microLife最新文献

{"title":"Cyclic di-AMP, a multifaceted regulator of central metabolism and osmolyte homeostasis in <i>Listeria monocytogenes</i>.","authors":"Inge Schwedt,&nbsp;Mengyi Wang,&nbsp;Johannes Gibhardt,&nbsp;Fabian M Commichau","doi":"10.1093/femsml/uqad005","DOIUrl":"https://doi.org/10.1093/femsml/uqad005","url":null,"abstract":"<p><p>Cyclic di-AMP is an emerging second messenger that is synthesized by many archaea and bacteria, including the Gram-positive pathogenic bacterium <i>Listeria monocytogenes. Listeria monocytogenes</i> played a crucial role in elucidating the essential function of c-di-AMP, thereby becoming a model system for studying c-di-AMP metabolism and the influence of the nucleotide on cell physiology. c-di-AMP is synthesized by a diadenylate cyclase and degraded by two phosphodiesterases. To date, eight c-di-AMP receptor proteins have been identified in <i>L. monocytogenes</i>, including one that indirectly controls the uptake of osmotically active peptides and thus the cellular turgor. The functions of two c-di-AMP-receptor proteins still need to be elucidated. Here, we provide an overview of c-di-AMP signalling in <i>L. monocytogenes</i> and highlight the main differences compared to the other established model systems in which c-di-AMP metabolism is investigated. Moreover, we discuss the most important questions that need to be answered to fully understand the role of c-di-AMP in osmoregulation and in the control of central metabolism.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"4 ","pages":"uqad005"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/47/d0/uqad005.PMC10117814.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9516276","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}

{"title":"The New Microbiology: an international lecture course on the island of Spetses.","authors":"Pascale Cossart,&nbsp;Roberto Kolter,&nbsp;Bruno Lemaitre,&nbsp;Athanasios Typas","doi":"10.1093/femsml/uqac026","DOIUrl":"https://doi.org/10.1093/femsml/uqac026","url":null,"abstract":"<p><p>In September 2022, an international summer course entitled 'The new microbiology' took place in Greece, on the island of Spetses. The organizers aimed to highlight the spectacular advances and the renaissance occurring in Microbiology, driven by developments in genomics, proteomics, imaging techniques, and bioinformatics. Combinations of these advances allow for single cell analyses, rapid and relatively inexpensive metagenomic and transcriptomic data analyses and comparisons, visualization of previously unsuspected mechanisms, and large-scale studies. A 'New Microbiology' is emerging which allows studies that address the critical roles of microbes in health and disease, in humans, animals, and the environment. The concept of one health is now transforming microbiology. The goal of the course was to discuss all these topics with members of the new generation of microbiologists all of whom were highly motivated and fully receptive.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"4 ","pages":"uqac026"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10212125/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9545272","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}

{"title":"Dear <i>Listeria</i>, what is your preferred niche?","authors":"Sarah Wettstadt","doi":"10.1093/femsml/uqad004","DOIUrl":"https://doi.org/10.1093/femsml/uqad004","url":null,"abstract":"Seeing Pascale Cossart in one of her many science outreach videos online, one can usually recognize two major features: a lot of scientific expertise and a big smile. Both stem from her experience of being a microbiologist and her passion for the field. After her PhD in chemistry at the University of Paris, Pascale came across the microbial world by studying protein–DNA interactions. She learned about microbial physiology and started to study how microbes interact with their hosts. She then got more and more fascinated by microbes and the fact that they ‘are not only everywhere, but they are absolutely critical for the equilibrium of the human body, animals, plants, insects and the environment’. From early on, Pascale decided to focus on the Gram-positive pathogen Listeria monocytogenes, which can live silently in the gastro-intestinal tract of some healthy humans. However, in immuno-compromised people, newborns, elderly, or pregnant women, it can lead to severe infections and meningitis, encephalitis, or even miscarriage. Pascale was the first to sequence the hlyA gene, which encodes listeriolysin O—a major virulence factor— in Listeria. Together with her team, Pascale then discovered internalin, the protein that allows Listeria to enter mammalian cells, as well as its receptor on mammalian cells, the protein E-cadherin. She then became interested in how Listeria would enter host cells, and she identified many important key molecules whose role in bacterial cell entry had never been suspected. Her work on Listeria specificity for human cells versus murine was remarkable and led to the generation of a transgenic animal model for human listeriosis. As an early-stage Professor at the Institut Pasteur in Paris, Pascale made a discovery that ‘triggered a whole tsunami in the field’. She discovered the mechanisms of how L. monocytogenes uses the actin of a host to move and spread across tissue. Once inside the cytosol of the host cell, the bacterial surface protein ActA nucleates and polymerizes actin and recruits other proteins to these actin filaments (Kocks et al. 1992). Through this polymerization process, ActA triggers the formation of long actin tails and ultimately of bacteria-containing membrane protrusions. These help L. monocytogenes contact and enter neighbouring cells without ever leaving the host cytosol (Lecuit et al. 2001). Thanks to growing techniques like fluorescence microscopy, Pascale and her team managed to visualize these microbe-induced processes and establish herself in the field of infection microbiology.","PeriodicalId":74189,"journal":{"name":"microLife","volume":"4 ","pages":"uqad004"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/1d/26/uqad004.PMC10117850.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9516278","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}

