Journal of Membrane Biology最新文献

{"title":"Deciphering Membrane Pore Formation Mechanisms of Plasmodium falciparum Perforin-Like Protein 1 (PfPLP1).","authors":"Sanket B Patil, Subrata Dasgupta, Prasenjit Bhaumik","doi":"10.1007/s00232-026-00376-5","DOIUrl":"https://doi.org/10.1007/s00232-026-00376-5","url":null,"abstract":"<p><p>Membrane Attack Complex/Perforin (MACPF) domain proteins are β-pore forming toxins (β-PFTs) involved in the pathogenesis of various organisms. Among them, Perforin-like proteins (PLPs), produced by Plasmodium species, play essential roles in parasite invasion and egress. Due to increasing drug resistance in Plasmodium, PLPs represent promising but underexplored therapeutic targets, largely due to the lack of structural and mechanistic data. This study investigates the binding and pore formation mechanism of the Plasmodium falciparum PLP1 (PfPLP1), which is expressed during the human life cycle of the parasite. We modeled PfPLP1 structure and performed both all-atom and coarse-grained molecular dynamics simulations in soluble and membrane-associated states. PfPLP1 comprises two domains, a canonical MACPF domain and a β-pleated sheet domain- apicomplexan perforin β-domain (APCβ). Initial membrane binding is mediated by cationic residues at the base of the APCβ domain, which interact with the polar headgroups of the lipids from the host cell membrane. We analyzed the membrane-inserted tetrameric form where water molecules were observed to penetrate between the tetramer and the lipid bilayer, initiating pore opening. During this process, lipids reorganize into a toroidal edge to shield their hydrophobic tails, while water mixes with lipid headgroups in a disordered, heterogeneous fashion. Larger oligomeric assemblies show lateral displacement of lipids and a clear tendency to form pore-like structures. This study provides molecular insights into PfPLP1's membrane binding and pore-forming behavior in both monomeric and oligomeric forms. The outcome of this study would be applicable in understanding pore formation mechanism in other PLPs and similar toxins.</p>","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":"259 1","pages":""},"PeriodicalIF":2.9,"publicationDate":"2026-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147864758","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular Partners of Voltage-Gated Calcium Channel β and α₂δ Auxiliary Subunits: Roles in Channel Complex Regulation and Beyond.","authors":"Alejandra Corzo-López, Margarita Leyva-Leyva, Ricardo González-Ramírez, Alejandro Sandoval, Ricardo Felix","doi":"10.1007/s00232-026-00371-w","DOIUrl":"10.1007/s00232-026-00371-w","url":null,"abstract":"<p><p>Research on the auxiliary subunits β (Ca_Vβ) and α₂δ (Ca_Vα₂δ) of voltage-gated calcium channels has gained increasing interest as novel and unexpected functional interactions for these proteins are discovered. Beyond their classic role as regulators of the channel complex, these subunits participate in the spatiotemporal fine-tuning of the channels and in diverse cellular processes. Currently, multiple studies are investigating the interactions between Ca_Vβ and Ca_Vα₂δ with other proteins outside the channel complex, and how these associations affect relevant cellular functions such as cell growth, differentiation, and gene expression beyond their effects on channel activity. The auxiliary subunits have also been observed to associate with components involved in calcium channel biogenesis, a process independent of the direct modulation of channel activity. Furthermore, their involvement in the intracellular transport of other channels and receptors, as well as in nuclear signaling, has been demonstrated. The expression of different variants or isoforms may fulfill specific functions in diverse tissues and developmental stages, even outside the channel complex. Undoubtedly, the study of these proteins as scaffolding or regulatory molecules for other proteins has significantly enriched our understanding of their influence on cell signaling and excitability.