Channels (Austin, Tex.)最新文献

Piezo1 in microglial cells: Implications for neuroinflammation and tumorigenesis. 小胶质细胞中的Piezo1：对神经炎症和肿瘤发生的影响。

Channels (Austin, Tex.) Pub Date : 2025-12-01 Epub Date: 2025-04-13 DOI: 10.1080/19336950.2025.2492161

Bo Yang, Zhenyu Li, Peiliang Li, Yuhan Liu, Xinghuan Ding, Enshan Feng

{"title":"Piezo1 in microglial cells: Implications for neuroinflammation and tumorigenesis.","authors":"Bo Yang, Zhenyu Li, Peiliang Li, Yuhan Liu, Xinghuan Ding, Enshan Feng","doi":"10.1080/19336950.2025.2492161","DOIUrl":"https://doi.org/10.1080/19336950.2025.2492161","url":null,"abstract":"Microglia, the central nervous system (CNS) resident immune cells, are pivotal in regulating neurodevelopment, maintaining neural homeostasis, and mediating neuroinflammatory responses. Recent research has highlighted the importance of mechanotransduction, the process by which cells convert mechanical stimuli into biochemical signals, in regulating microglial activity. Among the various mechanosensitive channels, Piezo1 has emerged as a key player in microglia, influencing their behavior under both physiological and pathological conditions. This review focuses on the expression and role of Piezo1 in microglial cells, particularly in the context of neuroinflammation and tumorigenesis. We explore how Piezo1 mediates microglial responses to mechanical changes within the CNS, such as alterations in tissue stiffness and fluid shear stress, which are common in conditions like multiple sclerosis, Alzheimer's disease, cerebral ischemia, and gliomas. The review also discusses the potential of targeting Piezo1 for therapeutic intervention, given its involvement in the modulation of microglial activity and its impact on disease progression. This review integrates findings from recent studies to provide a comprehensive overview of Piezo1's mechanistic pathways in microglial function. These insights illuminate new possibilities for developing targeted therapies addressing CNS disorders with neuroinflammation and pathological tissue mechanics.","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":"19 1","pages":"2492161"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12005408/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144013533","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Biophysical and structural mechanisms of epilepsy-associated mutations in the S4-S5 Linker of KCNQ2 channels. KCNQ2通道S4-S5连接子癫痫相关突变的生物物理和结构机制

Channels (Austin, Tex.) Pub Date : 2025-12-01 Epub Date: 2025-02-19 DOI: 10.1080/19336950.2025.2464735

Inn-Chi Lee, Yen-Yu Yang, Hsueh-Kai Chang, Swee-Hee Wong, Shi-Bing Yang

{"title":"Biophysical and structural mechanisms of epilepsy-associated mutations in the S4-S5 Linker of KCNQ2 channels.","authors":"Inn-Chi Lee, Yen-Yu Yang, Hsueh-Kai Chang, Swee-Hee Wong, Shi-Bing Yang","doi":"10.1080/19336950.2025.2464735","DOIUrl":"10.1080/19336950.2025.2464735","url":null,"abstract":"Mutations in KCNQ2 are linked to various neurological disorders, including neonatal-onset epilepsy. The severity of these conditions often correlates with the mutation's location and the biochemical properties of the altered amino acid side chains. Two mutations affecting aspartate at position 212 (D212) in the S4-S5 linker of KCNQ2 have been identified. Interestingly, while the charge-conserved D212E mutation leads to severe neonatal-onset developmental and epileptic encephalopathy (DEE), the more dramatic substitution to glycine (D212G) results in self-limited familial neonatal epilepsy (SLFNE), a much milder pathology. To elucidate the underlying mechanisms, we performed electrophysiological studies and in silico simulations to investigate these mutations' biophysical and structural effects. Our findings reveal that the D212E mutation stabilizes the channel in the voltage sensor down-state and destabilizes the up-state, leading to a rightward shift in the voltage-dependent activation curve, slower activation kinetics, and accelerated deactivation kinetics. This disruption in KCNQ2 voltage sensitivity persists even in the more physiologically relevant KCNQ2/3 heterotetrameric channels. In contrast, the D212G mutation primarily destabilizes the up-state, but its impact on voltage sensitivity is significantly reduced in KCNQ2/3 heterotetrameric channels. These findings provide key insights into the biophysical and structural basis of KCNQ2 D212 mutations and their contribution to epilepsy-related symptoms, offering a clearer understanding of how these mutations drive the varied clinical outcomes observed in patients.","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":"19 1","pages":"2464735"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11845087/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143460980","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Electrophysiological characterization of sourced human iPSC-derived motor neurons. 来源于人ipsc的运动神经元的电生理特性。

Channels (Austin, Tex.) Pub Date : 2025-12-01 Epub Date: 2025-03-25 DOI: 10.1080/19336950.2025.2480713

