FEBS Open BioPub Date : 2025-04-21DOI: 10.1002/2211-5463.70040
{"title":"Correction to “The first crystal structure of a family 45 glycosidehydrolase from a brown-rot fungus, Gloeophyllum trabeum GtCel45A”","authors":"","doi":"10.1002/2211-5463.70040","DOIUrl":"10.1002/2211-5463.70040","url":null,"abstract":"<p>\u0000 <span>Laura Okmane</span>, <span>Louise Fitkin</span>, <span>Mats Sandgren</span>, <span>Jerry Ståhlberg</span>. <span>The first crystal structure of a family 45 glycosidehydrolase from a brown-rot fungus, <i>Gloeophyllum trabeum</i> GtCel45A</span>. <i>FEBS Openbio.</i> <span>2024</span>; <span>14</span>: <span>505</span>-<span>514</span>. 10.1002/2211-5463.13774\u0000 </p><p>The authors include the following sentence in the acknowledgements section:</p><p>“We acknowledge the European Synchrotron Radiation Facility for provision of synchrotron radiation facilities and we would like to thank the staff of the ESRF and EMBL Grenoble for assistance and support in using beamline ID30B.”</p><p>The acknowledgements section has been updated as:</p><p>We thank Dr. Fernando Segato, University of São Paulo, Brazil, for providing spores of the <i>Gt</i>Cel45A expressing <i>A. nidulans</i> strain. This work was supported by the Swedish Research Council for Environment, Agricultural Sciences and Spatial Planning (Formas), Grant Number 2017–01130. We acknowledge the European Synchrotron Radiation Facility for provision of synchrotron radiation facilities and we would like to thank the staff of the ESRF and EMBL Grenoble for assistance and support in using beamline ID30B.</p>","PeriodicalId":12187,"journal":{"name":"FEBS Open Bio","volume":"15 6","pages":""},"PeriodicalIF":2.8,"publicationDate":"2025-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/2211-5463.70040","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144003847","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":"Matrigel inhibits elongation and drives endoderm differentiation in aggregates of mouse embryonic stem cells.","authors":"Atoosa Amel, Rachel Brown, Alexa Rabeling, Mubeen Goolam","doi":"10.1002/2211-5463.70044","DOIUrl":"https://doi.org/10.1002/2211-5463.70044","url":null,"abstract":"<p><p>Modelling peri-implantation mammalian development using the self-organising properties of stem cells is a rapidly growing field that has advanced our understanding of cell fate decisions occurring in the early embryo. Matrigel, a basement membrane matrix, is a critical substrate used in various protocols for its efficacy in promoting stem cell growth and self-organisation. However, its role in driving stem cell lineage commitment, and whether this effect is driven by biochemical or physical cues, is not currently clear. Here, we grow embryoid bodies in suspension, Matrigel and agarose, an inert polysaccharide, to attempt to decouple the physical and biochemical roles of Matrigel and better understand how it drives stem cell differentiation. We use a combination of light microscopy, quantitative PCR and immunostaining to investigate gene and protein changes in our different culture conditions. We show that stem cell aggregates in Matrigel are hindered in their ability to elongate compared with those grown in agarose or in suspension, indicating that prohibitive role in self-organisation. Aggregates in Matrigel are also driven to differentiate into endoderm, with ectoderm differentiation inhibited. Furthermore, these effects are not due to the physical presence of Matrigel, as the same effects are not witnessed in aggregates grown in agarose. Our results thus indicate that Matrigel has a significant and complex effect on the differentiation and morphology of embryoid bodies.</p>","PeriodicalId":12187,"journal":{"name":"FEBS Open Bio","volume":" ","pages":""},"PeriodicalIF":2.8,"publicationDate":"2025-04-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143958483","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}
FEBS Open BioPub Date : 2025-04-16DOI: 10.1002/2211-5463.70028
Jaehoon Lee, Gi-Bang Koo, Jihye Park, Byung-Cheol Han, Mijin Kwon, Seung-Ho Lee
