject nucleic acids and virion proteins into host cells that inflict damage rivaling that of conventional venoms. Collectively, these examples suggest that venom delivery systems-and even toxungen delivery systems, which we briefly address-are much more widespread than previously recognized. Thus, our understanding of venom as an evolutionary novelty has focused on only a small proportion of venomous organisms. With regard to this widespread form of toxin deployment, the words of the Sherman Brothers in Disney's iconic tune, <i>It's a Small World</i>, could hardly be more apt: \"There's so much that we share, that it's time we're aware, it's a small world after all\".</p>","PeriodicalId":23119,"journal":{"name":"Toxins","volume":"17 3","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11945383/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143731808","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synthesis and Evaluation of Melittin-Modified Peptides for Antibacterial Activity.","authors":"Xiangxiang Xu, Hongyi Fu, Weihui Wu, Liang Zong, Dan Li, Bo Zhuang, Yelin Qi, Xiuli Qi, Ting Liang","doi":"10.3390/toxins17020098","DOIUrl":"10.3390/toxins17020098","url":null,"abstract":"<p><p>Melittin, a naturally occurring antimicrobial peptide, demonstrates broad-spectrum activity, effectively suppressing and eliminating both Gram-positive and Gram-negative bacteria, including specific drug-resistant strains. In this study, molecular simulation software was employed to investigate and modify the structure of melittin with the aim of synthesizing a modified peptide exhibiting enhanced antibacterial potency and assessing its bacteriostatic and antibacterial properties. The primary research objectives were as follows: 1. Preparation and characterization of melittin-modified peptide-Using molecular simulation software, the structure of the melittin-modified peptide was adjusted to predict its activity and select the most appropriate amino acid sequence. The peptide was synthesized through solid-phase peptide synthesis employing the Fmoc strategy and subsequently purified using liquid chromatography. The yield of the purified modified melittin was determined to be 30.97%, and the identity of the product was confirmed by LC-MS and MALDI-TOF-MS. 2. Evaluation of the antimicrobial activity of the melittin-modified peptide-The minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) of melittin and its modified peptide were measured using gradient dilution and plate counting techniques. The results revealed that both melittin and its modified peptide exhibited strong antibacterial efficacy against Gram-positive and Gram-negative bacteria, as well as certain drug-resistant strains. This showed that melittin and its modified peptide have the same antibacterial (killing) effect. A scanning electron microscope analysis indicated that both melittin and its modified peptide were capable of disrupting bacterial cell structures, leading to bacterial cell death.</p>","PeriodicalId":23119,"journal":{"name":"Toxins","volume":"17 2","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11860715/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143493389","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Delineation of Aflatoxicosis on Health and Performance of Water Buffalo (<i>Bubalus bubalis</i>) and Its Therapeutic and Nutritional Management.","authors":"Rajesh Kumar, Sanjay Kumar, Supriya Chhotaray, Madhu Singh, Rupali Rautela, Avijit Dey","doi":"10.3390/toxins17020097","DOIUrl":"10.3390/toxins17020097","url":null,"abstract":"<p><p>A symptom of reduced feed intake, conception and progressive emaciation was noticed in the Murrah buffalo farm of the institute with tail gangrene in some buffaloes and the sudden death of many animals. Thus, the objective of the study was for the systemic investigation to find out the causative agents and necessary ameliorative measures. The tail lesion includes alopecia, scales, necrosis, oedematous and a painful area. After thorough examination of the signs and symptoms of the disease, it was speculated that the case may be due to the presence of mycotoxins in the feeds offered to the animals. The severely affected buffaloes that died subjected to post-mortem examination demonstrated liver damage, nephritis and haemorrhages in all the vital organs. The analyses of offered feed revealed a high concentration of aflatoxin B1 content in maize, groundnut cake, cottonseed cake and compound feed mixtures. The case was typically diagnosed as the aflatoxicosis in water buffalo and ameliorative measures viz. the withdrawal of contaminated feeds, supplementation of toxin binder and penta-sulphate mixture in the feed taken sustained animal health and production performances. Severely affected animals with tail gangrene were treated with local disinfectants and antibiotics as well as systemic injection with broad-spectrum antibiotics and supportive vitamins and minerals to recover to their previous stage. Therefore, routine check-ups of feeds are of utmost importance to prevent feeding of aflatoxin-contaminated feeds. Systemic efforts viz. therapeutic management with topical medicines, broad-spectrum antibiotics, supportive therapies with vitamins and antioxidants along with replacement of contaminated feeds and inclusion of peta-sulphate mixture, and a toxin binder are effective in the prevention and control of aflatoxicosis in buffaloes.