{"title":"Proteomics Uncovers Enrichment Bias of Common Extracellular Vesicle Isolation Methods in HEK293T Cells","authors":"Shipan Fan, , , Yuqi Lin, , , Zuoquan Chen, , and , Ansgar Poetsch*, ","doi":"10.1021/acs.jproteome.5c00123","DOIUrl":"10.1021/acs.jproteome.5c00123","url":null,"abstract":"<p >Extracellular vesicles (EVs) are membranous structures consisting of lipid bilayers that are released by most cell types and serve as important mediators of intercellular communication. The HEK293T cell line model has gained considerable attention from the scientific community, particularly in the fields of engineering and drug delivery. Nevertheless, there is a dearth of systematic comparisons of the most prevalent EV isolation methodologies for HEK293T in terms of recovery and specificity. In this study, common EV isolation workflows using either ultracentrifugation (UC), ultrafiltration (UF), polyethylene glycol precipitation (PEG), or EXODUS were compared in HEK293T cells and profiled using proteomics, which enabled the identification of almost 4000 proteins. Moreover, the observed large discrepancy between PEG and other methods can be attributed to the cofractionation of two EV populations that differed in density and protein composition, as revealed by isopycnic ultracentrifugation. Therefore, it was assumed that the cargo inside EVs is correlated with their density, which presents intrinsic heterogeneity in HEK293T EVs. This study aimed to facilitate the selection and implementation of an EV enrichment procedure for the HEK293T cell line and to discern heterogeneity in the HEK293T EV population.</p>","PeriodicalId":48,"journal":{"name":"Journal of Proteome Research","volume":"24 10","pages":"4900–4910"},"PeriodicalIF":3.6,"publicationDate":"2025-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145013529","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Yuri E. M. van der Burgt, , , Emile de Meijer, , and , Magnus Palmblad*,
{"title":"Brief Evaluation of Olink Reveal Proximity Extension Assay for High-Throughput Proteomics: A Case Study Using NIST SRM 1950 and Two Spike-In Protein Standards","authors":"Yuri E. M. van der Burgt, , , Emile de Meijer, , and , Magnus Palmblad*, ","doi":"10.1021/acs.jproteome.5c00571","DOIUrl":"10.1021/acs.jproteome.5c00571","url":null,"abstract":"<p >Plasma proteomics has regained attention in recent years through advancements in mass spectrometry instrumentation and sample preparation as well as new high-throughput affinity-based technologies. Here, we evaluate the analytical performance of the new Olink Reveal platform, a proximity extension assay (PEA)-based technology quantifying 1034 proteins and covering many biological pathways, in particular immune system processes. Using spiked-in recombinant Interleukin-10 (IL-10) and vascular endothelial growth factor D (VEGF-D) in the NIST SRM 1950 plasma standard, we assessed the linearity, sensitivity, precision, and accuracy of the Olink Reveal assay. The results demonstrated strong linear relationships (<i>R</i><sup>2</sup> 0.922–0.953) for both IL-10 and VEGF-D across spiked-in concentrations, confirming the robust technical performance for these two proteins in the Olink Reveal platform. The resulting data contain no sensitive or personally identifiable information and are therefore suitable for use in benchmarking and software development. The data are publicly available in the PRIDE repository with identifier PAD000009.</p>","PeriodicalId":48,"journal":{"name":"Journal of Proteome Research","volume":"24 10","pages":"5292–5296"},"PeriodicalIF":3.6,"publicationDate":"2025-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.5c00571","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145022451","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Identification of Novel Protein Biomarkers for Myasthenia Gravis by Integrating Human Proteomics with Genetic Instruments","authors":"Hong-Xi Chen, , , Xue Lin, , , Na-Na Zhang, , , Zi-Yan Shi, , , Ying Zhang, , , Qin Du, , , Ling-Yao Kong, , , Dong-Ren Sun, , , Rui Wang, , , Zi-Chao Mou, , , Yang-Yang Zhang, , , Yun-Tao Mo, , , Xiao-Fei Wang*, , and , Hong-Yu Zhou*, ","doi":"10.1021/acs.jproteome.5c00527","DOIUrl":"10.1021/acs.jproteome.5c00527","url":null,"abstract":"<p >Myasthenia gravis (MG) presents significant health and economic challenges. To