{"title":"Downregulation of O-GlcNAcylation enhances etoposide-induced p53-mediated apoptosis in HepG2 human liver cancer cells.","authors":"Jaehoon Lee, Gi-Bang Koo, Jihye Park, Byung-Cheol Han, Mijin Kwon, Seung-Ho Lee","doi":"10.1002/2211-5463.70028","DOIUrl":"https://doi.org/10.1002/2211-5463.70028","url":null,"abstract":"<p><p>Etoposide, an anticancer drug that inhibits topoisomerase II, is commonly used in combination chemotherapy. However, the impact of O-GlcNAcylation regulation on etoposide's anticancer effects has rarely been investigated. This study evaluated the effect of etoposide on cellular O-GlcNAcylation and whether modulating this process enhances etoposide-induced apoptosis. O-GlcNAc expression was measured after 24 h of etoposide treatment, and the effect of O-GlcNAc transferase (OGT) inhibition by OSMI-1 on etoposide's anticancer activity in HepG2 human liver cancer cells was quantitatively analyzed. Additionally, molecular analyses were used to confirm that the observed effects were mediated by p53-induced apoptosis. Etoposide reduced O-GlcNAcylation in a dose-dependent manner without directly interacting with OGT. Cotreatment with 20 μm of OSMI-1 lowered the IC<sub>50</sub> value for cell viability by approximately 1.64-fold to 60.68 μm and increased the EC<sub>50</sub> value for cytotoxicity by around 4.07-fold to 43.41 μm. Furthermore, this synergistic effect was linked to the activation of the p53/caspase-3/PARP1 pathway. These findings suggest that downregulating O-GlcNAcylation may enhance the efficacy of etoposide-based chemotherapy and help overcome tumor resistance.</p>","PeriodicalId":12187,"journal":{"name":"FEBS Open Bio","volume":" ","pages":""},"PeriodicalIF":2.8,"publicationDate":"2025-04-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143958480","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}
FEBS Open BioPub Date : 2025-04-16DOI: 10.1002/2211-5463.70022
Richard Huang, Lynn Kee, Alexander Gont, Jalna Meens, Fraser G Ferens, Meredith S Irwin, Laurie Ailles, Scott A Yuzwa, Claire M Robinson, Michael Ohh
{"title":"Comparative single-cell transcriptomic profiling of patient-derived renal carcinoma cells in cellular and animal models of kidney cancer.","authors":"Richard Huang, Lynn Kee, Alexander Gont, Jalna Meens, Fraser G Ferens, Meredith S Irwin, Laurie Ailles, Scott A Yuzwa, Claire M Robinson, Michael Ohh","doi":"10.1002/2211-5463.70022","DOIUrl":"https://doi.org/10.1002/2211-5463.70022","url":null,"abstract":"<p><p>Clear cell renal cell carcinoma (ccRCC) is the most common form of kidney cancer that often displays resistance to conventional cancer therapies, including chemotherapy and radiation therapy. Targeted treatments, including immunotherapies and small molecular inhibitors, have been associated with improved outcomes. However, variations in the patient response and the development of resistance suggest that more models that better recapitulate the pathogenesis and metastatic mechanisms of ccRCC are required to improve our understanding and disease management. Here, we examined the transcriptional landscapes of in vitro cell culture as well as in vivo orthotopic and metastatic NOD/SCID-γ mouse models of ccRCC using a single patient-derived RCC243 cell line to allow unambiguous comparison between models. In our mouse model assays, RCC243 cells formed metastatic tumors, and all tumors retained clear cell morphology irrespective of model type. Notably, gene expression profiles differed markedly between the RCC243 tumor models-cell culture, orthotopic tumors, and metastatic tumors-suggesting an impact of the experimental model system and whether the tumor was orthotopic or metastatic. Furthermore, we found conserved prognostic markers between RCC243 tumor models and human ccRCC patient datasets, and genes upregulated in metastatic RCC243 were associated with worse patient outcomes.</p>","PeriodicalId":12187,"journal":{"name":"FEBS Open Bio","volume":" ","pages":""},"PeriodicalIF":2.8,"publicationDate":"2025-04-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143999228","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}
FEBS Open BioPub Date : 2025-04-15DOI: 10.1002/2211-5463.70005
Elena Perla, Faiza Abbas, Luigia Rossi, Mauro Magnani, Sara Biagiotti
