ProteomicsPub Date : 2025-09-04DOI: 10.1002/pmic.70038
Omar Arias-Gaguancela, Carmen Palii, Mehar Un Nissa, Marjorie Brand, Jeffrey Ranish
{"title":"QuickProt: A Bioinformatics and Visualization Tool for DIA and PRM Mass Spectrometry-Based Proteomics Datasets","authors":"Omar Arias-Gaguancela, Carmen Palii, Mehar Un Nissa, Marjorie Brand, Jeffrey Ranish","doi":"10.1002/pmic.70038","DOIUrl":"10.1002/pmic.70038","url":null,"abstract":"<div>\u0000 \u0000 <p>Mass spectrometry (MS)-based proteomics focuses on identifying and quantifying peptides and proteins in biological samples. Processing of MS-derived raw data, including deconvolution, alignment, and peptide-protein prediction, has been achieved through various software platforms. However, the downstream analysis, including quality control, visualizations, and interpretation of proteomics results, remains cumbersome due to the lack of integrated tools to facilitate the analyses. To address this challenge, we developed QuickProt, a series of Python-based Google Colab notebooks for analyzing data-independent acquisition (DIA) and parallel reaction monitoring (PRM) proteomics datasets. These pipelines are designed so that users with no coding expertise can utilize the tool. Furthermore, as open-source code, QuickProt notebooks can be customized and incorporated into existing workflows. As proof of concept, we applied QuickProt to analyze in-house DIA and stable isotope dilution (SID)-PRM MS proteomics datasets from a time-course study of human erythropoiesis. The analysis resulted in annotated tables and publication-ready figures revealing a dynamic rearrangement of the proteome during erythroid differentiation, with the abundance of proteins linked to gene regulation, metabolic, and chromatin remodeling pathways increasing early in erythropoiesis. Altogether, these tools aim to automate and streamline DIA and PRM-MS proteomics data analysis, making it more efficient and less time-consuming.</p>\u0000 </div>","PeriodicalId":224,"journal":{"name":"Proteomics","volume":"25 19","pages":"62-72"},"PeriodicalIF":3.9,"publicationDate":"2025-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144999335","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":"SLB-msSIM: A Spectral Library-Based Multiplex Segmented SIM Platform for Single-Cell Proteomic Analysis","authors":"Lakmini Senavirathna, Cheng Ma, Van-An Duong, Hong-Yuan Tsai, Ru Chen, Sheng Pan","doi":"10.1002/pmic.70037","DOIUrl":"10.1002/pmic.70037","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>Mass spectrometry (MS)-based single-cell proteomics, while highly challenging, offers unique potential for a wide range of applications to interrogate cellular heterogeneity, trajectories, and phenotypes at a functional level. We report here the development of the spectral library-based multiplex segmented selected ion monitoring (SLB-msSIM) method, a conceptually unique approach with significantly enhanced sensitivity and robustness for single-cell analysis. The single-cell MS data is acquired by a multiplex segmented selected ion monitoring (msSIM) technique, which sequentially applies multiple isolation cycles with the quadrupole using a wide isolation window in each cycle to accumulate and store precursor ions in the C-trap for a single scan in the Orbitrap. Proteomic identification is achieved through spectral matching using a well-defined spectral library. We applied the SLB-msSIM method to interrogate cellular heterogeneity in various pancreatic cancer cell lines, revealing common and distinct functional traits among PANC-1, MIA-PaCa2, AsPc-1, HPAF, and normal HPDE cells. Furthermore, for the first time, our novel data revealed the diverse cell trajectories of individual PANC-1 cells during the induction and reversal of epithelial-mesenchymal transition (EMT). Collectively, our results demonstrate that SLB-msSIM is a highly sensitive and robust platform, applicable to a wide range of instruments for single-cell proteomic studies.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Summary</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>\u0000 <p>We present the SLB-msSIM method, a conceptually unique approach in mass spectrometry-based single-cell proteomics that significantly enhances sensitivity and robustness.</p>\u0000 </li>\u0000 \u0000 <li>\u0000 <p>This innovative platform enables detailed analysis of the proteome landscape, capturing cellular heterogeneity, trajectories, and phenotypes at a single-cell resolution.