{"title":"From an Hsp90 - binding protein to a peptide drug.","authors":"Aparna Viswanathan Ammanath,&nbsp;Anders Jarneborn,&nbsp;Minh-Thu Nguyen,&nbsp;Laura Wessling,&nbsp;Paula Tribelli,&nbsp;Mulugeta Nega,&nbsp;Christian Beck,&nbsp;Arif Luqman,&nbsp;Khaled A Selim,&nbsp;Hubert Kalbacher,&nbsp;Boris Macek,&nbsp;Sandra Beer Hammer,&nbsp;Tao Jin,&nbsp;Friedrich Götz","doi":"10.1093/femsml/uqac023","DOIUrl":"https://doi.org/10.1093/femsml/uqac023","url":null,"abstract":"<p><p>The Lpl proteins represent a class of lipoproteins that was first described in the opportunistic bacterial pathogen <i>Staphylococcus aureus</i>, where they contribute to pathogenicity by enhancing F-actin levels of host epithelial cells and thereby increasing <i>S. aureus</i> internalization. The model Lpl protein, Lpl1 was shown to interact with the human heat shock proteins Hsp90α and Hsp90ß, suggesting that this interaction may trigger all observed activities. Here we synthesized Lpl1-derived peptides of different lengths and identified two overlapping peptides, namely, L13 and L15, which interacted with Hsp90α. Unlike Lpl1, the two peptides not only decreased F-actin levels and <i>S. aureus</i> internalization in epithelial cells but they also decreased phagocytosis by human CD14⁺ monocytes. The well-known Hsp90 inhibitor, geldanamycin, showed a similar effect. The peptides not only interacted directly with Hsp90α, but also with the mother protein Lpl1. While L15 and L13 significantly decreased lethality of <i>S. aureus</i> bacteremia in an insect model, geldanamycin did not. In a mouse bacteremia model L15 was found to significantly decreased weight loss and lethality. Although the molecular bases of the L15 effect is still elusive, <i>in vitro</i> data indicate that simultaneous treatment of host immune cells with L15 or L13 and <i>S. aureus</i> significantly increase IL-6 production. L15 and L13 represent not antibiotics but they cause a significant reduction in virulence of multidrug-resistant <i>S. aureus</i> strains in <i>in vivo</i> models. In this capacity, they can be an important drug alone or additive with other agents.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"4 ","pages":"uqac023"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10117725/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9518991","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}

{"title":"Different culture media and purification methods unveil the core proteome of <i>Propionibacterium freudenreichii</i>-derived extracellular vesicles.","authors":"Vinícius de Rezende Rodovalho,&nbsp;Brenda Silva Rosa da Luz,&nbsp;Aurélie Nicolas,&nbsp;Julien Jardin,&nbsp;Valérie Briard-Bion,&nbsp;Edson Luiz Folador,&nbsp;Anderson Rodrigues Santos,&nbsp;Gwénaël Jan,&nbsp;Yves Le Loir,&nbsp;Vasco Ariston de Carvalho Azevedo,&nbsp;Éric Guédon","doi":"10.1093/femsml/uqad029","DOIUrl":"https://doi.org/10.1093/femsml/uqad029","url":null,"abstract":"<p><p>Bacterial extracellular vesicles (EVs) are natural lipidic nanoparticles implicated in intercellular communication. Although EV research focused mainly on pathogens, the interest in probiotic-derived EVs is now rising. One example is <i>Propionibacterium freudenreichii</i>, which produces EVs with anti-inflammatory effects on human epithelial cells. Our previous study with <i>P. freudenreichii</i> showed that EVs purified by size exclusion chromatography (SEC) displayed variations in protein content according to bacterial growth conditions. Considering these content variations, we hypothesized that a comparative proteomic analysis of EVs recovered in different conditions would elucidate whether a representative vesicular proteome existed, possibly providing a robust proteome dataset for further analysis. Therefore, <i>P. freudenreichii</i> was grown in two culture media, and EVs were purified by sucrose density gradient ultracentrifugation (UC). Microscopic and size characterization confirmed EV purification, while shotgun proteomics unveiled that they carried a diverse set of proteins. A comparative analysis of the protein content of UC- and SEC-derived EVs, isolated from cultures either in UF (cow milk ultrafiltrate medium) or YEL (laboratory yeast extract lactate medium), showed that EVs from all these conditions shared 308 proteins. This EV core proteome was notably enriched in proteins related to immunomodulation. Moreover, it showed distinctive features, including highly interacting proteins, compositional biases for some specific amino acids, and other biochemical parameters. Overall, this work broadens the toolset for the purification of <i>P. freudenreichii</i>-derived EVs, identifies a representative vesicular proteome, and enumerates conserved features in vesicular proteins. These results hold the potential for providing candidate biomarkers of purification quality, and insights into the mechanisms of EV biogenesis and cargo sorting.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"4 ","pages":"uqad029"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/57/2b/uqad029.PMC10265600.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9656045","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}

