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Advancements in Mass Spectrometry-Based Glycomics in Food and Nutritional Science 食品与营养科学中基于质谱的糖组学研究进展。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2025-08-01 DOI: 10.1002/mas.70003
JaeHui Song, HyunJi Lee, Youngshik Choe, Hyeyoung Lee
{"title":"Advancements in Mass Spectrometry-Based Glycomics in Food and Nutritional Science","authors":"JaeHui Song,&nbsp;HyunJi Lee,&nbsp;Youngshik Choe,&nbsp;Hyeyoung Lee","doi":"10.1002/mas.70003","DOIUrl":"10.1002/mas.70003","url":null,"abstract":"<p>This review highlights advancements in mass spectrometry (MS)-based glycomics in food and nutritional science. Carbohydrates, which are vital for human health, exhibit complex structures, making their analysis challenging. MS has become an indispensable tool for elucidating the structures of carbohydrates, including glycans, through soft ionization techniques such as MALDI and ESI. Furthermore, coupling MS with advanced separation techniques enhances sensitivity and resolution. This review underscores the pivotal contributions of Professor Carlito B. Lebrilla to glycomics research, particularly regarding milk oligosaccharides and dietary fibers, and their roles in gut health. Comprehensive food glycomic databases and MS-based studies offer valuable insights into the functions of carbohydrates and their implications for nutrition.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"829-850"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/mas.70003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144758815","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Carlito B. Lebrilla: Building Instruments, Fields and Opportunities From the Ground up Carlito B. Lebrilla：从头开始构建工具、领域和机会。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2026-05-15 DOI: 10.1002/mas.70032
Benjamin A. Garcia
{"title":"Carlito B. Lebrilla: Building Instruments, Fields and Opportunities From the Ground up","authors":"Benjamin A. Garcia","doi":"10.1002/mas.70032","DOIUrl":"10.1002/mas.70032","url":null,"abstract":"","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"591-596"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147947323","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Mass Spectrometry-Based Proteomics Technologies to Define Endogenous Protein-Protein Interactions and Their Applications to Cancer and Viral Infectious Diseases 基于质谱的蛋白质组学技术定义内源性蛋白质-蛋白质相互作用及其在癌症和病毒性传染病中的应用。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2025-02-09 DOI: 10.1002/mas.21926
Clinton Yu, Rithika Adavikolanu, Robyn M. Kaake, Lan Huang
{"title":"Mass Spectrometry-Based Proteomics Technologies to Define Endogenous Protein-Protein Interactions and Their Applications to Cancer and Viral Infectious Diseases","authors":"Clinton Yu,&nbsp;Rithika Adavikolanu,&nbsp;Robyn M. Kaake,&nbsp;Lan Huang","doi":"10.1002/mas.21926","DOIUrl":"10.1002/mas.21926","url":null,"abstract":"<div>\u0000 \u0000 <p>An intricate network of protein assemblies and protein-protein interactions (PPIs) underlies nearly every biological process in living systems. The organization of these cellular networks is highly dynamic and intimately tied to the genomic and proteomic landscapes of a cell. Disruptions in normal PPIs can impair cellular functions and contribute to the development of human diseases. In recent years, targeting PPIs has emerged as an attractive strategy for drug discovery. Consequently, the identification and characterization of endogenous PPIs—those occurring naturally under physiological conditions—has become crucial for unraveling the molecular mechanisms driving human pathology and for laying the groundwork for novel diagnostics and therapeutics. Owing to numerous technological advancements, mass spectrometry (MS)-based proteomics has transformed the study of PPIs at the systems-level. This review focuses on proteomics approaches that enable the characterization of physiologically relevant endogenous interactions, spanning complex-centric to structure-centric analyses. Additionally, their applications to define native PPIs in the contexts of cancer and viral infectious diseases is highlighted.</p>\u0000 </div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"714-744"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143381386","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
MS-Based Glycome Characterization of Biotherapeutics With N- and O-Glycosylation 基于质谱的N-和o -糖基化生物治疗药物的糖化表征。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2025-01-27 DOI: 10.1002/mas.21925
Myung Jin Oh, Youngsuk Seo, Nari Seo, Hyun Joo An