{"title":"Red blood cells could protect miRNAs from degradation or loss thanks to Argonaute 2 binding","authors":"Elena Perla, Faiza Abbas, Luigia Rossi, Mauro Magnani, Sara Biagiotti","doi":"10.1002/2211-5463.70005","DOIUrl":"https://doi.org/10.1002/2211-5463.70005","url":null,"abstract":"<p>Red blood cells (RBCs) have emerged as reservoirs of microRNAs (miRNAs) in the circulatory system, challenging the traditional view of their nucleic acid absence. This study investigates the miRNA profiles and stability of both native and engineered RBCs. We demonstrate that RBCs are rich in miRNAs, which remain stable under physiological conditions, likely due to their association with Ago2, a key RNA-binding protein. The stability and retention of miRNAs persist even after hypotonic dialysis used for RBC engineering. These findings underline the potential of RBCs as miRNA carriers for therapeutic applications and as a foundation for RNA-based delivery systems. Such advancements could redefine their role in transfusion medicine and advanced RNA therapies.</p>","PeriodicalId":12187,"journal":{"name":"FEBS Open Bio","volume":"15 5","pages":"810-821"},"PeriodicalIF":2.8,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/2211-5463.70005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143905345","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":"Enhanced discovery of bacterial laccase-like multicopper oxidase through computer simulation and metagenomic analysis of industrial wastewater.","authors":"Ting Cui, Ariel Kushmaro, Hana Barak, Anja Poehlein, Rolf Daniel, Hans-Jürgen Mägert","doi":"10.1002/2211-5463.70037","DOIUrl":"https://doi.org/10.1002/2211-5463.70037","url":null,"abstract":"<p><p>Laccases belong to the superfamily of multicopper oxidases (MCO), a group of enzymes with the ability to reduce oxygen to water in a reaction without producing harmful byproducts. Laccase activity is influenced by many factors, such as structure; the number, location and binding status of copper ions; and the substrate-binding status. A large number of sequences that have not been experimentally characterized yet have been annotated as laccases. However, the biological functions of the characterized MCOs are considered to vary, and the substrate spectrum overlaps with that of other MCOs. Here, we identified 34 putative bacterial laccase sequences from metagenome data for industrial wastewater. We used machine-learning tools to screen enzymes with laccase activity by combining the T1 copper-binding capacity, the overall copper-binding capacity and the substrate-binding capacity. We also used the software comparisons to remove sequences with large discrepancies between different software applications. Three-dimensional structures of identified enzymes were predicted using alphafold, the positions of metal ions within the proteins were predicted by metal3d and autodock-vina, and their docking with ABTS [i.e. 2,2'-azinobis(3‑ethylbenzo-6‑thiazolinesulfonic acid)] as a substrate was predicted by rosetta and autodock-vina. Based on the docking results, we selected 10 high-scoring proteins, two low-scoring proteins and one composite protein for expression using the pET-21d (+) vector. In line with our predictions, all selected high-scoring proteins exhibited activity towards ABTS. Overall, we describe a method for discovering and designing novel bacterial laccase-like multicopper oxidases, offering increased possibilities for the degradation of various harmful components derived from environmental pollution.</p>","PeriodicalId":12187,"journal":{"name":"FEBS Open Bio","volume":" ","pages":""},"PeriodicalIF":2.8,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143984836","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}
FEBS Open BioPub Date : 2025-04-15DOI: 10.1002/2211-5463.70042
Ellen T Tran, Ruchi A Patel, Amogh Chariyamane, Ratna B Ray