identify novel biomarkers, we analyzed proteomic data from 52,704 UK Biobank individuals, focusing on 1463 baseline proteins with follow-up >10 years. Baseline and potential MG cases were 1:5 matched to controls by using propensity score matching. We identified 38 consistently up-regulated differentially expressed proteins (DEPs) in both the baseline and potential MG groups compared to controls, categorized into cardiometabolic, inflammation, neurology, and oncology panels. These DEPs showed potential diagnostic value for distinguishing MG from other neuromuscular disorders, with the area under curves ranging from 0.616 to 0.735 across three models (logistic regression, support vector machine, and random forest). To further investigate causality, two-sample Mendelian Randomization (2SMR) and Cox proportional hazard regression were conducted, and we confirmed 18 potential causal proteins associated with MG, including those in the cardiometabolic panel (CEACAM8, OLR1, PGLYRP1, S100A11, and TNC), inflammation panel (CST7, HGF, IL1RN, IL-6, JCHAIN, OSM, PLAUR, and TGFA), neurology panel (CTSS, MMP8, TBC1D17, and VCAN), and oncology panel (S100A12). Currently, no approved drugs for MG specifically target these identified potential causal proteins and ligands. This comprehensive proteomic analysis highlights novel biomarkers associated with MG, suggesting potential targets for identifying risk proteins and future therapeutic interventions.</p>","PeriodicalId":48,"journal":{"name":"Journal of Proteome Research","volume":"24 10","pages":"5148–5158"},"PeriodicalIF":3.6,"publicationDate":"2025-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145013503","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The Atlas of the Shell Proteome in Oysters Reveals the Potential Roles of the Cytoskeleton and Extracellular Matrix in Biomineralization","authors":"Qi Yang, , , Shentong Wang, , , Mingkun Liu, , , Wei Wang, , , Guofan Zhang, , and , Li Li*, ","doi":"10.1021/acs.jproteome.5c00671","DOIUrl":"10.1021/acs.jproteome.5c00671","url":null,"abstract":"<p >Shell matrix proteins (SMPs) are fundamental biological macromolecules for mollusk shell formation, yet fewer than 400 SMPs in mollusks have been previously identified, hindering our understanding of how mollusks construct and maintain their shells. Here, we identified 1689 SMPs in the Pacific oyster <i>Crassostrea gigas</i> using three different mass spectrometry techniques, representing a significant methodological advancement in shell proteomics, enabling a 6.52-fold increase in SMP identification compared to previous studies. Gene ontology and domain annotation revealed cytoskeletal proteins (with cofilin ADF, tubulin, and myosin head domains) and extracellular matrix (ECM)-related proteins (with carbonic anhydrase, chitin-binding, von Willebrand type A, and EGF domains) as the key functional SMPs involved in biomineralization. Furthermore, developmental transcriptomics highlighted that microtubule- and microfilament-related SMPs were enriched in larvae and adults, respectively, potentially reflecting differences in cytoskeletal regulation associated with larval aragonitic and adult calcitic shells. Transcriptomic analyses revealed that acidifying stress significantly downregulated the expression of genes encoding collagen and stress-fiber-related proteins, while activating the BMP signaling pathway in oysters. These transcriptional changes suggest a potential impairment in ECM and cytoskeletal maintenance. Our findings indicate the potential roles of the cytoskeleton and ECM proteins in biomineralization and emphasize the complexity of biological controls on shell formation in oysters. Furthermore, the proteomic strategy combining three distinct technologies can be applied to other mollusks and provide deeper insights into their evolutionary trajectories under future environmental changes.</p>","PeriodicalId":48,"journal":{"name":"Journal of Proteome Research","volume":"24 10","pages":"5242–5253"},"PeriodicalIF":3.6,"publicationDate":"2025-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145013462","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Helena Beatriz Ferreira*, , , Tara van Merrienboer, , , Inês M. S. Guerra, , , Tânia Melo, , , Kak Khee Yeung, , , Venkat Ayyalasomayajula, , , Fábio Trindade, , , Rita Nogueira-Ferreira, , , Adelino Leite-Moreira, , , Laura Goracci, , , Rita Ferreira, , , M. Rosário Domingues, , , Marina Dias-Neto, , and ,