{"title":"MS-Based Glycome Characterization of Biotherapeutics With N- and O-Glycosylation","authors":"Myung Jin Oh,&nbsp;Youngsuk Seo,&nbsp;Nari Seo,&nbsp;Hyun Joo An","doi":"10.1002/mas.21925","DOIUrl":"10.1002/mas.21925","url":null,"abstract":"<div>\u0000 \u0000 <p>With the increasing FDA approvals of glycoprotein-based biotherapeutics including monoclonal antibodies, cytokines, and enzyme treatments, the significance of glycosylation in modulating drug efficacy and safety becomes central. This review highlights the crucial role of mass spectrometry (MS) in elucidating the glycome of biotherapeutics that feature N- and O-glycosylation, directly addressing the challenges posed by glycosylation complexity and heterogeneity. We have detailed the advancements and application of MS technologies including MALDI-TOF MS, LC-MS, and tandem MS in the precise characterization of glycoprotein therapeutics. Emphasizing MS-based strategies for detecting immunogenic glycans and ensuring batch-to-batch consistency, this review highlights targeted approaches for glycoprotein, glycopeptide, and glycan analysis tailored to meet the stringent analytical and regulatory demands of biopharmaceutical development.</p>\u0000 </div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"691-713"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143051188","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Mass Spectrometry Structural Proteomics Enabled by Limited Proteolysis and Cross-Linking 通过有限蛋白质分解和交联实现质谱结构蛋白质组学。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2024-09-19 DOI: 10.1002/mas.21908
Haiyan Lu, Zexin Zhu, Lauren Fields, Hua Zhang, Lingjun Li
{"title":"Mass Spectrometry Structural Proteomics Enabled by Limited Proteolysis and Cross-Linking","authors":"Haiyan Lu,&nbsp;Zexin Zhu,&nbsp;Lauren Fields,&nbsp;Hua Zhang,&nbsp;Lingjun Li","doi":"10.1002/mas.21908","DOIUrl":"10.1002/mas.21908","url":null,"abstract":"<p>The exploration of protein structure and function stands at the forefront of life science and represents an ever-expanding focus in the development of proteomics. As mass spectrometry (MS) offers readout of protein conformational changes at both the protein and peptide levels, MS-based structural proteomics is making significant strides in the realms of structural and molecular biology, complementing traditional structural biology techniques. This review focuses on two powerful MS-based techniques for peptide-level readout, namely limited proteolysis-mass spectrometry (LiP-MS) and cross-linking mass spectrometry (XL-MS). First, we discuss the principles, features, and different workflows of these two methods. Subsequently, we delve into the bioinformatics strategies and software tools used for interpreting data associated with these protein conformation readouts and how the data can be integrated with other computational tools. Furthermore, we provide a comprehensive summary of the noteworthy applications of LiP-MS and XL-MS in diverse areas including neurodegenerative diseases, interactome studies, membrane proteins, and artificial intelligence-based structural analysis. Finally, we discuss the factors that modulate protein conformational changes. We also highlight the remaining challenges in understanding the intricacies of protein conformational changes by LiP-MS and XL-MS technologies.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"644-671"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/mas.21908","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142277684","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Quantifying Protein–Glycan Interactions Using Native Mass Spectrometry 使用天然质谱法定量蛋白质-聚糖相互作用。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2025-06-30 DOI: 10.1002/mas.21943
Duong T. Bui, Elena N. Kitova, Ling Han, Lara K. Mahal, John S. Klassen
{"title":"Quantifying Protein–Glycan Interactions Using Native Mass Spectrometry","authors":"Duong T. Bui,&nbsp;Elena N. Kitova,&nbsp;Ling Han,&nbsp;Lara K. Mahal,&nbsp;John S. Klassen","doi":"10.1002/mas.21943","DOIUrl":"10.1002/mas.21943","url":null,"abstract":"<p>Interactions between glycan-binding proteins (GBPs) and carbohydrates (glycans) are essential to many biological processes relevant to human health and disease. For most GBPs, however, their glycan interactome—the repertoire of glycans recognized and their specificities—is poorly defined. The structural diversity of biologically relevant glycans and their limited availability in purified form, as well as their varied presentation, often as glycoconjugates, and weak affinities are key challenges hindering comprehensive glycan interaction mapping. Native mass spectrometry (nMS), a versatile, sensitive and label-free tool for the discovery of GBP–glycan interactions and quantifying their stoichiometry and thermodynamic parameters, is poised to play a leading role in defining the glycan interactome of GBPs. Here, we review established nMS methodologies, as well as important experimental and instrumental considerations, for detecting GBP<b>–</b>glycan interactions in vitro, and reliably measuring their stoichiometry and affinity. Recent advances in nMS methods for high-throughput library screening, including shotgun glycomics, and quantifying GBP interactions with glycoproteins and glycosphingolipids, are also described.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"800-828"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/mas.21943","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144525635","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Editorial for the Special Honor Issue Honoring Dr. Carlito B. Lebrilla 专为纪念卡里托·b·勒布里拉博士而写的社论。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2026-04-17 DOI: 10.1002/mas.70027
