Mass Spectrometry Reviews最新文献_第2页

Software Design and Analytical Challenges for Confident Glycopeptide Identification With Data-Independent Acquisition. 数据独立获取的糖肽鉴定的软件设计和分析挑战。

IF 6.9 2区化学

Mass Spectrometry Reviews Pub Date : 2025-07-01 DOI: 10.1002/mas.70000

Mary Rachel Nalehua, Joseph Zaia

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 6.9 2区化学

Mass Spectrometry Reviews Pub 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, Elena N Kitova, Ling Han, Lara K Mahal, John S Klassen","doi":"10.1002/mas.21943","DOIUrl":"https://doi.org/10.1002/mas.21943","url":null,"abstract":"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-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.","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":" ","pages":""},"PeriodicalIF":6.9,"publicationDate":"2025-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","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":"","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 6.9 2区化学

Mass Spectrometry Reviews Pub 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, Alyssa T Paparella, Nicolas L Young","doi":"10.1002/mas.21941","DOIUrl":"https://doi.org/10.1002/mas.21941","url":null,"abstract":"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.","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":" ","pages":""},"PeriodicalIF":6.9,"publicationDate":"2025-06-01","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

Analysis of Methylated Quaternary Ammonium Compounds Using Hydrophilic Interaction Liquid Chromatography Combined With Mass Spectrometry. 亲水相互作用液相色谱-质谱联用分析甲基化季铵化合物。

IF 6.9 2区化学

Mass Spectrometry Reviews Pub Date : 2025-05-29 DOI: 10.1002/mas.21942

Iman Zarei, Ambrin Farizah Babu, Ville M Koistinen, Marjo Tuomainen, Anna Kårlund, Retu Haikonen, Marko Lehtonen, Kati Hanhineva

引用次数: 0

Reflections on an International Career in Chemistry 对国际化学事业的思考。

IF 6.6 2区化学

Mass Spectrometry Reviews Pub Date : 2025-05-24 DOI: 10.1002/mas.21939

Richard B. Cole

引用次数: 0

Practical Applications of Secondary/Extractive Electrospray Ionization (SESI): A Versatile Tool for Real-Time Chemical Analysis. 二次/萃取电喷雾电离（SESI）的实际应用：实时化学分析的通用工具。