Cell Surface最新文献

{"title":"Insights into the complex formation of a trimeric autotransporter adhesin with a peptidoglycan-binding periplasmic protein","authors":"Shogo Yoshimoto ,&nbsp;Jun Sasahara ,&nbsp;Atsuo Suzuki ,&nbsp;Junichi Kanie ,&nbsp;Kotaro Koiwai ,&nbsp;Andrei N. Lupas ,&nbsp;Katsutoshi Hori","doi":"10.1016/j.tcsw.2025.100155","DOIUrl":"10.1016/j.tcsw.2025.100155","url":null,"abstract":"<div><div>Trimeric autotransporter adhesins (TAAs) are outer membrane (OM) proteins that are widely distributed in gram-negative bacteria and are involved primarily in adhesion to biotic and abiotic surfaces, cell agglutination, and biofilm formation. TAAs consist of a passenger domain, which is secreted onto the cell surface, and a transmembrane domain, which forms a pore in the OM to secrete and anchor the passenger domain. Because the interactions between TAAs and chaperones or dedicated auxiliary proteins during secretion are short-lived, TAAs are thought to reside on the OM without forming complexes with other proteins after secretion. In this study, we aimed to clarify the interactions between an <em>Acinetobacter</em> TAA, AtaA, and a peptidoglycan (PG)-binding periplasmic protein, TpgA. Pull-down assays using recombinant proteins identified the interacting domains. X-ray crystallography at 2.6 Å resolution revealed an A3B3 heterohexameric complex structure composed of the N-terminal domain of TpgA and the transmembrane domain of AtaA. TpgA-N consists of two short α helices and three antiparallel β strands, yielding an ααβββ topology similar to BamE. However, the regions corresponding to BamE interfaces with BamA and BamD differ in TpgA-N. All-atom molecular dynamics simulations and mutational assays revealed that both electrostatic and hydrophobic interactions contribute to stable complex formation. Bioinformatic analyses indicate that the TAA-TpgA complex occurs in a wide range of species. These findings will contribute to a better understanding of TAAs and the cell envelope.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100155"},"PeriodicalIF":6.2,"publicationDate":"2025-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145219489","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":"AmpC β-lactamases: A key to antibiotic resistance in ESKAPE pathogens","authors":"Deeksha Pandey ,&nbsp;Isha Gupta ,&nbsp;Dinesh Gupta","doi":"10.1016/j.tcsw.2025.100154","DOIUrl":"10.1016/j.tcsw.2025.100154","url":null,"abstract":"<div><h3>Background</h3><div>AmpC β-lactamases (<em>blaAmpC</em>) are essential drivers of antimicrobial resistance (AMR) in ESKAPE pathogens, bacteria that cause hospital-acquired infections. Understanding AmpC enzymes is essential for uncovering resistance mechanisms and guiding antimicrobial strategies. We analyzed <em>blaAmpC</em> presence, genomic location, copy number, sequence variability, and evolutionary traits in ESKAPE pathogens.</div></div><div><h3>Results</h3><div>We identified 1790 AmpC enzymes in 4713 complete genomes, classified into nine enzyme groups. Consistent with known taxonomic profiles, no class C β-lactamases were detected in Gram-positive bacteria (<em>Staphylococcus aureus</em> and <em>Enterococcus faecium</em>). <em>Acinetobacter baumannii</em> exhibited the highest occurrence of class C β-lactamases, with <em>Enterobacter</em> spp. showing the second highest prevalence, followed by <em>Pseudomonas aeruginosa</em> and <em>Klebsiella pneumoniae</em>. The largest enzyme group, ADC was restricted to <em>A. baumannii</em>; similarly, ACC, ACT, CMH, and MIR to <em>Enterobacter</em> spp.; and PDC and PIB to <em>P. aeruginosa.</em> Phylogenetic analysis showed divergence among some groups and closer evolutionary relationships in others. Functional Motif analysis revealed conserved catalytic residues across all groups except PIB. Instead of the canonical YXN and KTG motifs, PIB contains YST and AQG variants, respectively. Because of these variations, PIB's ability to bind cephalosporins decreases while enhancing their activity against carbapenems.