{"title":"Lipidomic Signature of Abdominal Aortic Aneurysm and Peripheral Artery Disease","authors":"Helena Beatriz Ferreira*, , , Tara van Merrienboer, , , Inês M. S. Guerra, , , Tânia Melo, , , Kak Khee Yeung, , , Venkat Ayyalasomayajula, , , Fábio Trindade, , , Rita Nogueira-Ferreira, , , Adelino Leite-Moreira, , , Laura Goracci, , , Rita Ferreira, , , M. Rosário Domingues, , , Marina Dias-Neto, , and , ","doi":"10.1021/acs.jproteome.5c00293","DOIUrl":"10.1021/acs.jproteome.5c00293","url":null,"abstract":"<p >Vascular diseases are powerful predictors of cardiovascular mortality, but they are typically under-recognized and undertreated. There is no effective treatment for either abdominal aortic aneurysm (AAA) or peripheral artery disease (PAD). Lipids are key molecules in cardiovascular diseases and good candidates for diagnosis, monitoring, and risk prediction; nonetheless, there is very limited information on the lipidomic profile of patients with AAA and PAD. We hypothesize that lipids can be used as important prognostic biomarkers of these diseases. To achieve this, we conducted a comprehensive C18 reversed-phase (RP) liquid chromatography-tandem mass spectrometry (LC-MS) lipidomic analysis of plasma from AAA and PAD patients undergoing open repair surgery, comparing their profiles with those of healthy controls. We observed a marked reduction in PAD and AAA of the relative abundances of (i) phospholipids bearing polyunsaturated fatty acids, primarily from the phosphatidylcholine (PC), phosphatidylethanolamine (PE), and phosphatidylinositol (PI) classes, mostly due to oxidative degradation, and (ii) plasmalogen species of PC and PE, which serve as endogenous antioxidants. On the other side, SM and Cer increased in both pathologies. Our findings suggest a dysregulation of the lipid metabolism in AAA and PAD compared with healthy controls that deserves exploration to unravel putative biomarkers or disease hallmarks.</p>","PeriodicalId":48,"journal":{"name":"Journal of Proteome Research","volume":"24 10","pages":"4865–4874"},"PeriodicalIF":3.6,"publicationDate":"2025-09-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144999192","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ahmed Atwa, , , Mohammed M. Alhadidy, , , Jared Lamp, , , Benjamin Combs, , and , Nicholas M. Kanaan*,
{"title":"BioID2-Based Tau Interactome Reveals Novel and Known Protein Interactions Associated with Multiple Cellular Pathways","authors":"Ahmed Atwa, , , Mohammed M. Alhadidy, , , Jared Lamp, , , Benjamin Combs, , and , Nicholas M. Kanaan*, ","doi":"10.1021/acs.jproteome.5c00473","DOIUrl":"10.1021/acs.jproteome.5c00473","url":null,"abstract":"<p >Pathological inclusions composed of tau are hallmarks of neurodegenerative diseases termed tauopathies, the most common of which is Alzheimer’s disease. Accumulating evidence suggests that tau is involved in a multitude of physiological functions that are regulated, in part, by direct and/or transient protein interactions. Deciphering the tau interactome is critical for understanding the physiological and pathological roles of tau. This work aimed to identify potential tau interactors using the <i>in situ</i> protein labeling biotin identification (BioID2) method. Advantages of this approach include in-cell interactor labeling and an enhanced likelihood of detecting transient and/or weak interactions. We identified 324 potential tau interactors spanning multiple cellular compartments and pathways. We validated tau interactions with selected candidates using two independent approaches: proximity ligation assay and co-immunoprecipitation (co-IP) which included cytoskeletal proteins (MAP2 and MAP6), nucleus-associated proteins (FUS and prune1), and synaptic proteins (synapsin-1 and neurabin-2). Importantly, this approach revealed potential novel interactors that were not clearly identified by other interaction approaches such as co-IP. Thus, this approach is a powerful tool to identify potential members of the tau interactome via <i>in situ</i> labeling. This work helps expand our understanding of tau’s physiological roles, which may also advance our understanding of its role in neurodegenerative diseases.</p>","PeriodicalId":48,"journal":{"name":"Journal of Proteome Research","volume":"24 10","pages":"5099–5115"},"PeriodicalIF":3.6,"publicationDate":"2025-09-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.5c00473","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144999287","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ruba A. Zenati*, , , Nelson C. Soares, , , Hasan Y. Alniss, , , Hamza M. Al-Hroub, , , Raafat El-Awady, , , Ahmad Y. Abuhelwa, , , Wafaa S. Ramadan, , , Shereen M. Aleidi, , , Waseem El-Huneidi, , , Eman Abu-Gharbieh, , , Karem H. Alzoubi, , , Yasser Bustanji, , and , Mohammad H. Semreen*,
