Mass Spectrometry Reviews最新文献

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Antithrombin: Deficiency, Diversity, and the Future of Diagnostics 抗凝血酶:缺乏、多样性和诊断的未来。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2025-03-15 DOI: 10.1002/mas.21929
Mirjam Kruijt, Christa M. Cobbaert, L. Renee Ruhaak
{"title":"Antithrombin: Deficiency, Diversity, and the Future of Diagnostics","authors":"Mirjam Kruijt,&nbsp;Christa M. Cobbaert,&nbsp;L. Renee Ruhaak","doi":"10.1002/mas.21929","DOIUrl":"10.1002/mas.21929","url":null,"abstract":"<p>Our healthcare system provides reactive sick-care, treating patients after symptoms have appeared by prescription of generic and often suboptimal therapy. This strategy brings along high costs and high pressure which is not sustainable. Alternatively, P5 healthcare is proposed focusing on five key elements: prevention, personalization, prediction, participation, psychocognition, however, changes in current clinical care pathways are required, for which antithrombin deficiency is a prime example. Hereditary antithrombin deficiency (ATD) is a genetic disorder, for which screening is instigated after a thrombotic episode. Current diagnostic tests for ATD lack sensitivity and refinement to correctly classify patients, and generic treatments are prescribed. A molecular understanding of ATD through a molecular diagnostic test that analyzes all clinically relevant features of antithrombin is required. Here, clinically relevant molecular characteristics of antithrombin, the diversity of antithrombin (deficiency) in heath and disease, and the strengths and weaknesses of antithrombin tests are reviewed. A mass spectrometry test that molecularly characterizes a patients antithrombin proteoforms harbors the highest potential to improve the clinical pathway for ATD. Application of this MS-based test in a future enhanced clinical pathway will improve patient management and outcome through molecular characterization of antithrombin and enables the promise of P5 healthcare for ATD.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"745-768"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/mas.21929","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143633284","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
Mass Spectrometry Analysis of Nucleic Acid Modifications: From Beginning to Future 核酸修饰的质谱分析:从起点到未来。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2024-09-22 DOI: 10.1002/mas.21907
Yixuan Xie, Carolina Brás-Costa, Zongtao Lin, Benjamin A. Garcia
{"title":"Mass Spectrometry Analysis of Nucleic Acid Modifications: From Beginning to Future","authors":"Yixuan Xie,&nbsp;Carolina Brás-Costa,&nbsp;Zongtao Lin,&nbsp;Benjamin A. Garcia","doi":"10.1002/mas.21907","DOIUrl":"10.1002/mas.21907","url":null,"abstract":"<div>\u0000 \u0000 <p>Nucleic acids are fundamental biological molecules that encode and convey genetic information within living organisms. Over 150 modifications have been found in nucleic acids, which are involved in critical biological functions, including regulating gene expression, stabilizing nucleic acid structure, modulating protein translation, and so on. The dysregulation of nucleic acid modifications is correlated with many diseases such as cancers and neurological disorders. However, it is still challenging to simultaneously characterize and quantify diverse modifications using traditional genomic methods. Mass spectrometry (MS) has served as a crucial tool to solve this issue, and can directly identify the modified species through their distinct mass differences compared to the canonical ones and provide accurate quantitative information. This review surveys the history of nucleic acid modification discovery, advancements in MS-based methods, nucleic acid sample preparation, and applications in biological and medical research. We expect the high-throughput and valuable quantitative information from MS analysis will be more broadly applied to studying nucleic acid modification status in different pathological conditions, which is key to filling gaps in traditional genomics and transcriptomics research and enabling researchers to gain insights into epigenetics and epitranscriptomics.</p></div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"624-643"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142277683","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
Advances in Fragmentation Techniques for Glycomics and Glycoproteomics 糖组学和糖蛋白组学的片段化技术进展。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-06-07 Epub Date: 2025-10-26 DOI: 10.1002/mas.70011