</div></div><div><h3>Conclusions</h3><div>We identified 1790 AmpC enzymes in nine distinct groups across ESKAPE pathogens, with species-specific distribution patterns and notable absence in Gram-positive bacteria. The PIB enzyme group demonstrated unique motif variants (YST/AQG) conferring carbapenem resistance, while other groups maintained conserved catalytic motifs. Phylogenetic analysis revealed evolutionary divergence and horizontal gene transfer potential, emphasizing the need for targeted therapeutic approaches against AmpC-mediated resistance.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100154"},"PeriodicalIF":6.2,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145219466","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":"Pathogenic diversity of Cryptococcus in Galleria mellonella extends beyond classical virulence factors","authors":"Bianca A.G. Sena ,&nbsp;Marlon D.M. Santos ,&nbsp;Cassia M. Souza ,&nbsp;Amanda C. Camillo-Andrade ,&nbsp;Haroldo C. de Oliveira ,&nbsp;Flavia C.G. Dos Reis ,&nbsp;Rafael F. Castelli ,&nbsp;Diogo Kuczera ,&nbsp;Henrique R.M. Antoniolli ,&nbsp;Hellen G.G. Santos ,&nbsp;Charley C. Staats ,&nbsp;Guilherme L. Sassaki ,&nbsp;Paulo C. Carvalho ,&nbsp;Marcio L. Rodrigues","doi":"10.1016/j.tcsw.2025.100153","DOIUrl":"10.1016/j.tcsw.2025.100153","url":null,"abstract":"<div><div>Pathogenic determinants in the <em>Cryptococcus</em> genus have been extensively studied, often using standard laboratory isolates. Here, we analyzed the virulence of ten <em>Cryptococcus</em> isolates from diverse sources, species, and genotypes. These isolates exhibited marked differences in their ability to colonize and kill the invertebrate host <em>Galleria mellonella</em>, as well as in their interactions with hemocytes. Capsule formation also varied widely among isolates, with no clear correlation between virulence in <em>G. mellonella</em> and source of isolation, species, fungal burden, capsule size, or interaction with larval hemocytes. To further investigate the basis of this pathogenic diversity, we selected two hypervirulent isolates (<em>C. deuterogattii</em> and <em>C. neoformans</em>) and two hypovirulent isolates (<em>C. gattii</em> and <em>C. neoformans</em>) for in-depth analysis. Differences in the induction of antimicrobial peptides during infection did not account for the observed variation in virulence. Genomic analysis of capsule-related genes, scanning electron microscopy of capsule morphology in vitro and in vivo, and nuclear magnetic resonance of the major capsular polysaccharide all revealed high variability among isolates, but none of these features correlated with virulence. Proteomic profiling of cellular extracts showed that virulent strains were enriched in proteins associated with oxidative processes. Supplementation with an antioxidant during infection increased the virulence of hypovirulent isolates in <em>G. mellonella</em>. These results reveal a high pathogenic diversity in <em>Cryptococcus</em> that goes beyond its classical virulence factors.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100153"},"PeriodicalIF":6.2,"publicationDate":"2025-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145157505","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":"Growth conditions shape the proteome and diversity of Neurospora crassa extracellular vesicles","authors":"Daniel A. Salgado-Bautista,&nbsp;Meritxell Riquelme","doi":"10.1016/j.tcsw.2025.100152","DOIUrl":"10.1016/j.tcsw.2025.100152","url":null,"abstract":"<div><div>Extracellular vesicles (EVs) are nanosized, lipid bilayer-enclosed particles secreted by all living organisms. While EV research has primarily focused on mammalian systems, fungal EVs are gaining attention for their biological significance. Here, we investigated how growth conditions influence the protein cargo of EVs produced by <em>Neurospora crassa</em>, a non-pathogenic filamentous fungus and well-established model organism. EVs were isolated from cultures grown on glucose for 16 h (G16) and on sucrose for 16 (S16) and 24 h (S24). Dynamic light scattering (DLS) revealed similar size distributions for S16 and S24 EVs (24–165 nm), whereas G16 EVs exhibited a broader range (32–825 nm). Across all conditions, particles &lt;50 nm were detected, potentially corresponding to mitochondrial-derived vesicles (MDVs) or exomeres, EV subtypes described in mammalian systems. Proteomic profiling identified 682 