{"title":"The eukaryome of African children is influenced by geographic location, gut biogeography, and nutritional status.","authors":"Pascale Vonaesch,&nbsp;Vincent Billy,&nbsp;Allison E Mann,&nbsp;Evan Morien,&nbsp;Azimdine Habib,&nbsp;Jean-Marc Collard,&nbsp;Michel Dédé,&nbsp;Nathalie Kapel,&nbsp;Philippe J Sansonetti,&nbsp;Laura Wegener Parfrey","doi":"10.1093/femsml/uqad033","DOIUrl":"https://doi.org/10.1093/femsml/uqad033","url":null,"abstract":"<p><p>Eukaryotes have historically been studied as parasites, but recent evidence suggests they may be indicators of a healthy gut ecosystem. Here, we describe the eukaryome along the gastrointestinal tract of children aged 2-5 years and test for associations with clinical factors such as anaemia, intestinal inflammation, chronic undernutrition, and age. Children were enrolled from December 2016 to May 2018 in Bangui, Central African Republic and Antananarivo, Madagascar. We analyzed a total of 1104 samples representing 212 gastric, 187 duodenal, and 705 fecal samples using a metabarcoding approach targeting the full ITS2 region for fungi, and the V4 hypervariable region of the 18S rRNA gene for the overall eukaryome. Roughly, half of all fecal samples showed microeukaryotic reads. We find high intersubject variability, only a handful of taxa that are likely residents of the gastrointestinal tract, and frequent co-occurrence of eukaryotes within an individual. We also find that the eukaryome differs between the stomach, duodenum, and feces and is strongly influenced by country of origin. Our data show trends towards higher levels of <i>Fusarium equiseti</i>, a mycotoxin producing fungus, and lower levels of the protist <i>Blastocystis</i> in stunted children compared to nonstunted controls. Overall, the eukaryome is poorly correlated with clinical variables. Our study is of one of the largest cohorts analyzing the human intestinal eukaryome to date and the first to compare the eukaryome across different compartments of the gastrointestinal tract. Our results highlight the importance of studying populations across the world to uncover common features of the eukaryome in health.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"4 ","pages":"uqad033"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10481997/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10186521","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}

{"title":"The symbolic power of nucleotide second messengers - or how prokaryotes link sensing and responding to their outside world.","authors":"Regine Hengge","doi":"10.1093/femsml/uqad036","DOIUrl":"https://doi.org/10.1093/femsml/uqad036","url":null,"abstract":"Editorial Nucleotide second messengers are k e y components of molecular information processing pathways and networks that allow bacteria and archaea to navigate and adapt to an e v er c hanging exter-nal world. Being produced and/or degraded by often membrane-associated enzymes that can sense and react to environmental or cellular changes, the intracellular second messenger molecules are in turn sensed by cellular effectors—usually proteins or protein domains , sometimes ribos witc hes—that trigger dir ectl y associated target systems to produce specific molecular reactions. T hus , second messengers are informational molecules, which stand as intracellular molecular symbols or signs for something else, namel y, some potentiall y life-thr eatening condition, and which inform the executive machinery of the cell that an a ppr o-priate ada ptiv e r esponse is ur gentl y needed. It is pr obabl y not accidental that two major classes of intracellular molecules with symbolic functions are both deri vati ves of n ucleotides although there is a clear functional division of labour between them. The nucleotide polymers DNA and RNA function in the stor a ge and ef-fectuation of genetic information that has to be maintained over long times. By constrast, nucleotide second messengers are tiny RNAs, which consist only of one or two, often cyclic nucleotides, that have to transiently represent environmental or cellular states in real time . T his requires high dynamics of second messenger pr oduction and degr adation by specific enzymes whose expr es-sion and activity has to be tightl y contr olled by sensory input. It is likely that second messenger signaling is the evolutionary oldest form of molecular information processing, rudimentary forms of which ma y ha ve already evolved in the early RN A w orld. The cur-r ent pictur e of second messenger signaling in Pr okary otes, ho we","PeriodicalId":74189,"journal":{"name":"microLife","volume":"4 ","pages":"uqad036"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/66/13/uqad036.PMC10449370.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10099795","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}