{"title":"Untargeted Multiomics of LNCaP Cell Line Treated with a Novel DNA Minor Groove Binder and/or Doxorubicin Using Mass Spectrometry","authors":"Ruba A. Zenati*, , , Nelson C. Soares, , , Hasan Y. Alniss, , , Hamza M. Al-Hroub, , , Raafat El-Awady, , , Ahmad Y. Abuhelwa, , , Wafaa S. Ramadan, , , Shereen M. Aleidi, , , Waseem El-Huneidi, , , Eman Abu-Gharbieh, , , Karem H. Alzoubi, , , Yasser Bustanji, , and , Mohammad H. Semreen*, ","doi":"10.1021/acs.jproteome.5c00135","DOIUrl":"10.1021/acs.jproteome.5c00135","url":null,"abstract":"<p >Prostate cancer (PCa) remains a major global health concern, ranking among the most prevalent cancer in men worldwide. Despite the availability of various therapeutic options, the clinical efficacy of current anti-PCa agents is often compromised by drug resistance and adverse effects. DNA minor groove binders offer a potential therapeutic alternative, owing to their selective mechanism of action and favorable safety profiles. In the present study, we utilized a multiomics strategy to investigate the molecular impact of novel compound MGB4. LNCaP cells were treated with doxorubicin, MGB4, or a combination of both, followed by LC–MS/MS-based untargeted proteomics and metabolomics analyses. One-way ANOVA (<i>p</i>-value <0.05) revealed 55 significantly dysregulated proteins and 57 altered metabolites across treatments. Our findings indicate that both MGB4 and doxorubicin impacted key cellular pathways, including inhibition of translation and alterations in sphingolipid and amino acid metabolism, while doxorubicin and the combination therapy also reduced spermine and spermidine metabolism. Notably, the combined treatment exhibited synergistic effects, significantly impacting purine metabolism and reducing metabolite levels more than individual therapies. This study provides key molecular insights into MGB4 and doxorubicin’s mechanisms, supporting MGB4 as a potential prostate cancer drug candidate.</p>","PeriodicalId":48,"journal":{"name":"Journal of Proteome Research","volume":"24 10","pages":"4911–4924"},"PeriodicalIF":3.6,"publicationDate":"2025-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144999262","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Nadezhda T. Doncheva, , , Veit Schwämmle, , and , Marie Locard-Paulet*,
{"title":"Understanding Data Analysis Steps in Mass-Spectrometry-Based Proteomics Is Key to Transparent Reporting","authors":"Nadezhda T. Doncheva, , , Veit Schwämmle, , and , Marie Locard-Paulet*, ","doi":"10.1021/acs.jproteome.5c00287","DOIUrl":"10.1021/acs.jproteome.5c00287","url":null,"abstract":"<p >Mass spectrometry (MS)-based proteomics data analysis is composed of many stages from quality control, data cleaning, and normalization to statistical and functional analysis, without forgetting multiple visualization steps. All of these need to be reported next to published results to make them fully understandable and reusable for the community. Although this seems straightforward, exhaustively reporting all aspects of an analysis workflow can be tedious and error prone. This letter reports good practices when describing data analysis of MS-based proteomics data and discusses why and how the community should put efforts into more transparently reporting data analysis workflows.</p>","PeriodicalId":48,"journal":{"name":"Journal of Proteome Research","volume":"24 10","pages":"4965–4976"},"PeriodicalIF":3.6,"publicationDate":"2025-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144936126","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Shirin Alex, , , Ruben Almey, , , Rachel Sian Dennis, , , Olivier Tytgat, , , Robbin Bouwmeester, , , Dieter Deforce, , , Marcel De Puit, , , Maarten Dhaenens*, , and , Laura De Clerck,