</p>\u0000 </li>\u0000 \u0000 <li>\u0000 <p>Utilizing the SLB-msSIM technique, we identified both common and distinct functional traits among various pancreatic cancer cell lines and normal cells. Moreover, our study unveiled new insights into the diverse cell trajectories of individual cancer cells during the induction and reversal of epithelial-mesenchymal transition (EMT).</p>\u0000 </li>\u0000 \u0000 <li>\u0000 <p>In summary, the SLB-msSIM method offers a highly sensitive and robust platform for single-cell proteomic studies, with broad applicability across different instruments.</p>\u0000 </li>\u0000 ","PeriodicalId":224,"journal":{"name":"Proteomics","volume":"25 19","pages":"50-61"},"PeriodicalIF":3.9,"publicationDate":"2025-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/epdf/10.1002/pmic.70037","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144991080","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}
ProteomicsPub Date : 2025-09-02DOI: 10.1002/pmic.70030
Vanya Bhushan, Clinton J Bradfield, Sandhini Saha, Sung Hwan Yoon, Iain D C Fraser, Aleksandra Nita-Lazar
{"title":"Nigericin-Triggered Phosphodynamics in Inflammasome Formation and Pyroptosis.","authors":"Vanya Bhushan, Clinton J Bradfield, Sandhini Saha, Sung Hwan Yoon, Iain D C Fraser, Aleksandra Nita-Lazar","doi":"10.1002/pmic.70030","DOIUrl":"https://doi.org/10.1002/pmic.70030","url":null,"abstract":"<p><p>Innate immune signaling relies heavily on phosphorylation cascades to mount effective immune responses. Although traditional innate immune signaling cascades following TLR4 stimulation have been investigated through a temporally quantitative phosphoproteomic lens, far fewer studies have applied these methods to distinct signaling following the inflammasome trigger leading to IL-1β release. Here, we conducted time-resolved phosphoproteomic profiling to investigate kinase signaling downstream of the inflammasome trigger nigericin. We found that nigericin induces rapid and potent alterations in the phosphorylation landscape where immune-related signaling, mitogen-activated protein kinases (MAPKs), and PKC signaling are prevalent. We also found significant evidence of phospho-modified metabolic cascades, suggesting that phosphosignaling plays a role in previously described immunometabolic regulation. These signaling events preceded robust phosphorylation of DNA damage and chromatin reorganization proteins before pyroptotic rupture. Lastly, by performing temporal clustering of phospho-dynamics, we revealed novel ontology-level shifts in phosphosignaling cascades following nigericin treatment that highlight abrupt changes in cellular behavior during early and late intracellular inflammatory events. SUMMARY: Protein phosphorylation is critical to convey innate immune signaling information to specific effector arms of the cellular immune response. This study focuses on characterizing phosphoproteomic alterations stemming from the inflammasome trigger nigericin. By gaining a deeper understanding of global kinase phosphodynamics in response to inflammasome activation, we aim to identify novel pharmacological targets to treat chronic inflammatory diseases driven by inflammasome-dependent IL-1β release.</p>","PeriodicalId":224,"journal":{"name":"Proteomics","volume":" ","pages":"e70030"},"PeriodicalIF":3.9,"publicationDate":"2025-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144937444","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}
ProteomicsPub Date : 2025-08-29DOI: 10.1002/pmic.70031
Yucheng Liao, Rui Qian, Mengting Zhang, Chenghao Sun, Han Wen, Weinan E, Weijie Zhang, Mowei Zhou
{"title":"TDEase: An Open-Source Data Visualization Software Framework for Targeted Proteoform Characterization by Top-Down Proteomics.","authors":"Yucheng Liao, Rui Qian, Mengting Zhang, Chenghao Sun, Han Wen, Weinan E, Weijie Zhang, Mowei Zhou","doi":"10.1002/pmic.70031","DOIUrl":"https://doi.org/10.1002/pmic.70031","url":null,"abstract":"<p><p>Top-down proteomics (TDP) is a powerful approach for characterizing intact protein molecules and their diverse proteoforms. Despite recent advances, current TDP software tools often suffer from fragmented workflows, steep learning curves for non-experts, or limited interactive visualization capabilities. To address these challenges, we introduce TDEase, an integrated analytical framework designed to streamline and enhance