Benjamin A. Garcia
{"title":"Editorial for the Special Honor Issue Honoring Dr. Carlito B. Lebrilla","authors":"Benjamin A. Garcia","doi":"10.1002/mas.70027","DOIUrl":"10.1002/mas.70027","url":null,"abstract":"","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"589-590"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147715399","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Unraveling Posttranslational Modification Complexity: Advances in Quantitative Histone Proteoform Mass Spectrometry 揭示翻译后修饰的复杂性：定量组蛋白蛋白质谱的进展。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2025-06-01 DOI: 10.1002/mas.21941
Karl F. Poncha, Alyssa T. Paparella, Nicolas L. Young
{"title":"Unraveling Posttranslational Modification Complexity: Advances in Quantitative Histone Proteoform Mass Spectrometry","authors":"Karl F. Poncha,&nbsp;Alyssa T. Paparella,&nbsp;Nicolas L. Young","doi":"10.1002/mas.21941","DOIUrl":"10.1002/mas.21941","url":null,"abstract":"<div>\u0000 \u0000 <p>Histone proteins and their posttranslational modifications are central to chromatin structure and function. These modifications often occur in combinations, generating a diverse array of histone proteoforms that contribute to the dynamic regulation of chromatin architecture. Advancements in mass spectrometry-based proteomics, particularly top-down and middle-down approaches, have significantly enhanced our ability to characterize these proteoforms and elucidate PTM crosstalk. This review provides an analysis of the epigenetic machinery involved in the addition, recognition, and removal of histone PTMs, emphasizing the complexity introduced by histone variants and combinatorial PTM patterns. We examine the challenges and limitations of traditional antibody-based methods for PTM analysis and highlight the advantages of mass spectrometry techniques in providing comprehensive and quantitative insights into histone proteoforms. Key considerations in experimental design, sample preparation, chromatographic separation, and data analysis are outlined for the effective application of mass spectrometry for histone proteoform studies. By integrating these technological advancements on the side of sample preparation, instrumentation, and data processing a deeper understanding of chromatin regulation through PTM crosstalk is achieved, paving the way for mass spectrometry-based proteomics to spearhead the discovery of novel therapeutic strategies with proteoform level specificity.</p></div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"769-799"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144197795","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Personal Reflection on Dr. Carlito Lebrilla Carlito Lebrilla博士的个人反思。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2026-04-17 DOI: 10.1002/mas.70026
Benjamin A. Garcia
{"title":"Personal Reflection on Dr. Carlito Lebrilla","authors":"Benjamin A. Garcia","doi":"10.1002/mas.70026","DOIUrl":"10.1002/mas.70026","url":null,"abstract":"","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"597-598"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147715337","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Mass spectrometry imaging of N-linked glycans: Fundamentals and recent advances N-连接糖的质谱成像：基本原理和最新进展。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2024-06-27 DOI: 10.1002/mas.21895
Tana V. Palomino, David C. Muddiman
{"title":"Mass spectrometry imaging of N-linked glycans: Fundamentals and recent advances","authors":"Tana V. Palomino,&nbsp;David C. Muddiman","doi":"10.1002/mas.21895","DOIUrl":"10.1002/mas.21895","url":null,"abstract":"<p>With implications in several medical conditions, <i>N</i>-linked glycosylation is one of the most important posttranslation modifications present in all living organisms. Due to their nontemplate synthesis, glycan structures are extraordinarily complex and require multiple analytical techniques for complete structural elucidation. Mass spectrometry is the most common way to investigate <i>N</i>-linked glycans; however, with techniques such as liquid-chromatography mass spectrometry, there is complete loss of spatial information. Mass spectrometry imaging is a transformative analytical technique that can visualize the spatial distribution of ions within a biological sample and has been shown to be a powerful tool to investigate <i>N</i>-linked glycosylation. This review covers the fundamentals of mass spectrometry imaging and <i>N</i>-linked glycosylation and highlights important findings of recent key studies aimed at expanding and improving the glycomics imaging field.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"599-623"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11671621/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141454236","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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