proteins in G16, 668 in S16, and a reduced set of 367 proteins in S24. Regardless of condition, EVs were enriched in proteins related to cell wall remodeling, protein synthesis, and carbohydrate metabolism. A high proportion of intracellular proteins confirms that fungal EVs participate in unconventional secretion. In addition, the detection of proteins involved in vesicle biogenesis and trafficking suggests that EV formation may also involve the classical secretory pathway. These findings demonstrate that EV composition and biogenesis in <em>N. crassa</em> are modulated by growth conditions and highlight the importance of physiological context in fungal EV research. Notably, the data reveal a diversity of EV types, including forms potentially unrelated to exosomes, expanding our understanding of fungal EV complexity.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100152"},"PeriodicalIF":6.2,"publicationDate":"2025-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145060082","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":"Localization characteristics of cell wall synthesis protein Wag31 and penicillin binding protein C in Clavibacter michiganensis","authors":"Chengxuan Yu,&nbsp;Xiaoli Xu,&nbsp;Jia Shi,&nbsp;Wenqing Chu,&nbsp;Na Jiang,&nbsp;Jianqiang Li,&nbsp;Laixin Luo","doi":"10.1016/j.tcsw.2025.100151","DOIUrl":"10.1016/j.tcsw.2025.100151","url":null,"abstract":"<div><div>CmWag31 is a member of the DivIVA family of proteins in <em>Clavibacter michiganensis</em>. The DivIVA family have been demonstrated to play a key role in the synthesis of cell wall peptidoglycan and cell division in most bacterial species. It has been previously confirmed that the <em>pbp</em>C (penicillin-binding protein C) deletion mutants affect bacterial division and cell wall synthesis. Based on the confirmation of the interaction between CmWag31 and CmPBPC, the present study conducted a systemic analysis on their localization characteristics. The results indicated that CmWag31 exhibited the capacity to interact with the transglycosylase (TG) and transpeptidase (TP) domain of CmPBPC, while CmPBPC only interacted with the NTD region of CmWag31. Co-localization analysis showed that CmWag31 co-localized with CmPBPC at the bacterial growth tips of <em>Clavibacter michiganensis</em> and <em>Escherichia coli</em>. The mutation of R19A, R19C, A99T, and A102T of CmWag31 resulted in abnormal localization in <em>Escherichia coli</em>. In the case of <em>C. michiganensis,</em> the CmWag31^A102T protein exhibited a diffuse localization, which is a departure from the polar localization of its wild type. The co-localization of the CmWag31^A102T mutation with CmPBPC exhibited discrepancies between <em>C. michiganensis</em> and <em>E. coli</em>. The diffused localization of CmWag31^A102T can be restored by overexpression of CmPBPC in <em>C. michiganensis</em>, yet this restoration is not observed in <em>E. coli</em>. This result indicates that CmPBPC from <em>C. michiganensis</em> may not fully excute their function in <em>E. coli</em> due to species-specific differences.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100151"},"PeriodicalIF":6.2,"publicationDate":"2025-08-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144932135","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":"Innate immune recognition of Mycobacterium tuberculosis: receptor engagement and inflammatory outcomes at the site of infection","authors":"N.E. Mvubu","doi":"10.1016/j.tcsw.2025.100150","DOIUrl":"10.1016/j.tcsw.2025.100150","url":null,"abstract":"<div><div><em>M. tuberculosis</em> is a notorious global pathogen responsible for over a million fatalities annually. It has been estimated that one-third of the world's population is latently infected with <em>M. tuberculosis</em>; however, only ∼10 million individuals develop an active disease annually. The innate immune defence system is the first to encounter the bacilli and initiates a cascade of events to protect the host from developing tuberculosis. Innate immune cells such as pulmonary epithelial cells, alveolar macrophages, and dendritic cells express Toll-like Receptors (TLRs), C-type Lectin Receptors (CLRs), NOD-like Receptors (NLRs), Scavenger Receptors, Surfactant