TDP data interpretation, with a current focus on integration with the TopPIC suite package for targeted proteoform characterization. TDEase features a modular architecture comprising TDPipe, a multi-process data processing engine, and TDVis, an interactive web-based visualization module. TDPipe automates the execution of mainstream TDP analysis algorithms through a user-configurable pipeline, ensuring seamless and reproducible data processing. The TDVis module then transforms these results into dynamic, interactive dashboards, enabling multidimensional data exploration, including feature maps and PTM analysis. An alternative version, TDVisWeb, is also available for visualizing the results on an internet server or intranet workstation at institutional core facilities. We demonstrated the software capabilities in proteoform identification and comparative analysis using published histone datasets. TDEase is built with Python and open-source, allowing future improvements and incorporation of more data types as the TDP community develops new software. Source code is available at https://github.com/Computational-TDMS/TDEase.</p>","PeriodicalId":224,"journal":{"name":"Proteomics","volume":" ","pages":"e70031"},"PeriodicalIF":3.9,"publicationDate":"2025-08-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144937390","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}
ProteomicsPub Date : 2025-08-28DOI: 10.1002/pmic.70035
Van-An Duong, Evan Pan, Prerna Dabral, Kristina M. Utzschneider, Johanna W. Lampe, Ru Chen, Meredith A.J. Hullar
{"title":"Metaproteomic Analysis to Assess the Impact of Storage Media on Human Gut Microbiome in Fecal Samples","authors":"Van-An Duong, Evan Pan, Prerna Dabral, Kristina M. Utzschneider, Johanna W. Lampe, Ru Chen, Meredith A.J. Hullar","doi":"10.1002/pmic.70035","DOIUrl":"10.1002/pmic.70035","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>The human gut microbiome is a diverse community of microorganisms residing in the gastrointestinal tract. The storage condition of fecal samples may impact the taxonomic and protein compositions of microbiomes in these samples. Here, we performed a mass spectrometry-based metaproteomic study to assess the impact of storage media on human gut microbiome in fecal samples. We evaluated FDA-authorized OMNIgene·GUT (OG), phosphate-buffered saline (PBS), and RNALater (RNAL) buffers and identified 38,185 microbial peptides corresponding to 7348 microbial proteins, which matched 16 phyla, 20 classes, 50 orders, 104 families, 332 genera, and 453 species. We found a high similarity among the fecal microbiomes preserved in OG, PBS, and RNAL in terms of the identification of proteins, taxa, and functional annotations. Both alpha and beta diversity suggested the high similarity among samples stored in the three media. Nonetheless, we also found some notable differences among buffers regarding the abundances of a few taxon groups. A partial human proteome (over 400 proteins) was identified in the fecal samples, with most of these proteins associated with the membrane and extracellular regions. The findings indicate the similarity among microbiomes in the fecal samples stored in OG, PBS, and RNAL regarding proteome profile, taxa, and functional capacity.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Summary</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>\u0000 <p>This study thoroughly analyzed and compared the metaproteomes of fecal samples preserved at −80°C in PBS, RNALater, and OMNIgene·GUT Dx buffers, offering novel insights into the effectiveness of these buffers in maintaining the stability and composition of the human gut microbiome.</p>\u0000 </li>\u0000 \u0000 <li>\u0000 <p>We found a high similarity in the identification and quantification of proteins, taxa, and functional annotations across the three buffers, with notable quantitative differences highlighting subtle yet important variations in preservation efficacy.</p>\u0000 </li>\u0000 \u0000 <li>\u0000 <p>The unique datasets and findings could offer valuable revelations into the impact of fecal sample preservation on translational and clinical analyses of the human gut microbiome.</p>\u0000 </li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":224,"journal":{"name":"Proteomics","volume":"25 19","pages":"39-49"},"PeriodicalIF":3.9,"publicationDate":"2025-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/epdf/10.1002/pmic.70035","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144937502","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}