</p>","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":"259 1","pages":""},"PeriodicalIF":2.9,"publicationDate":"2026-03-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12992490/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147469994","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Deciphering the Influence of Side Chains of Short Cationic Hydrophobic Peptides on Macroscopic and Molecular Properties of Mixed Lipid Bilayers.","authors":"Lea Pašalić, Andreja Jakas, Ana Čikoš, Barbara Pem, Danijela Bakarić","doi":"10.1007/s00232-026-00373-8","DOIUrl":"https://doi.org/10.1007/s00232-026-00373-8","url":null,"abstract":"<p><p>Cell-penetrating peptides (CPPs) are increasingly used for delivering cargo into cells, but the mechanisms of their membrane crossing remain poorly understood, even for shorter cationic hydrophobic peptides. This study explores how cationic hydrophobic peptides with various combinations of cationic (K and R) and hydrophobic (W and I) amino acids interact with lipid bilayers made of 90% neutral lipid 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (PC) and 10% anionic lipids (either 1,2-dipalmitoyl-sn-glycero-3-phosphatidylglycerol (PG) or 1,2-dipalmitoyl-sn-glycero-3-phosphoserine (PS)). Specifically, it was found that changing the hydrophobic segment from W to I significantly influences turbidity during the pretransition for the PC/PG mixture. Conversely, in the PC/PS mixture, the interaction with I-peptides causes changes in turbidity during the main phase transition, regardless of whether the cationic segment is R or K. Molecular features analyzed through FTIR spectroscopy revealed significant differences in the vibrations of methylene groups within hydrocarbon chains. In the presence of I-peptides, regardless of whether they are R or K derivatives, a notably higher number of kink conformers were observed compared to W-peptides. Although W-peptides tend to form aggregates due to the insertion of their hydrophobic segments into the lipid bilayer, they appear to maintain the membrane's integrity and the organization of lipids. In contrast, the branched side chains of the I-segment induce out-of-plane movements in the hydrocarbon chains. As the initial interaction between the peptide and the lipid membrane is crucial for its translocation, these findings provide insights into the molecular events occurring before translocation and emphasize the specifics that make it unique to CPPs.</p>","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":"259 1","pages":""},"PeriodicalIF":2.9,"publicationDate":"2026-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147437032","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mechanistic Insights into Human Defensin Antimicrobial Activity from Membrane Simulations.","authors":"Anna K Manukyan","doi":"10.1007/s00232-026-00372-9","DOIUrl":"10.1007/s00232-026-00372-9","url":null,"abstract":"<p><p>Defensins function as critical effectors of innate immunity, displaying broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. While experimental studies have extensively characterized these peptides, the molecular mechanisms governing their membrane interactions remain poorly understood. This investigation employed comprehensive molecular dynamics simulations to analyze six defensins (human and rabbit α-defensins HNP1, HNP3, rabbit NP4 and human β-defensins HBD1, HBD2, HBD3) using the IMM1 implicit membrane model for studying interactions with anionic bacterial membranes. Both monomeric and dimeric forms were examined to elucidate oligomerization effects on membrane binding and penetration mechanisms. Transfer energy calculations revealed distinct binding patterns and orientations among different defensin subtypes, with β-defensins demonstrating superior membrane affinity compared to α-defensins. HBD3 exhibited the most favorable membrane interactions, correlating with its exceptional antimicrobial potency. Binding orientation analysis demonstrated that defensins adopt specific membrane-bound configurations that optimize electrostatic interactions with anionic membrane surfaces while strategically positioning hydrophobic regions for effective membrane insertion. These findings provide molecular level insights into defensin selectivity mechanisms for bacterial membranes and establish a foundation for defensin-based therapeutic development. The results validate that computational approaches effectively complement experimental studies in elucidating complex antimicrobial peptide mechanisms. This modeling framework supports rational design of next generation defensin therapeutics with optimized antimicrobial activity and pathogen selectivity.