Proteins, RIG-I–like Receptors (RLRs), Complement Receptors, and Fc Receptors upon exposure to <em>M. tuberculosis</em> Pathogen-Associated Molecular Patterns (PAMPs). The interaction between host Pathogen Recognition Receptors (PRRs) and <em>M. tuberculosis</em> PAMPs results in the activation of several signalling pathways that initiate an inflammatory response through the production of cytokines and chemokines at the site of infection. This Surface Feature manuscript provides an up-to-date report on the expression of host PRRs in pulmonary epithelial cells, alveolar macrophages and dendritic cells and their interactions with <em>M. tuberculosis</em> PAMPs to initiate an inflammatory response at the site of infection. Furthermore, this manuscript sheds light on the role of this inflammatory response as a “double-edged sword” in the fight against <em>M. tuberculosis</em> infection. Understanding these interactions provides a directive for host-directed therapies to modulate the innate immune response.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100150"},"PeriodicalIF":6.2,"publicationDate":"2025-08-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144878298","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":"Bacteriophages as an alternative strategy for the treatment of drug resistant bacterial infections: Current approaches and future perspectives","authors":"Abayeneh Girma","doi":"10.1016/j.tcsw.2025.100149","DOIUrl":"10.1016/j.tcsw.2025.100149","url":null,"abstract":"<div><div>A persistent increase in antimicrobial resistance presents a significant danger to global public health. The application of bactericidal phages that do not interfere with the body's natural flora becomes a promising approach to alternative treatments. This section offers an in-depth examination of the use of bacteriophage therapy in both laboratory and human trials for the treatment of specific bacterial infections. The benefits and hurdles of increasing the use of bacteriophages as a supplemental or alternative treatment for bacterial infections resistant to antibiotics are examined. The use of highly adaptable bacteriophage populations, combined with antibiotic chemical compounds, as molecular tools to combat rapidly evolving pathogenic bacteria in the host environment, presents significant virologic complexities. Pre-clinical studies, isolated clinical reports and a few randomized clinical trials have demonstrated that bacteriophages can be effective for treating bacterial infections that are resistant to multiple drugs. The capability of certain bacteriophages to reverse antibiotic resistance, as well as resistance to human complement and other bacteriophages seems to be a significant benefit of bacteriophage therapy, despite the predictable appearance of bacteriophage-resistant strains. Bacteriophages or specific products derived from them can improve antimicrobial effectiveness by decreasing bacteria's harmful properties through changes to fundamental bacterial structures, mainly their cell walls and membranes. Despite several ongoing issues regarding their practical use, it seems that bacteriophage-based treatments combined with antibiotics can serve as an effective solution to addressing the spread of antimicrobial resistance.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100149"},"PeriodicalIF":0.0,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144570124","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":"Sterols in plant biology – Advances in studying membrane dynamics","authors":"Paul Vogel ,&nbsp;Staffan Persson ,&nbsp;Guillermo Moreno-Pescador ,&nbsp;Lise C. Noack","doi":"10.1016/j.tcsw.2025.100147","DOIUrl":"10.1016/j.tcsw.2025.100147","url":null,"abstract":"<div><div>Plants sense their environment at the cell surface, i.e. the plasma membrane, where extracellular signals are perceived and transduced. Together with the cortical cytoskeleton and the cell wall, membrane lipids can influence these processes by acting on protein dynamics at the plasma membrane. Among these lipids, sterols regulate membrane fluidity and thus, protein functions. However, plant sterols are diverse in structure and particularly difficult to study due to technical limitations. Nevertheless, advances in sterol imaging, sterol-protein interaction studies, and sterol perturbation methods have resulted in a better understanding of their functions in plant development and physiology. Here we summarize the current knowledge and the latest breakthroughs, and discuss future challenges, in the field of plant sterol biology and cell surface organization.