Vishal Sandilya, Sarah Sahioun, Tanjina Akter Suma, Abiodun Adewolu, Abderrahman Koraich, Shafia Shafiq Nishe, Esther Oji, Cristian D. Gutierrez Reyes, Yehia Mechref
{"title":"Advances in Fragmentation Techniques for Glycomics and Glycoproteomics","authors":"Vishal Sandilya,&nbsp;Sarah Sahioun,&nbsp;Tanjina Akter Suma,&nbsp;Abiodun Adewolu,&nbsp;Abderrahman Koraich,&nbsp;Shafia Shafiq Nishe,&nbsp;Esther Oji,&nbsp;Cristian D. Gutierrez Reyes,&nbsp;Yehia Mechref","doi":"10.1002/mas.70011","DOIUrl":"10.1002/mas.70011","url":null,"abstract":"<div>\u0000 \u0000 <p>Glycosylation, the enzymatic addition of carbohydrate moieties to proteins, is essential for immune recognition, protein folding, and disease progression. The structural complexity of glycans and the heterogeneity of glycosylation sites present significant challenges towards accurate identification and quantification, necessitating advanced methodologies for comprehensive characterization. Tandem MS (MS/MS) has emerged as the primary analytical platform for glycomics and glycoproteomics. This review highlights the recent developments in fragmentation techniques, ranging from well-established techniques such as CID/HCD and ETD, to newer and more advanced techniques such as electron-based methods (EThcD), photodissociation strategies (UVPD, IRMPD), and hybrid approaches (sceHCD, EThcD-sceHCD, HCD-pd-ETD), each providing distinct advantages towards glycan structure elucidation and glycosite mapping. This review also discusses emerging computational strategies, especially deep learning for automated interpretation of complex glycomics and glycoproteomics data.</p>\u0000 </div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 4","pages":"851-873"},"PeriodicalIF":6.6,"publicationDate":"2026-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145372121","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
Recent Advances in Top-Down Proteomics for Single-Cell Research. 自上而下蛋白质组学在单细胞研究中的最新进展。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-05-14 DOI: 10.1002/mas.70031
Jake A Melby, Pei Su, Fabio P Gomes
{"title":"Recent Advances in Top-Down Proteomics for Single-Cell Research.","authors":"Jake A Melby, Pei Su, Fabio P Gomes","doi":"10.1002/mas.70031","DOIUrl":"https://doi.org/10.1002/mas.70031","url":null,"abstract":"<p><p>Individual cells have distinctive molecular characteristics, including biologically relevant proteoforms. Although single-cell (SC) molecular omics offer unprecedented insights into cellular heterogeneity and function, the characterization of proteoforms in SCs remains an uncharted territory. Mass spectrometry (MS)-based proteomics is a key technology for analyzing proteins and their proteoforms in SCs. Top-down proteomics (TDP) is the MS technique of choice to characterize proteoforms from the bulk of cellular extracts. TDP has also shown proficiency in characterizing these biomolecules in SC. Recent advances in sample processing, separation techniques, MS instrumentation, and computational approaches have evolved the application of TDP to SC analysis, overcoming longstanding technical barriers and opening new avenues for large-scale studies. This review discusses the importance of TDP for profiling proteoforms within SC and provides examples of the biological relevance of these biomolecules. Furthermore, this review describes recent advances in the TDP for SC research while providing a detailed overview of MS-based methods for analysis of proteoforms in individual cells. The potential and limitations of these MS-based approaches are discussed, along with perspectives about the future direction of the SC-TDP field.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":" ","pages":""},"PeriodicalIF":6.6,"publicationDate":"2026-05-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147939789","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
Applications of Top-Down Protein Analysis in Clinical Diagnostics. 自顶向下蛋白质分析在临床诊断中的应用。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-05-12 DOI: 10.1002/mas.70030
Morgan W Mann, Priscilla S-W Yeung, Ruben Y Luo