{"title":"The role of site-2-proteases in bacteria: a review on physiology, virulence, and therapeutic potential.","authors":"Sofie S Kristensen,&nbsp;Dzung B Diep,&nbsp;Morten Kjos,&nbsp;Geir Mathiesen","doi":"10.1093/femsml/uqad025","DOIUrl":"https://doi.org/10.1093/femsml/uqad025","url":null,"abstract":"<p><p>Site-2-proteases are a class of intramembrane proteases involved in regulated intramembrane proteolysis. Regulated intramembrane proteolysis is a highly conserved signaling mechanism that commonly involves sequential digestion of an anti-sigma factor by a site-1- and site-2-protease in response to external stimuli, resulting in an adaptive transcriptional response. Variation of this signaling cascade continues to emerge as the role of site-2-proteases in bacteria continues to be explored. Site-2-proteases are highly conserved among bacteria and play a key role in multiple processes, including iron uptake, stress response, and pheromone production. Additionally, an increasing number of site-2-proteases have been found to play a pivotal role in the virulence properties of multiple human pathogens, such as alginate production in <i>Pseudomonas aeruginosa</i>, toxin production in <i>Vibrio cholerae</i>, resistance to lysozyme in enterococci and antimicrobials in several <i>Bacillus</i> spp, and cell-envelope lipid composition in <i>Mycobacterium tuberculosis</i>. The prominent role of site-2-proteases in bacterial pathogenicity highlights the potential of site-2-proteases as novel targets for therapeutic intervention. In this review, we summarize the role of site-2-proteases in bacterial physiology and virulence, as well as evaluate the therapeutic potential of site-2-proteases.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"4 ","pages":"uqad025"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10202637/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9518993","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}

{"title":"Characterization of a soluble library of the <i>Pseudomonas aeruginosa</i> PAO1 membrane proteome with emphasis on c-di-GMP turnover enzymes.","authors":"Anna Scherhag,&nbsp;Markus Räschle,&nbsp;Niklas Unbehend,&nbsp;Benedikt Venn,&nbsp;David Glueck,&nbsp;Timo Mühlhaus,&nbsp;Sandro Keller,&nbsp;Eugenio Pérez Patallo,&nbsp;Susanne Zehner,&nbsp;Nicole Frankenberg-Dinkel","doi":"10.1093/femsml/uqad028","DOIUrl":"https://doi.org/10.1093/femsml/uqad028","url":null,"abstract":"<p><p>Studies of protein-protein interactions in membranes are very important to fully understand the biological function of a cell. The extraction of proteins from the native membrane environment is a critical step in the preparation of membrane proteins that might affect the stability of protein complexes. In this work, we used the amphiphilic diisobutylene/maleic acid copolymer to extract the membrane proteome of the opportunistic pathogen <i>Pseudomonas aeruginosa</i>, thereby creating a soluble membrane-protein library within a native-like lipid-bilayer environment. Size fractionation of nanodisc-embedded proteins and subsequent mass spectrometry enabled the identification of 3358 proteins. The native membrane-protein library showed a very good overall coverage compared to previous proteome data. The pattern of size fractionation indicated that protein complexes were preserved in the library. More than 20 previously described complexes, e.g. the SecYEG and Pili complexes, were identified and analyzed for coelution. Although the mass-spectrometric dataset alone did not reveal new protein complexes, combining pulldown assays with mass spectrometry was successful in identifying new protein interactions in the native membrane-protein library. Thus, we identified several candidate proteins for interactions with the membrane phosphodiesterase NbdA, a member of the c-di-GMP network. We confirmed the candidate proteins CzcR, PA4200, SadC, and PilB as novel interaction partners of NbdA using the bacterial adenylate cyclase two-hybrid assay. Taken together, this work demonstrates the usefulness of the native membrane-protein library of <i>P. aeruginosa</i> for the investigation of protein interactions and membrane-protein complexes. Data are available via ProteomeXchange with identifiers PXD039702 and PXD039700.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"4 ","pages":"uqad028"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/e6/b3/uqad028.PMC10335732.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9872409","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}

{"title":"Correction to: control of light-dependent behaviour in cyanobacteria by the second messenger cyclic di-GMP.","authors":"","doi":"10.1093/femsml/uqad035","DOIUrl":"https://doi.org/10.1093/femsml/uqad035","url":null,"abstract":"<p><p>[This corrects the article DOI: 10.1093/femsml/uqad019.].</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"4 ","pages":"uqad035"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10430786/pdf/uqad035.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10022106","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}