Bohumila Jurkovicova-Tarabova, Robin N Stringer, Zuzana Sevcikova Tomaskova, Norbert Weiss

{"title":"Electrophysiological characterization of sourced human iPSC-derived motor neurons.","authors":"Bohumila Jurkovicova-Tarabova, Robin N Stringer, Zuzana Sevcikova Tomaskova, Norbert Weiss","doi":"10.1080/19336950.2025.2480713","DOIUrl":"10.1080/19336950.2025.2480713","url":null,"abstract":"Induced pluripotent stem cell (iPSC)-derived motor neurons provide a powerful platform for studying motor neuron diseases. These cells enable human-specific modeling of disease mechanisms and high-throughput drug screening. While commercially available iPSC-derived motor neurons offer a convenient alternative to time-intensive differentiation protocols, their electrophysiological properties and maturation require comprehensive evaluation to validate their utility for research and therapeutic applications. In this study, we characterized the electrophysiological properties of commercially available iPSC-derived motor neurons. Immunofluorescence confirmed the expression of motor neuron-specific biomarkers, indicating successful differentiation and maturation. Electrophysiological recordings revealed stable passive membrane properties, maturation-dependent improvements in action potential kinetics, and progressive increases in repetitive firing. Voltage-clamp analyses confirmed the functional expression of key ion channels, including high- and low-voltage-activated calcium channels, TTX-sensitive and TTX-insensitive sodium channels, and voltage-gated potassium channels. While the neurons exhibited hallmark features of motor neuron physiology, high input resistance, depolarized resting membrane potentials, and limited firing capacity suggest incomplete electrical maturation. Altogether, these findings underscore the potential of commercially available iPSC-derived motor neurons as a practical resource for MND research, while highlighting the need for optimized protocols to support prolonged culture and full maturation.","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":"19 1","pages":"2480713"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11938304/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143702178","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Exploring the potential for gene therapy in Cav1.4-related retinal channelopathies. 探索基因治疗cav1.4相关视网膜通道病变的潜力。

Channels (Austin, Tex.) Pub Date : 2025-12-01 Epub Date: 2025-03-25 DOI: 10.1080/19336950.2025.2480089

Matthias Ganglberger, Alexandra Koschak

引用次数: 0

The GluN3-containing NMDA receptors. 含glun3的NMDA受体。

Channels (Austin, Tex.) Pub Date : 2025-12-01 Epub Date: 2025-04-16 DOI: 10.1080/19336950.2025.2490308

Kunlong Xiong, Shulei Lou, Zuoyu Lian, Yunlin Wu, Zengwei Kou

{"title":"The GluN3-containing NMDA receptors.","authors":"Kunlong Xiong, Shulei Lou, Zuoyu Lian, Yunlin Wu, Zengwei Kou","doi":"10.1080/19336950.2025.2490308","DOIUrl":"https://doi.org/10.1080/19336950.2025.2490308","url":null,"abstract":"N-methyl-D-aspartate receptors (NMDARs) are heterotetrameric ion channels that play crucial roles in brain function. Among all the NMDAR subtypes, GluN1-N3 receptors exhibit unique agonist binding and gating properties. Unlike \"conventional\" GluN1-N2 receptors, which require both glycine and glutamate for activation, GluN1-N3 receptors are activated solely by glycine. Furthermore, GluN1-N3 receptors display faster desensitization, reduced Ca2+ permeability, and lower sensitivity to Mg2+ blockage compared to GluN1-N2 receptors. Due to these characteristics, GluN1-N3 receptors are thought to play critical roles in eliminating redundant synapses and pruning spines in early stages of brain development. Recent studies have advanced pharmacological tools for specifically targeting GluN1-N3 receptors and provided direct evidence of these glycine-activated excitatory receptors in native brain tissue. The structural basis of GluN1-N3 receptors has also been elucidated through cryo-EM and artificial intelligence. These findings highlight that GluN1-N3 receptors are not only involved in essential brain functions but also present potential targets for drug development.","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":"19 1","pages":"2490308"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12005412/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144059965","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Role of the C-terminal domain in modifying pH-dependent regulation of Ca_v1.4 Ca²⁺ channels. c端结构域在修改Cav1.4 Ca2+通道ph依赖性调节中的作用。

Channels (Austin, Tex.) Pub Date : 2025-12-01 Epub Date: 2025-03-21 DOI: 10.1080/19336950.2025.2473074