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"13 ","pages":"Article 100147"},"PeriodicalIF":0.0,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144189297","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":"Immunomodulatory function of chitosan is dependent on complement receptor 3","authors":"Jeanette Wagener ,&nbsp;Xiaowen Wang ,&nbsp;Katharina L. Becker ,&nbsp;Vishu Aimanianda ,&nbsp;Isabel Valsecchi ,&nbsp;Mark S. Gresnigt ,&nbsp;Mihai G. Netea ,&nbsp;Jean-Paul Latge ,&nbsp;Neil A.R. Gow ,&nbsp;Frank L. van de Veerdonk","doi":"10.1016/j.tcsw.2025.100146","DOIUrl":"10.1016/j.tcsw.2025.100146","url":null,"abstract":"<div><div>Chitosan, the deacetylated product of chitin, is a significant component of the cell walls of nearly all fungi. In contrast with the high level of attention paid to plant immune recognition of chitin and chitosan of plant pathogenic fungi we know much less about the mammalian immune system immune recognition of chitosan during infections by human pathogenic fungal species. Here we show that the mammalian β-integrin CR3 complement scavenger receptor, that is expressed on monocytes and macrophages, recognises chitosan from a range of fungal sources and that this leads to the secretion of IL-6, IL-1β and TNF. The secretion of these pro-inflammatory cytokines was dependent on the phagocytosis of chitosan. The co-provision of chitosan along with a peptide (Aspf2 from <em>Aspergillus fumigatus</em>) presented by the MHCII complex potentiated a Th response leading to IL-22 production. Fungal cell wall chitosan therefore activates both the innate and adaptive arms of the human immune system.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100146"},"PeriodicalIF":0.0,"publicationDate":"2025-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144231690","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":"Peptides in plant–microbe interactions: Functional diversity and pharmacological applications","authors":"Minghui Song ,&nbsp;Yunbing Zhou ,&nbsp;Gang Li ,&nbsp;Anna S. Barashkova ,&nbsp;Eugene A. Rogozhin ,&nbsp;Wenqiang Chang","doi":"10.1016/j.tcsw.2025.100145","DOIUrl":"10.1016/j.tcsw.2025.100145","url":null,"abstract":"<div><div>As dynamic interfaces governing molecular recognition and signal transduction, interactions between plants and microbes fundamentally shape ecosystem dynamics and evolutionary trajectories. This review summarizes peptides involved in plant–microbe interactions, emphasizing their diversity, biological functions mediated at the cell surface, pharmacological applications, and recent methodological advances in their discovery. Plant-derived peptides, including cysteine-rich peptides (NCRs, RALFs, DEFs, nsLTPs) and post-translationally modified peptides (CLEs, CEPs, GLV/RGF, PSKs), regulate symbiotic relationships and plant defenses. Endophyte-derived peptides, notably <em>Bacillus</em> lipopeptides (surfactins, fengycins, iturins), exhibit pathogen inhibition and plant growth promotion. Additionally, plant polypeptides such as lipid transfer proteins, hevein-like peptides, thionins, defensins, and snakins significantly enhance plant immunity through direct antimicrobial action and systemic resistance. Technological advancements in isolation techniques, multi-omics approaches, bioinformatics, and artificial intelligence have accelerated peptide discovery. However, challenges remain regarding functional characterization, peptide stability, production costs, and ecological impacts. Addressing these through interdisciplinary research and collaboration will promote practical applications of peptides in agriculture and medicine.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"13 ","pages":"Article 100145"},"PeriodicalIF":0.0,"publicationDate":"2025-05-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144070254","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}