ProteomicsPub Date : 2025-08-28DOI: 10.1002/pmic.70032
Dietmar Kültz, Alison M. Gardell, Anthony DeTomaso, Greg Stoney, Baruch Rinkevich, Andy Qarri, Jens Hamar
{"title":"Proteome-Wide 4-Hydroxy-2-Nonenal Signature of Oxidative Stress in the Marine Invasive Tunicate Botryllus schlosseri","authors":"Dietmar Kültz, Alison M. Gardell, Anthony DeTomaso, Greg Stoney, Baruch Rinkevich, Andy Qarri, Jens Hamar","doi":"10.1002/pmic.70032","DOIUrl":"10.1002/pmic.70032","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>The ascidian <i>Boytryllus schlosseri</i> is a marine chordate that thrives under conditions of anthropogenic climate change. The <i>B. schlosseri</i> expressed proteome contains unusually high levels of proteins adducted with 4-hydroxy-2-nonenal (HNE). HNE represents a prominent posttranslational modification resulting from oxidative stress. Prior to this study, which identified 1052 HNE adducted proteins in <i>B. schlosseri by</i> LCMS, HNE protein modification has not been determined in any marine species. Adducted residues were ascertained for 1849 HNE modifications, 1195 of which had a maximum amino acid localization score. Most HNE modifications were at less reactive lysines (rather than more reactive cysteines). HNE prevalence on most sites was high, suggesting that <i>B. schlosseri</i> experiences and tolerates high intracellular reactive oxygen species levels, resulting in substantial lipid peroxidation. HNE adducted <i>B. schlosseri</i> proteins show enrichment in mitochondrial, proteostasis, and cytoskeletal functions. We propose that redox signaling contributes to regulating energy metabolism, the blastogenic cycle, oxidative burst defenses, and cytoskeleton dynamics in <i>B. schlosseri</i>. DIA-LCMS quantification of 72 HNE-adducted sites across 60 proteins revealed significant population-specific differences. We conclude that the vast amount of HNE protein adduction in this circumpolar tunicate is indicative of high oxidative stress tolerance contributing to its range expansion into diverse environments.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Summary</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>\u0000 <p>Oxidative stress results from environmental challenges that increase in frequency and severity during the Anthropocene.</p>\u0000 </li>\u0000 \u0000 <li>\u0000 <p>Oxygen radical attack causes lipid peroxidation, leading to HNE production.</p>\u0000 </li>\u0000 \u0000 <li>\u0000 <p>Proteome-wide HNE adduction is highly prevalent in <i>Botryllus schlosseri</i>, a widely distributed, highly invasive, and economically important biofouling ascidian, and the first marine species to be analyzed for proteome HNE modification.</p>\u0000 </li>\u0000 \u0000 <li>\u0000 <p>HNE adduction of specific proteins may physiologically sequester reactive oxygen species, which could enhance fitness and resilience during environmental change.</p>\u0000 </li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":224,"journal":{"name":"Proteomics","volume":"25 19","pages":"12-25"},"PeriodicalIF":3.9,"publicationDate":"2025-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/epdf/10.1002/pmic.70032","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144937432","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":"Mining Alzheimer's Interactomes, Macromolecular Complexes and Pathways for Drug Discovery.","authors":"Kalpana Panneerselvam, Krishna Kumar Tiwari, Luana Licata, Simona Panni, Sylvie Ricard-Blum, Sucharitha Balu, Susie Huget, Juan Jose Medina Reyes, Eliot Ragueneau, Livia Perfetto, Birgit Meldal, Sandra Orchard, Henning Hermjakob","doi":"10.1002/pmic.70018","DOIUrl":"https://doi.org/10.1002/pmic.70018","url":null,"abstract":"<p><p>Alzheimer's disease (AD) is a progressive neurodegenerative disorder that leads to dementia. Many cases are diagnosed annually and there is no currently available cure. Understanding the underlying disease biology of AD through the study of molecular networks, particularly by mapping clinical variants to tissue-specific interactomes and regulatory macromolecular assemblies, offers a promising avenue to elucidate altered disease pathways. In this study, we applied differential interactome analysis using a manually curated AD dataset to identify how disease-associated mutations alter both transient and stable