Juan de la Rosa Vázquez, Amy Lee

{"title":"Role of the C-terminal domain in modifying pH-dependent regulation of Cav1.4 Ca2+ channels.","authors":"Juan de la Rosa Vázquez, Amy Lee","doi":"10.1080/19336950.2025.2473074","DOIUrl":"10.1080/19336950.2025.2473074","url":null,"abstract":"In the retina, Ca2+ influx through Cav1.4 Ca2+ channels triggers neurotransmitter release from rod and cone photoreceptors. Changes in extracellular pH modify channel opening, enabling a feedback regulation of photoreceptor output that contributes to the encoding of color and contrast. However, the mechanisms underlying pH-dependent modulation of Cav1.4 are poorly understood. Here, we investigated the role of the C-terminal domain (CTD) of Cav1.4 in pH-dependent modulation of Ba2+ currents (IBa) in HEK293T cells transfected with the full length CaV1.4 (FL) or variants lacking portions of the CTD due to alternative splicing (Δe47) or a disease-causing mutation (K1591X). While extracellular alkalinization caused an increase in IBa for each variant, the magnitude of this increase was significantly diminished (~40-50%) for both CTD variants; K1591X was unique in showing no pH-dependent increase in maximal conductance. Moreover, the auxiliary α2δ-4 subunit augmented the pH sensitivity of IBa, as compared to α2δ-1 or no α2δ, for FL and K1591X but not Δe47. We conclude that the CTD and α2δ-4 are critical determinants of pH-dependent modulation of Cav1.4 and may influence the processing of visual information in normal and diseased states of the retina.","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":"19 1","pages":"2473074"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11934190/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143671726","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The role and mechanism of vascular wall cell ion channels in vascular fibrosis remodeling. 血管壁细胞离子通道在血管纤维化重塑中的作用和机制。

Channels (Austin, Tex.) Pub Date : 2024-12-01 Epub Date: 2024-10-19 DOI: 10.1080/19336950.2024.2418128

Xiaolin Zhang, Hai Tian, Cheng Xie, Yan Yang, Pengyun Li, Jun Cheng

{"title":"The role and mechanism of vascular wall cell ion channels in vascular fibrosis remodeling.","authors":"Xiaolin Zhang, Hai Tian, Cheng Xie, Yan Yang, Pengyun Li, Jun Cheng","doi":"10.1080/19336950.2024.2418128","DOIUrl":"10.1080/19336950.2024.2418128","url":null,"abstract":"Fibrosis is usually the final pathological state of many chronic inflammatory diseases and may lead to organ malfunction. Excessive deposition of extracellular matrix (ECM) molecules is a characteristic of most fibrotic tissues. The blood vessel wall contains three layers of membrane structure, including the intima, which is composed of endothelial cells; the media, which is composed of smooth muscle cells; and the adventitia, which is formed by the interaction of connective tissue and fibroblasts. The occurrence and progression of vascular remodeling are closely associated with cardiovascular diseases, and vascular remodeling can alter the original structure and function of the blood vessel. Dysregulation of the composition of the extracellular matrix in blood vessels leads to the continuous advancement of vascular stiffening and fibrosis. Vascular fibrosis reaction leads to excessive deposition of the extracellular matrix in the vascular adventitia, reduces vessel compliance, and ultimately alters key aspects of vascular biomechanics. The pathogenesis of fibrosis in the vasculature and strategies for its reversal have become interesting and important challenges. Ion channels are widely expressed in the cardiovascular system; they regulate blood pressure, maintain cardiovascular function homeostasis, and play important roles in ion transport, cell differentiation, proliferation. In blood vessels, different types of ion channels in fibroblasts, smooth muscle cells and endothelial cells may be relevant mediators of the development of fibrosis in organs or tissues. This review discusses the known roles of ion channels in vascular fibrosis remodeling and discusses potential therapeutic targets for regulating remodeling and repair after vascular injury.","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":"18 1","pages":"2418128"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11492694/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142482288","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A phenylalanine at the extracellular side of Kir1.1 facilitates potassium permeation. Kir1.1 细胞外侧的苯丙氨酸可促进钾渗透。

Channels (Austin, Tex.) Pub Date : 2024-12-01 Epub Date: 2024-01-07 DOI: 10.1080/19336950.2023.2294661