{"title":"Applications of Top-Down Protein Analysis in Clinical Diagnostics.","authors":"Morgan W Mann, Priscilla S-W Yeung, Ruben Y Luo","doi":"10.1002/mas.70030","DOIUrl":"https://doi.org/10.1002/mas.70030","url":null,"abstract":"<p><p>This review evaluates the applications of top-down mass spectrometry (TDMS) and intact mass measurement of proteins in clinical laboratories. Both methods involve the measurement of intact proteins in a mass spectrometer without the use of enzymatic or chemical digestion to convert the protein into smaller peptides, and TDMS includes fragmentation of selected proteins. These analytical techniques offer significant advantages in the ability to distinguish pathologically relevant proteoforms from nonpathologic proteoforms compared to alternative immunoassays, and the potential to reduce laboratory turnaround times relative to proteolysis-aided approaches. As a result, TDMS and intact MS have already penetrated the clinical laboratory for many tests that require high analytical specificity and high throughput. This article describes several examples for which TDMS and intact MS methods are currently used in clinical diagnostics, including hemoglobinopathy determination, myeloma isotyping, transferrin glycosylation measurement, and the quantitation of endogenous and exogenous hormones (e.g., insulin and therapeutic variants), while examining new TDMS-based clinical tests which may soon be offered in clinical laboratories. The overall outlook of future TDMS clinical testing is also discussed.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":" ","pages":""},"PeriodicalIF":6.6,"publicationDate":"2026-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147872527","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
Recent Advances (2023-2025) of Capillary Electrophoresis-Mass Spectrometry (CE-MS) for Top-Down Proteomics. 毛细管电泳-质谱(CE-MS)用于自上而下蛋白质组学的最新进展(2023-2025)。
IF 6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-05-07 DOI: 10.1002/mas.70028
Guijie Zhu, David A Alvarez Rodriguez, Noah Gould, Alexander R Ivanov, Kevin Jooß, Liangliang Sun
{"title":"Recent Advances (2023-2025) of Capillary Electrophoresis-Mass Spectrometry (CE-MS) for Top-Down Proteomics.","authors":"Guijie Zhu, David A Alvarez Rodriguez, Noah Gould, Alexander R Ivanov, Kevin Jooß, Liangliang Sun","doi":"10.1002/mas.70028","DOIUrl":"10.1002/mas.70028","url":null,"abstract":"<p><p>Top-down proteomics (TDP) characterizes proteoforms in cells, tissues, and biofluids, in discovery mode and on a global scale, requiring analytical tools with high peak capacity for proteoform separation and high sensitivity for proteoform detection, given the extremely high proteoform complexity and wide proteoform concentration dynamic range. Capillary electrophoresis-mass spectrometry (CE-MS) has become an essential tool for TDP in various biomedical applications due to its excellent separation efficiency and high measurement sensitivity for proteoforms, especially with continued improvements in reproducibility and robustness over the last several years. This review summarizes the technological advancements and biomedical applications of CE-MS-based TDP in the last 3 years (2023-2025) and offers brief perspectives at the end.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":" ","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147831584","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
A Perspective of Multi-Reflecting TOF MS 透视多反射 TOF MS。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-04-08 Epub Date: 2024-11-12 DOI: 10.1002/mas.21915
A. N. Verenchikov, V. V. Makarov, A. V. Vorobyev, S. N. Kirillov
{"title":"A Perspective of Multi-Reflecting TOF MS","authors":"A. N. Verenchikov,&nbsp;V. V. Makarov,&nbsp;A. V. Vorobyev,&nbsp;S. N. Kirillov","doi":"10.1002/mas.21915","DOIUrl":"10.1002/mas.21915","url":null,"abstract":"<p>Time-of-flight mass spectrometry (TOF MS) excels in rapid and high-sensitivity analysis, making it a cornerstone of analytical chemistry. But as sample complexity explodes in omics studies, so does the need for higher resolving power to ensure accurate results. Traditional TOF instruments face a challenge: achieving high resolution often requires a very large instrument. To overcome this limitation, scientists developed alternative designs for TOF analyzers called multi-pass TOF analyzers (MPT). These MPT analyzers come in two main configurations: multi-turn (MTT) and multi-reflecting (MRT). Drawing on the authors’ extensive experience, this review describes two decades of MPT advancements. It highlights the critical development of optimized analyzer designs, tracing the evolution towards mirror-based MRT instruments, generally providing superior resolution and spatial acceptance compared to MTT. While the manuscript attempts to overview MTT advances, it primarily focuses on MRT technology. Additionally, the review explores the role of orthogonal accelerators and trap pulse converters, comparing their efficiency and the dynamic range limits imposed by space charge effects. By comparing various MRT configurations and commercially available instruments, the review sets out to inform and empower researchers so they can make informed decisions about MRT mass spectrometers.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 3","pages":"476-506"},"PeriodicalIF":6.6,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13062609/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142613259","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