protein interactions. By focussing on variant-specific associations detected in brain-relevant tissues, we mapped disruptions in stable macromolecular assemblies and performed Reactome enrichment analysis to uncover perturbed pathways unique to each variant. Additionally, we explored therapeutic insights through the analysis of amyloid precursor protein (APP) physical interactors, identifying potential intervention points that influence amyloidogenic processing. Complementing protein-level data, we integrated microRNA (miRNA)-mediated regulatory interactions, revealing an additional layer of posttranscriptional control over key AD genes. Together, this multilayered strategy provides a framework for precision therapeutics in AD.</p>","PeriodicalId":224,"journal":{"name":"Proteomics","volume":" ","pages":"e70018"},"PeriodicalIF":3.9,"publicationDate":"2025-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144937473","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":"Proteomics Reveals AP-2 Complex Depletion Suppressing Listeria monocytogenes Intracellular Replication","authors":"Zhangfu Li, Haiying Ran, Xiangyu Tang, Xiao Liu, Xiaoyuan Wan, Pei Xiong, Zhe Gan, Xu Liu, Liting Wang, Jiangbei Yuan","doi":"10.1002/pmic.70034","DOIUrl":"10.1002/pmic.70034","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p><i>Listeria monocytogenes</i> represents a significant zoonotic pathogen that completes its infectious cycle by invading intestinal epithelial cells, breaching mucosal barriers, and disseminating to target organs such as the liver and spleen. During this process, the innate immune system, particularly macrophages and dendritic cells, plays a pivotal role in pathogen clearance. In this study, we established an in vitro infection model utilizing Raw264.7 macrophages, DC2.4 dendritic cells, HeLa, and Caco-2 epithelial cells. We demonstrated <i>L. monocytogenes</i> infection significantly upregulates the expression of Ap2s1, a key subunit of the AP-2 adaptor complex, in host cells. Subsequent proteomic analysis revealed that two additional AP-2 complex subunits, Ap2m1 and Ap2a2, functionally cooperate with Ap2s1 during infection. Genetic knockout experiments confirmed that specific silencing of any of these three subunits, Ap2m1, Ap2a2, or Ap2s1, markedly inhibited intracellular bacterial proliferation. These findings establish the AP-2 complex as a promising molecular target for developing novel therapeutic strategies against <i>L. monocytogenes</i> infections.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Summary</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>\u0000 <p>This study unveils a critical role of the AP-2 adaptor complex in <i>L. monocytogenes</i> intracellular replication, identifying three subunits, Ap2s1, Ap2m1, and Ap2a2, as key host factors exploited by the pathogen.</p>\u0000 </li>\u0000 \u0000 <li>\u0000 <p>Using proteomics and CRISPR/Cas9-mediated knockout models, we demonstrate that <i>L. monocytogenes</i> infection upregulates Ap2s1 expression, and depletion of AP-2 subunit significantly impairs bacterial proliferation.</p>\u0000 </li>\u0000 \u0000 <li>\u0000 <p>Our findings reveal that AP-2 facilitates post-phagosomal cytosolic replication, independent of bacterial cell-to-cell spread.</p>\u0000 </li>\u0000 \u0000 <li>\u0000 <p>This study demonstrates that the AP-2 complex may represent a host factor exploited by <i>L. monocytogenes</i> to promote intracellular replication, offering a novel host-directed therapeutic target to combat antibiotic-resistant strains.</p>\u0000 </li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":224,"journal":{"name":"Proteomics","volume":"25 19","pages":"26-38"},"PeriodicalIF":3.9,"publicationDate":"2025-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144937463","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}
ProteomicsPub Date : 2025-08-21DOI: 10.1002/pmic.70029
Lucia Grenga, Magnus Øverlie Arntzen, Jean Armengaud
{"title":"Metaproteomics and Meta-Omics to Decrypt Microbiome Functionality.","authors":"Lucia Grenga, Magnus Øverlie Arntzen, Jean Armengaud","doi":"10.1002/pmic.70029","DOIUrl":"https://doi.org/10.1002/pmic.70029","url":null,"abstract":"","PeriodicalId":224,"journal":{"name":"Proteomics","volume":" ","pages":"e70029"},"PeriodicalIF":3.9,"publicationDate":"2025-08-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144937387","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}