Henry Sackin, Mikheil Nanazashvili

{"title":"A phenylalanine at the extracellular side of Kir1.1 facilitates potassium permeation.","authors":"Henry Sackin, Mikheil Nanazashvili","doi":"10.1080/19336950.2023.2294661","DOIUrl":"10.1080/19336950.2023.2294661","url":null,"abstract":"The Kir1.1 (ROMK) family of weak inward rectifiers controls K secretion in the renal CCT and K recycling in the renal TALH. A single point mutant of the inward rectifier, F127V-Kir1.1b was used to investigate the K transition between the selectivity filter and the outer mouth of the channel. We hypothesize that normally an aromatic Phe at the external entryway of Kir1.1b facilitates outward K secretion. We tested this by replacing F127-Kir1.1b with a small aliphatic Val. Results indicate that removal of the Phe at 127 suppresses outward currents that normally contribute to K secretion. Results with the F127V mutant could be explained by increased polyamine block and/or a decrease in the avidity of Kir1.1 for K ions near the outer mouth of the channel. The latter is supported by F127V-Kir1.1b having a lower affinity (Km = 33 mM) for K than wild-type Kir1.1b (Km = 7 mM) during external K elevation. Conversely, chelation of K with 18-Crown-6 ether reduced K conductance faster in F127V (half-time = 6s) than in wt-Kir1.1b (half-time = 120s), implying that F127V is less hospitable to external K. In other experiments, positive membrane potentials gated the F127V mutant channel closed at physiological levels of external Ca, possibly by electrostatically depleting K adjacent to the membrane, suggesting that the Phe residue is critical for outward K secretion at physiological Ca. We speculate that the avidity of wt-Kir1.1b for external K could result from a cation-Pi interaction between K and the aromatic F127.","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":"18 1","pages":"2294661"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10773671/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139111385","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A structural atlas of druggable sites on Na_v channels. Nav通道上可用药部位的结构地图集。

Channels (Austin, Tex.) Pub Date : 2024-12-01 Epub Date: 2023-11-30 DOI: 10.1080/19336950.2023.2287832

Zhangqiang Li, Qiurong Wu, Nieng Yan

{"title":"A structural atlas of druggable sites on Nav channels.","authors":"Zhangqiang Li, Qiurong Wu, Nieng Yan","doi":"10.1080/19336950.2023.2287832","DOIUrl":"10.1080/19336950.2023.2287832","url":null,"abstract":"Voltage-gated sodium (Nav) channels govern membrane excitability by initiating and propagating action potentials. Consistent with their physiological significance, dysfunction, or mutations in these channels are associated with various channelopathies. Nav channels are thereby major targets for various clinical and investigational drugs. In addition, a large number of natural toxins, both small molecules and peptides, can bind to Nav channels and modulate their functions. Technological breakthrough in cryo-electron microscopy (cryo-EM) has enabled the determination of high-resolution structures of eukaryotic and eventually human Nav channels, alone or in complex with auxiliary subunits, toxins, and drugs. These studies have not only advanced our comprehension of channel architecture and working mechanisms but also afforded unprecedented clarity to the molecular basis for the binding and mechanism of action (MOA) of prototypical drugs and toxins. In this review, we will provide an overview of the recent advances in structural pharmacology of Nav channels, encompassing the structural map for ligand binding on Nav channels. These findings have established a vital groundwork for future drug development.","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":"18 1","pages":"2287832"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10732651/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138464760","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The endocannabinoid ARA-S facilitates the activation of cardiac Kv7.1/KCNE1 channels from different species. 内源性大麻素 ARA-S 可促进激活不同物种的心脏 Kv7.1/KCNE1 通道。

Channels (Austin, Tex.) Pub Date : 2024-12-01 Epub Date: 2024-10-27 DOI: 10.1080/19336950.2024.2420651

Irene Hiniesto-Iñigo, Veronika A Linhart, Ali S Kusay, Sara I Liin

{"title":"The endocannabinoid ARA-S facilitates the activation of cardiac Kv7.1/KCNE1 channels from different species.","authors":"Irene Hiniesto-Iñigo, Veronika A Linhart, Ali S Kusay, Sara I Liin","doi":"10.1080/19336950.2024.2420651","DOIUrl":"10.1080/19336950.2024.2420651","url":null,"abstract":"The endogenous endocannabinoid-like compound N-arachidonoyl-L-serine (ARA-S) facilitates activation of the human Kv7.1/KCNE1 channel and shortens a prolonged action potential duration and QT interval in guinea pig hearts. Hence, ARA-S is interesting to study further in cardiac models to explore the functional impact of such Kv7.1/KCNE1-mediated effects. To guide which animal models would be suitable for assessing ARA-S effects, and to aid interpretation of findings in different experimental models, it is useful to know whether Kv7.1/KCNE1 channels from relevant species respond similarly to ARA-S. To this end, we used the two-electrode voltage clamp technique to compare the effects of ARA-S on Kv7.1/KCNE1 channels from guinea pig, rabbit, and human Kv7.1/KCNE1, when expressed in Xenopus laevis oocytes. We found that the activation of Kv7.1/KCNE1 channels from all tested species was facilitated by ARA-S, seen as a concentration-dependent shift in the voltage-dependence of channel opening and increase in current amplitude and conductance over a broad voltage range. The rabbit channel displayed quantitatively similar effects as the human channel, whereas the guinea pig channel responded with more prominent increase in current amplitude and maximal conductance. This study suggests that rabbit and guinea pig models are both suitable for studying ARA-S effects mediated via Kv7.1/KCNE1.","PeriodicalId":72555,"journal":{"name":"Channels (Austin, Tex.)","volume":"18 1","pages":"2420651"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11520554/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142514023","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0