</p>","PeriodicalId":23119,"journal":{"name":"Toxins","volume":"17 2","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11860594/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143493416","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Insights into the Role of Proteolytic and Adhesive Domains of Snake Venom Metalloproteinases from <i>Bothrops</i> spp. in the Control of <i>Toxoplasma gondii</i> Infection.","authors":"Samuel C Teixeira, Thales A M Fernandes, Guilherme de Souza, Luana C Luz, Marina Paschoalino, Joed P de L Junior, Alessandra M Rosini, Aryani F F Martínez, Vitor de Freitas, Daiana S Lopes, Patrícia B Clissa, Vinícius C de Souza, Milton Y Nishiyama-Jr, Bellisa F Barbosa, Eloisa A V Ferro, Veridiana de M R Ávila","doi":"10.3390/toxins17020095","DOIUrl":"10.3390/toxins17020095","url":null,"abstract":"<p><p>Toxoplasmosis is an alarming public health problem that affects more than one-third of the world's population. In our work, we investigated the antiparasitic effects of catalytically active [BpMP-I and Jararhagin (Jar)] and catalytically inactive [Jararhagin-C (Jar-C)] snake venom metalloproteinases (SVMPs) in human HeLa cells. These toxins impaired the parasite invasion and intracellular growth, and modulated IL-6, IL-8, and MIF cytokines that control the cell susceptibility and response against <i>T. gondii</i>. Furthermore, we verified that the antiprotozoal activities are not restricted to the presence of the proteolytic domain, and the adhesive domains participate in the control of <i>T. gondii</i> infection. Also, by analyzing the structures of Jar and Jar-C through molecular modeling and dynamics, we observed that the adhesive domains in Jar-C are more exposed due to the absence of the proteolytic domain, which could favor the interaction with different targets. Our investigation on the role of SVMP domains in combating <i>T. gondii</i> infection highlights their potential application as biotechnological tools for creating more effective treatments for toxoplasmosis.</p>","PeriodicalId":23119,"journal":{"name":"Toxins","volume":"17 2","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11861417/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143493625","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The First K⁺-Channel Blocker Described from <i>Tityus fasciolatus</i> Venom: The Purification, Molecular Cloning, and Functional Characterization of α-KTx4.9 (Tf5).","authors":"Isolda de Sousa Monteiro, Israel Flor Silva de Araújo, Thalita Soares Camargos, Ernesto Ortiz, Adolfo Carlos Barros de Souza, Jonathan Dias Lima, Lourival D Possani, Elisabeth Ferroni Schwartz, Diogo Vieira Tibery","doi":"10.3390/toxins17020096","DOIUrl":"10.3390/toxins17020096","url":null,"abstract":"<p><p>Hundreds of toxins, particularly from scorpions of lesser medical significance, remain unknown, especially those from species endemic to specific ecosystems, such as <i>Tityus fasciolatus</i>. Their discovery could contribute to the development of new drugs for channelopathies and other diseases. Tf5 is a new peptide that has been identified from the venom of <i>Tityus fasciolatus</i>, a scorpion species endemic to the Brazilian Cerrado ecosystem. A full-length cDNA sequence of the Tf5 gene was obtained through a previously constructed transcriptomic library, where an ORF (Open Reading Frame) sequence with a length of 180 was found, including the 37 aa mature KTx domain, which has six Cys residues. Tf5 was purified from the crude venom, resulting in a peptide with a molecular mass of 3983.95 Da. Its K⁺ channel blocker activity was evaluated on Kv1.1, Kv1.2, Kv1.3, and Kv1.4 subtypes. Of these Kv channels, the peptide demonstrated an ability to block Kv1.2 and Kv1.3 with an IC₅₀ of 15.53 nM and 116.41 nM, respectively. Additionally, Tf5 shares a high degree of sequence identity with toxins from the α-KTx4 subfamily, which led to it being classified as α-KTx4.9. This is the first Kv channel blocker described from the <i>T. fasciolatus</i> scorpion.