</p>","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":"259 1","pages":""},"PeriodicalIF":2.9,"publicationDate":"2026-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147357136","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Rapid Single-cell Measurement of Transient Transmembrane Water Flow under Osmotic Gradient.","authors":"Hong Jiang, Jinnawat Jongkhumkrong, Y J Chao, Qian Wang, Guiren Wang","doi":"10.1007/s00232-026-00375-6","DOIUrl":"10.1007/s00232-026-00375-6","url":null,"abstract":"<p><p>Aquaporins (AQPs) are critical for transmembrane water transport in response to osmotic gradients, but their gating and regulatory mechanisms remain poorly understood. A central challenge is the lack of methods to measure water flow across AQPs from individual cells with the spatiotemporal resolution and sensitivity equivalent to patch-clamp recordings of ion fluxes-a limitation stemming from the electrically silent nature of water flow. Here, we present a novel optical technique-Flow-Induced Fluorescence Increase Velocimetry (FIFIV) based on Laser-Induced Fluorescence Photobleaching Anemometry (LIFPA)-that enables direct, real-time monitoring of cytoplasmic flow induced by transmembrane water transport under osmotic pressure gradients. Using small molecular fluorescent dyes to label cytoplasm in single adherent MDA-MB-231 breast cancer cells, we show detection of instantaneous extremely low transmembrane water flow signals on the order of 1 μm/s following localized hypotonic stimulation. This approach circumvents the limitations of traditional volume-based osmotic permeability assays, achieving single-cell sensitivity and temporal resolution comparable to electrophysiological measurements of ion flux. FIFIV potentially provides a new optical approach for probing transmembrane water-flow-induced intracellular dynamics, and a foundation for future investigations of AQP regulation and gating mechanisms in physiopathological studies and drug discovery.</p>","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":"259 1","pages":""},"PeriodicalIF":2.9,"publicationDate":"2026-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12935827/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147286162","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Oxysterol Induced Fluid-Fluid Phase Separation in Saturated Phosphatidylcholine Membranes: Influence of Lipid Chain Length.","authors":"P K Shabeeb, Sreeja Sasidharan, S Madhukar, Md Arif Kamal, V A Raghunathan","doi":"10.1007/s00232-026-00374-7","DOIUrl":"https://doi.org/10.1007/s00232-026-00374-7","url":null,"abstract":"<p><p>We have recently reported the observation of closed-loop fluid-fluid immiscibility in 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) lipid membranes containing either 25-hydroxycholesterol (25HCH) or 27-hydroxycholesterol (27HCH) (Kamal et al. Proc Natl Acad Sci 120(25):2216002120, https://doi.org/10.1073/pnas.2216002120 ,  2023). Here we extend these studies to membranes of symmetric, saturated phospholipids having chain length varying from 12 to 16 carbon atoms. The phase behavior of the PC-25HCH and PC-27HCH membranes were probed by using fluorescence microscopy, atomic force microscopy and small angle X-ray scattering. 25HCH is found to induce fluid-fluid coexistence in these membranes for lipid chains lengths varying from 12 to 15 C atoms, whereas 27HCH induces similar phase behavior for chain lengths varying from 13 to 16. Thus the occurrence of fluid-fluid coexistence in these membranes depends both on the position of the -OH group in the oxysterol side chain as well as the membrane thickness. Our earlier studies have indicated that the phase behavior of these binary membranes can be understood in terms of the temperature-dependent orientation of the oxysterol in the membrane. Our present results suggest that the relative energies of these orientations depend on the membrane thickness and the oxysterol structure. Observation of fluid-fluid immiscibility in different saturated lipid model membranes containing 25HCH or 27HCH shows the generic nature of this phase behavior.