{"title":"Long non-coding RNAs as therapeutic targets in head and neck squamous cell carcinoma and clinical application.","authors":"Ellen T Tran, Ruchi A Patel, Amogh Chariyamane, Ratna B Ray","doi":"10.1002/2211-5463.70042","DOIUrl":"https://doi.org/10.1002/2211-5463.70042","url":null,"abstract":"<p><p>Head and neck squamous cell carcinoma (HNSCC) is a major global health burden, often associated with poor prognosis and limited therapeutic options. Long non-coding RNAs (lncRNAs), a diverse group of non-coding RNA molecules > 200 nucleotides in length, have emerged as critical regulators in the pathogenesis of HNSCC. This review summarizes the mechanisms through which certain lncRNAs regulate chromatin modification, mRNA splicing, and interactions with RNA-binding proteins and contribute to the development and progression of HNSCC. Interaction of lncRNAs with key oncogenic pathways, such as PI3K/AKT and Wnt/β-catenin, highlights their importance in tumor progression. The role of lncRNAs, such as ELDR, MALAT1, NEAT1, HOTAIR, and UCA1, which promote cell proliferation, metastasis, immune evasion, and therapy resistance is discussed. Moreover, several lncRNAs are being evaluated in clinical trials for their potential as biomarkers, reflecting their clinical significance. We further address the challenges and opportunities for targeting lncRNA therapeutically, highlighting the promise of lncRNA-based interventions for personalized cancer treatment. Gaining insight into the function of lncRNAs in HNSCC could pave the way for novel therapeutic strategies to potentially improve patient outcomes.</p>","PeriodicalId":12187,"journal":{"name":"FEBS Open Bio","volume":" ","pages":""},"PeriodicalIF":2.8,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144005348","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}
FEBS Open BioPub Date : 2025-04-15DOI: 10.1002/2211-5463.70038
Eloïse M Paulet, Julia Bartoli, Atakan Kabtan, Chloé M Piras, Audrey C Tempier, Eric Cascales, Julie P Viala
{"title":"Comparative study of adenosine 3'-pyrophosphokinase domains of MuF polymorphic toxins.","authors":"Eloïse M Paulet, Julia Bartoli, Atakan Kabtan, Chloé M Piras, Audrey C Tempier, Eric Cascales, Julie P Viala","doi":"10.1002/2211-5463.70038","DOIUrl":"https://doi.org/10.1002/2211-5463.70038","url":null,"abstract":"<p><p>Polymorphic toxins (PT) are multidomain proteins used for interbacterial competition and pathogenesis. The N-terminal domain of PT specifies the mode of transport and names the family, while the variable C-terminal domain carries the toxic activity, which can be counteracted by immunity proteins that protect the PT-producing bacterium. The MuF family of polymorphic toxins is specifically associated with temperate phages, and our recent work showed that the C-terminal domain of a MuF toxin encoded by a Streptococcus pneumoniae prophage carries adenosine 3'-pyrophosphokinase activity. This type of toxin, which combines a MuF N-terminal domain and an adenosine 3'-pyrophosphokinase C-terminal domain, is called Apk2 for adenosine 3'-pyrophosphokinase family 2. Here, we extend the characterization of this novel family of toxins by providing information on two new members encoded by prophages of Mannheimia haemolytica and Pasteurella multocida. Production of their adenosine 3'-pyrophosphokinase domains (Apk2<sub>tox</sub>) in the heterologous host Escherichia coli revealed different levels of toxicity, essentially due to their stability. In vitro assays with the purified M. haemolytica Apk2<sub>tox</sub> domain demonstrated that, identically to that of S. pneumoniae, it exclusively produces (p)ppApp from ATP. The role of immunity proteins and their interchangeability in cross-protection and protein-protein interaction assays was tested. While the immunity proteins that hydrolyse pppApp to ATP are interchangeable, those that inhibit the toxin by protein-protein interaction are mainly active against their intrastrain partner. Overall, this study highlights the conserved features of these enzymatic domains, such as their toxicity, their specific activity toward ATP, and their universal and specific immunities.</p>","PeriodicalId":12187,"journal":{"name":"FEBS Open Bio","volume":" ","pages":""},"PeriodicalIF":2.8,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143976598","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}
FEBS Open BioPub Date : 2025-04-15DOI: 10.1002/2211-5463.70041