Cold EI—The Way to Improve GC-MS and Increase Its Range of Applications 改进气相色谱-质谱法并扩大其应用范围的途径。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-04-08 Epub Date: 2025-03-05 DOI: 10.1002/mas.21928
Aviv Amirav, Benny Neumark, Oneg Elkabets, Alex Yakovchuk
{"title":"Cold EI—The Way to Improve GC-MS and Increase Its Range of Applications","authors":"Aviv Amirav,&nbsp;Benny Neumark,&nbsp;Oneg Elkabets,&nbsp;Alex Yakovchuk","doi":"10.1002/mas.21928","DOIUrl":"10.1002/mas.21928","url":null,"abstract":"<p>Gas chromatography-mass spectrometry (GC-MS) with Cold electron ionization (EI) is based on interfacing the GC and MS with a supersonic molecular beam (SMB) along with electron ionization of vibrationally cold sample compounds in the SMB in a contact-free fly-through ion source (hence the name Cold EI). Cold EI improves all the central performance aspects of GC-MS, including: a significantly extended range of compounds that are amenable for analysis, enhanced molecular ions, highly improved sample identification, faster analysis (much faster), uniform response to all analytes, greater selectivity and higher signal to noise ratios and lower limits of detection, particularly for compounds that are difficult to analyze. GC-MS with Cold EI executes the analysis of the full range of standard EI applications and most with major improvements of various metrics. Furthermore, it significantly extends the range of compounds and applications amenable for GC-MS analysis. Accordingly, it is a highly superior replacement ion source. In this review article, we describe Cold EI and its main features, discuss its benefits, and demonstrate several of its unique applications including cannabinoids analysis, synthetic organic compounds analysis, whole blood analysis for medical diagnostics, isomer distribution analysis for improved fuels and oils, and explosives analysis.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 3","pages":"548-582"},"PeriodicalIF":6.6,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13062617/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143565717","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
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-04-08
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 3","pages":"453-454"},"PeriodicalIF":6.6,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148067972","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
Deep Learning Methods for De Novo Peptide Sequencing 全新肽段测序的深度学习方法。
IF 6.6 2区 化学
Mass Spectrometry Reviews Pub Date : 2026-04-08 Epub Date: 2024-11-29 DOI: 10.1002/mas.21919
Wout Bittremieux, Varun Ananth, William E. Fondrie, Carlo Melendez, Marina Pominova, Justin Sanders, Bo Wen, Melih Yilmaz, William S. Noble
{"title":"Deep Learning Methods for De Novo Peptide Sequencing","authors":"Wout Bittremieux,&nbsp;Varun Ananth,&nbsp;William E. Fondrie,&nbsp;Carlo Melendez,&nbsp;Marina Pominova,&nbsp;Justin Sanders,&nbsp;Bo Wen,&nbsp;Melih Yilmaz,&nbsp;William S. Noble","doi":"10.1002/mas.21919","DOIUrl":"10.1002/mas.21919","url":null,"abstract":"<div>\u0000 \u0000 <p>Protein tandem mass spectrometry data are most often interpreted by matching observed mass spectra to a protein database derived from the reference genome of the sample being analyzed. In many application domains, however, a relevant protein database is unavailable or incomplete, and in such settings <i>de novo</i> sequencing is required. Since the introduction of the DeepNovo algorithm in 2017, the field of <i>de novo</i> sequencing has been dominated by deep learning methods, which use large amounts of labeled mass spectrometry data to train multi-layer neural networks to translate from observed mass spectra to corresponding peptide sequences. Here, we describe these deep learning methods, outline procedures for evaluating their performance, and discuss the challenges in the field, both in terms of methods development and evaluation protocols.</p>\u0000 </div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 3","pages":"507-526"},"PeriodicalIF":6.6,"publicationDate":"2026-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142749501","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
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