</p>","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":"259 1","pages":"5"},"PeriodicalIF":2.9,"publicationDate":"2026-02-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146127347","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Membrane Remodeling Activity of Dengue Virus NS4A and NS1 Proteins: A Computational Perspective.","authors":"Dwaipayan Chaudhuri, Kalyan Giri","doi":"10.1007/s00232-025-00369-w","DOIUrl":"https://doi.org/10.1007/s00232-025-00369-w","url":null,"abstract":"<p><p>Dengue virus (DENV) non-structural protein NS4A and NS1 are crucial for viral replication and have the ability to cause extensive remodeling of the host cell membrane. Here, a computational strategy has been used to study the structural and functional aspects of NS4A and NS1 in membrane interaction and remodeling. By employing multiscale all atom and coarse grained molecular dynamics simulations, we investigated the conformational dynamics of NS4A and NS1 and their interactions with model lipid bilayers. Our results establish that NS4A inserts preferentially into membranes in its native state as an integral membrane protein and causes curvature aided by its oligomerization event, which is in agreement with its proposed function in replication complex formation. NS1 has stable lipid-binding domains that can anchor and induce membrane curvature or stabilize remodelled membrane structures and perform its function as a peripherally bound membrane protein. These findings give molecular-level insights into the mechanism of how DENV hijacks host membranes for replication and identify potential targets for antiviral interventions. This study also plays an important role in updating our knowledge of flaviviral manipulation of membranes.</p>","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":"259 1","pages":"6"},"PeriodicalIF":2.9,"publicationDate":"2026-02-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146127330","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Analysis of the Effect of the Magnetic Field on Water Flux Through TIP3;1 Aquaporins Using Molecular Dynamics in GROMACS.","authors":"Diego Fernando Nieto-Giraldo, José Mauricio Rodas Rodríguez, Javier Torres-Osorio","doi":"10.1007/s00232-025-00368-x","DOIUrl":"10.1007/s00232-025-00368-x","url":null,"abstract":"<p><p>Magnetobiology studies the effects of magnetic fields on biological systems. In this context, the Magnetobiology Research Group at the University of Caldas has hypothesized that magnetic treatment may influence water flow through cell membranes. To contribute to evaluating this hypothesis, this study analyzes the effect of magnetic fields on water transport through TIP3;1 aquaporins of Zea mays L. Molecular dynamics simulations were performed using a modified version of GROMACS that includes magnetic forces in the Velocity-Verlet algorithm, exposing a TIP3;1 homotetramer embedded in a lipid bilayer to static, uniform magnetic flux densities (B) ranging from 0 to 10 T and oriented along the membrane normal (z-axis). The system was solvated with the SPC/E water model. To assess the impact on water flow, we analyzed the conformational dynamics of TIP3;1, protein-water interactions within the single-file channel, and the osmotic permeability coefficient (p_f). Trajectory analysis revealed that the magnetic field alters the average pore radius and increases protein conformational variability. These structural changes affect the intermolecular interactions between the protein and water molecules, influencing water mobility through the channel. Systems exposed to magnetic fields showed up to a threefold increase in pf compared to the control. These findings suggest that magnetic fields can modulate water flow through membranes, supporting a possible mechanism of magnetically influenced water transport in biological systems.</p>","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":"259 1","pages":"7"},"PeriodicalIF":2.9,"publicationDate":"2026-02-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12876521/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146127325","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Targeting hORAI1-Mediated Calcium Influx in Triple-Negative Breast Cancer: A Computational Drug Discovery Approach.","authors":"Sangavi Pandi, Hemavathy Nagarajan, Sneha Subramaniyan, Jeyakanthan Jeyaraman, Sampathkumar Ranganathan, Langeswaran Kulanthaivel","doi":"10.1007/s00232-025-00365-0","DOIUrl":"https://doi.org/10.1007/s00232-025-00365-0","url":null,"abstract":"<p><p>Store-operated calcium entry (SOCE) is a crucial pathway that aids in restoring depleted