</p>","PeriodicalId":23119,"journal":{"name":"Toxins","volume":"17 2","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11861696/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143493496","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"ConoGPT: Fine-Tuning a Protein Language Model by Incorporating Disulfide Bond Information for Conotoxin Sequence Generation.","authors":"Guohui Zhao, Cheng Ge, Wenzheng Han, Rilei Yu, Hao Liu","doi":"10.3390/toxins17020093","DOIUrl":"10.3390/toxins17020093","url":null,"abstract":"<p><p>Conotoxins are a class of peptide toxins secreted by marine mollusks of the Conus genus, characterized by their unique mechanism of action and significant biological activity, making them highly valuable for drug development. However, traditional methods of acquiring conotoxins, such as in vivo extraction or chemical synthesis, face challenges of high costs, long cycles, and limited exploration of sequence diversity. To address these issues, we propose the ConoGPT model, a conotoxin sequence generation model that fine-tunes the ProtGPT2 model by incorporating disulfide bond information. Experimental results demonstrate that sequences generated by ConoGPT exhibit high consistency with authentic conotoxins in physicochemical properties and show considerable potential for generating novel conotoxins. Furthermore, compared to models without disulfide bond information, ConoGPT outperforms in terms of generating sequences with ordered structures. The majority of the filtered sequences were shown to possess significant binding affinities to nicotinic acetylcholine receptor (nAChR) targets based on molecular docking. Molecular dynamics simulations of the selected sequences further confirmed the dynamic stability of the generated sequences in complex with their respective targets. This study not only provides a new technological approach for conotoxin design but also offers a novel strategy for generating functional peptides.</p>","PeriodicalId":23119,"journal":{"name":"Toxins","volume":"17 2","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11860916/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143493405","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Report from the 30th Meeting on Toxinology, \"Unlocking the Deep Secrets of Toxins\", Organized by the French Society of Toxinology on 2-3 December 2024.","authors":"Pascale Marchot, Ziad Fajloun, Évelyne Benoit, Sylvie Diochot","doi":"10.3390/toxins17020094","DOIUrl":"10.3390/toxins17020094","url":null,"abstract":"<p><p>The French Society of Toxinology (SFET) held its 30th Annual Meeting (RT30) on 2-3 December 2024 at Hôtel Le Saint Paul in Nice, France, on the beautiful French Riviera. It was the first time that the event was organized outside of Paris. The meeting brought together 74 participants and focused on the main theme, \"Unlocking the Deep Secrets of Toxins\", which delved into cutting-edge research in the field of animal venoms and toxins from animal, plant, fungal, algal, mold and bacterial sources. The event emphasized the dynamic and ever-evolving nature of toxins, often influenced by environmental factors, their interactions with molecular or cellular ligands, their mechanisms of action and their potential applications in therapy. These key topics were explored in depth during oral communications and poster sessions across three main thematic areas, each dedicated to a specific aspect of toxinology. A fourth, more general session provided an opportunity for participants to present recent work that fell outside the main themes but still contributed valuable insights to the broader field. This report presents the abstracts of seven of the invited lectures, fifteen of the selected lectures and sixteen of the posters, following the authors' agreement to publish them. Additionally, the names of the \"Best Oral Communication\" and \"Best Poster\" awardees are highlighted, recognizing the outstanding contributions made by early-career researchers and their innovative work in toxinology.</p>","PeriodicalId":23119,"journal":{"name":"Toxins","volume":"17 2","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11861921/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143493651","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Deciphering the Neurotoxic Effects of <i>Karenia selliformis</i>.","authors":"Ambbar Aballay-González, Jessica Panes-Fernández, Catharina Alves-de-Souza, Bernd Krock, Juan José Gallardo-Rodríguez, Nicole Espinoza-Rubilar, Jorge Fuentealba, Allisson Astuya-Villalón","doi":"10.3390/toxins17020092","DOIUrl":"10.3390/toxins17020092","url":null,"abstract":"<p><p><i>Karenia selliformis</i> is a globally recognized dinoflagellate associated with harmful algal blooms and massive fish kills along southern Chilean coasts. Its toxicity varies with environmental factors and genetic diversity. While <i>K. selliformis</i> is traditionally linked to neurotoxins like gymnodimines (GYMs), analysis of the strain CREAN-KS02 from Chile's Aysén Region (43° S) revealed no presence of toxins associated with this genus, such as gymnodimines, brevetoxins, or brevenal. Given the high toxicity and impact on marine