{"title":"Potential of Proteomics in Forensic Phenotyping: A Focus on Biological Sex Estimation","authors":"Shirin Alex, , , Ruben Almey, , , Rachel Sian Dennis, , , Olivier Tytgat, , , Robbin Bouwmeester, , , Dieter Deforce, , , Marcel De Puit, , , Maarten Dhaenens*, , and , Laura De Clerck, ","doi":"10.1021/acs.jproteome.5c00098","DOIUrl":"10.1021/acs.jproteome.5c00098","url":null,"abstract":"<p >Forensic DNA analysis is well established for phenotyping, providing valuable investigative leads. Proteomics, the large-scale study of proteins, is emerging as a complementary tool to DNA analysis, particularly for enhancing the evidential value of traces. This study explores the potential of proteomics to extract phenotypic traits from whole blood, using the estimation of biological sex as a starting point. Using LC–MS/MS, proteomes from 100 whole blood samples of known sex were analyzed to develop a biological sex classifier. Cross-validation of the model highlighted the model’s ability to achieve accurate classification, identifying key peptides, such as those from pregnancy zone protein and ceruloplasmin, as critical markers. To test real-world applicability, mock case samples were generated, bringing attention to the need for model robustness. Overall, our results suggest that using proteomics to infer phenotypic traits from whole blood samples in the context of forensics, while feasible, is hindered by hard-to-overcome technical challenges. We therefore recommend that future forensic proteomics research be directed toward areas where it can be most informative, such as source attribution and estimating the timeline of events, rather than focusing on extracting phenotypic traits for donor profiling.</p>","PeriodicalId":48,"journal":{"name":"Journal of Proteome Research","volume":"24 10","pages":"4888–4899"},"PeriodicalIF":3.6,"publicationDate":"2025-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.5c00098","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144936088","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Giorgi Tsiklauri, , , Runsheng Zheng, , , Nicole Kabella, , , Polina Prokofeva, , , Christopher Pynn, , and , Bernhard Kuster*,
{"title":"High-Performance Proteomics Using Nano-, Capillary-, and Microflow Chromatographic Separations","authors":"Giorgi Tsiklauri, , , Runsheng Zheng, , , Nicole Kabella, , , Polina Prokofeva, , , Christopher Pynn, , and , Bernhard Kuster*, ","doi":"10.1021/acs.jproteome.5c00327","DOIUrl":"10.1021/acs.jproteome.5c00327","url":null,"abstract":"<p >Current applications of mass-spectrometry-based proteomics range from single-cell to body fluid analysis, each presenting very different demands regarding sensitivity or sample throughput. Additionally, the vast molecular complexity of proteomes and the massive dynamic range of protein concentrations in these biological systems require highly performant chromatographic separations in tandem with the high speed and sensitivity afforded by modern mass spectrometers. In this study, we focused on the chromatographic aspect and, more specifically, systematically evaluated proteome analysis performance across a wide range of chromatographic flow rates (0.3–50 μL/min) and associated column diameters using a Vanquish Neo HPLC coupled online to a Q Exactive HF-X mass spectrometer. Serial dilutions of HeLa cell line digests were used for benchmarking, and the total analysis time from injection to injection was intentionally fixed at 60 min (24 samples per day). The three key messages of the study are that (i) all chromatographic flow rates are suitable for high-quality proteome analysis, (ii) capLC (1.5 μL/min) is a very robust, sensitive, and quantitative alternative to nLC for many applications, and (iii) showcased proteome, phosphoproteome, and drug proteome data provide sound empirical guidance for laboratories in selecting appropriate chromatographic flow rates and column diameters for their specific applications.</p>","PeriodicalId":48,"journal":{"name":"Journal of Proteome Research","volume":"24 10","pages":"4988–5000"},"PeriodicalIF":3.6,"publicationDate":"2025-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.5c00327","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144991065","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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