calcium levels in the endoplasmic reticulum (ER), consequently regulating cellular calcium homeostasis. When calcium stores are low, two key proteins are activated: STIM1, which senses the calcium levels in the ER, and ORAI1, the pore-forming subunit of calcium release-activated calcium (CRAC) channels. ORAI1 is overexpressed in triple-negative breast cancer (TNBC) and regulates the transcription of genes that regulate cancer progression. The complete atomic structure of human ORAI1 (hORAI1) remains unknown, which poses a challenge for developing targeted therapies. This study modeled the closed state of hORAI1, identifying it as a potential target for disrupting calcium influx and oncogenic signaling in TNBC. A pharmacophore hypothesis derived from Mildronate analogues was utilized to screen the COCONUT database for small compounds that stabilize the closed state of hORAI1. Five promising compounds were identified: CNP0006530, CNP0006516, CNP0008628, CNP0002844, and CNP0004972. These compounds exhibited docking scores ranging from - 7.461 to - 5.393 kcal/mol and formed stable interactions with crucial residues, Glu106 and Asp110. This likely aids in stabilizing the closed conformation and inhibiting calcium influx. Molecular dynamics simulations have demonstrated the structural stability and compactness of the lead complexes. Furthermore, principal PCA/FEL analyses have validated their conformational stability within a membrane environment. These findings provide novel insights into the structural gating processes of hORAI1 and emphasize the therapeutic potential of small compounds that target its closed state to inhibit calcium-mediated carcinogenesis in TNBC.</p>","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":"259 1","pages":"4"},"PeriodicalIF":2.9,"publicationDate":"2026-01-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146087819","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Na⁺ Uptake Triggered in Adrenal Chromaffin Cells by a 5-ns Electric Pulse is Facilitated by Ca²⁺ Influx Via an L-Type-Like Ca²⁺ Channel Independent of Changes in Membrane Potential.","authors":"Lisha Yang, Josette Zaklit, Thomas W Gould, Gale L Craviso, Normand Leblanc","doi":"10.1007/s00232-026-00370-x","DOIUrl":"https://doi.org/10.1007/s00232-026-00370-x","url":null,"abstract":"<p><p>Whole-cell voltage patch clamp studies have shown that in bovine adrenal chromaffin cells held at -70 mV, a single 5-ns, 5 MV/m pulse activates a membrane conductance carried partially by Na⁺ through TRPC4/5 channels and the sodium leak channel (NALCN). Here we used fluorescence imaging with the Na⁺ indicator ING-2 to further investigate Na⁺ influx pathways. A 5-ns, 5 MV pulse elicited a tetrodotoxin-insensitive rise in ING-2 fluorescence that exhibited a similar electric field dependency and response to pulse-pair stimulation as the inward current. Increases in ING-2 fluorescence were partially inhibited by the NALCN inhibitor CP96345, the TRPC4/5 channel inhibitor M084, or the broad spectrum TRP channel inhibitor La³⁺, and fully blocked by the combination of these agents, suggesting involvement also of a La³⁺-sensitive Na⁺ pathway. Cholesterol depletion with methyl-β-cyclodextrin or PIP₂ synthesis inhibition with wortmannin also reduced the response. Full inhibition was achieved with the selective L-type voltage-gated Ca²⁺ channel (VGCC) inhibitors nitrendipine, verapamil, or diltiazem but not the broad-spectrum inhibitor Cd²⁺. Inhibitors of N- and P/Q-type VGCC had no effect. Fluorescence Ca²⁺ imaging in voltage-clamped GCaMP6f-expressing murine chromaffin cells held at -70 mV revealed a nitrendipine-sensitive, Cd²⁺-insensitive increase in intracellular Ca²⁺ that accompanied the inward current. These results provide evidence that nanoelectropulse-induced Na⁺ influx into chromaffin cells involves several Na⁺ influx pathways that are facilitated by Ca²⁺ influx via an L-type-like Ca²⁺ channel associated with cholesterol-rich membrane domains. Investigating such membrane effects is essential for developing nanosecond electric pulse technologies for stimulating and/or modulating excitable cells.</p>","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":"259 1","pages":"3"},"PeriodicalIF":2.9,"publicationDate":"2026-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146013305","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}