Lonneke Hoffmanns, Dennis Svedberg, André Mateus
{"title":"Protein O-glycosylation in the Bacteroidota phylum.","authors":"Lonneke Hoffmanns, Dennis Svedberg, André Mateus","doi":"10.1002/2211-5463.70041","DOIUrl":"https://doi.org/10.1002/2211-5463.70041","url":null,"abstract":"<p><p>Glycans play crucial roles in bacteria, such as providing structural integrity or enabling interactions with the ecosystem. They can be linked to lipids, peptides, or proteins. In proteins, they modify either asparagine (N-glycosylation) or serine or threonine (O-glycosylation). Species of the Bacteroidota phylum, a major component of the human microbiome and marine and soil ecosystems, have a unique type of O-glycosylation that modifies multiple noncytoplasmic proteins containing a specific amino acid sequence. Only a small number of species have currently been characterized, but within one species, generally all proteins are modified with the same glycan structure. Most species share a common inner part but differ in the sugar composition and branching of the outer part of their glycan. This suggests that the biosynthesis of the glycan occurs in two separate steps. Both the inner core and the outer glycan are likely assembled from nucleotide-activated monosaccharides on undecaprenyl phosphate on the cytoplasmic side of the inner membrane, prior to being flipped to the periplasm and transferred to the protein. A genomic locus responsible for the biosynthesis of the outer glycan has been identified, containing some conserved genes across species. Despite substantial progress in the characterization of this O-glycosylation system, its function, the overall diversity of glycan structures across the phylum, and the complete biosynthetic pathway remain mostly unknown. Due to the importance of this group of species for the human gut microbiome, elucidating these aspects can open up strategies to modulate the composition of the microbiome community toward a healthy state.</p>","PeriodicalId":12187,"journal":{"name":"FEBS Open Bio","volume":" ","pages":""},"PeriodicalIF":2.8,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144001274","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":"KCS1 and VIP1, the genes encoding yeast phosphoinositol pyrophosphate synthases, are required for Ca<sup>2+</sup>-mediated response to dimethylsulfoxide (DMSO).","authors":"Larisa Ioana Gogianu, Lavinia Liliana Ruta, Claudia Valentina Popa, Simona Ghenea, Ileana Cornelia Farcasanu","doi":"10.1002/2211-5463.70039","DOIUrl":"https://doi.org/10.1002/2211-5463.70039","url":null,"abstract":"<p><p>Dimethylsulfoxide (DMSO) is widely used as a solvent or as a carrier when screening for biologic activity of various chemicals, but results need to be interpreted carefully due to its intrinsic toxicity. DMSO has been previously observed to impair the growth of yeast cells defective in calcium movement across cellular membranes and in phosphoinositol pyrophosphate synthases. Here, we set out to investigate the Ca<sup>2+</sup>-mediated response to DMSO in Saccharomyces cerevisiae. The cell exposure to DMSO was signaled by a two-phase cytosolic Ca<sup>2+</sup> wave that was dependent on Mid1, a subunit of the Cch1/Mid1 Ca<sup>2+</sup> channel located at the plasma membrane. While the vacuolar Ca<sup>2+</sup> channel Trpy1 also contributed by releasing Ca<sup>2+</sup> from the vacuole, the immediate cell response to DMSO exposure depended on the external Ca<sup>2+</sup> imported into the cell through Cch1/Mid1. A chemogenomic screen previously performed on a collection of yeast knockout mutants identified the two phosphoinositol pyrophosphate synthases Kcs1 and Vip1 as determinants for yeast tolerance to DMSO. Deletion of KCS1 or VIP1 genes suppressed the DMSO-induced Ca<sup>2+</sup> response, suggesting that both Ca<sup>2+</sup> and phosphoinositol pyrophosphate signaling contribute to cell adaptation under DMSO stress.</p>","PeriodicalId":12187,"journal":{"name":"FEBS Open Bio","volume":" ","pages":""},"PeriodicalIF":2.8,"publicationDate":"2025-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143974348","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}