life, our study aimed to functionally characterize the neurotoxic metabolites in the exudate of <i>K. selliformis</i> cultures. Cytotoxicity was evaluated using a Neuro-2a cell-based assay (CBA), determining an IC₅₀ of 2.41 ± 0.02 μg mL^-1. The incubation of Neuro-2a cells with the bioactive lipophilic extract obtained from the exudate of <i>K. selliformis</i> and the ouabain/veratridine couple showed activation of voltage-gated ion channels. Electrophysiological recordings on cultured mouse hippocampal neurons showed that the extract increased cell excitability in a dose-dependent manner, modulating action potential firing and exhibiting an opposed effect to tetrodotoxin. These findings indicate the presence of excitatory neurotoxic compounds affecting mammalian cells. This study provides the first mechanistic evidence of <i>K. selliformis</i> toxicity and highlights potential risks associated with its proliferation in marine environments.</p>","PeriodicalId":23119,"journal":{"name":"Toxins","volume":"17 2","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11861105/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143493411","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"First Report of Safe Italian Peanut Production Regarding Aflatoxin.","authors":"Matteo Crosta, Michele Croci, Chiara Dall'Asta, Michele Pisante, Paola Battilani","doi":"10.3390/toxins17020090","DOIUrl":"10.3390/toxins17020090","url":null,"abstract":"<p><p>The growing interest in peanut production in Italy represents a significant opportunity from both an agronomic and economic standpoint. Aflatoxin B₁ (AFB1) contamination is a major concern with imported peanuts; developing an Italian peanut supply chain can ensure a well-managed local product, with special care for food safety. This study aimed to provide a first overview of Italian peanut production, focusing on the <i>Aspergillus</i> section <i>Flavi</i> and AFB1 occurrence in the raw product. During 2022 and 2023, 18 peanut fields were sampled at complete maturity across the Italian production areas, considering three varieties: Lotos, SIS-AR_01, and IPG914. The results showed the occurrence of <i>Aspergillus</i> sec. <i>Flavi</i> in peanut pods, even though AFB1 was always absent or in traces, well below the European legal limits. These findings confirmed the quality of Italian peanut production, even though further research is requested to confirm the positive results of this first report.</p>","PeriodicalId":23119,"journal":{"name":"Toxins","volume":"17 2","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11860490/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143493615","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Breaking Barriers: Candidalysin Disrupts Epithelial Integrity and Induces Inflammation in a Gut-on-Chip Model.","authors":"Moran Morelli, Karla Queiroz","doi":"10.3390/toxins17020089","DOIUrl":"10.3390/toxins17020089","url":null,"abstract":"<p><p><i>Candida albicans</i> is an opportunistic pathogenic yeast commonly found in the gastrointestinal tract of healthy humans. Under certain conditions, it can become invasive and cause life-threatening systemic infections. One mechanism used by <i>C.albicans</i> to breach the epithelial barrier is the secretion of candidalysin, a cytolytic peptide toxin. Candidalysin damages epithelial membranes and activates the innate immune response, making it key to <i>C.albicans</i>' pathogenicity and a promising therapeutic target. Although candidalysin mediates <i>C. albicans</i> translocation through intestinal layers, its impact on epithelial responses is not fully understood. This study aims to characterize this response and develop scalable, quantitative methodologies to assess candidalysin's toxicological effects using gut-on-chip models. We used the OrganoPlate^® platform to expose Caco-2 tubules to candidalysin and evaluated their response with trans-epithelial electrical resistance (TEER), protein detection, and immunostaining. We then validated our findings in a proof-of-concept experiment using human intestinal organoid tubules. Candidalysin impaired barrier integrity, induced actin remodeling, and increased cell permeability. It also induced the release of LDH, cytokines, and the antimicrobial peptide LL37, suggesting cellular damage, inflammation, and antimicrobial activity. This study strengthens our understanding of candidalysin's role in <i>C. albicans</i> pathogenesis and suggests new therapeutic strategies targeting this toxin. Moreover, patient-derived organoids show promise for capturing patient heterogeneity and developing personalized treatments.</p>","PeriodicalId":23119,"journal":{"name":"Toxins","volume":"17 2","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11861147/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143493387","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}