Mass Spectrometry Reviews最新文献

This review traces the first 20 years of Orbitrap mass spectrometry as a mainstream high‑resolution and accurate‑mass (HR/AM) technology. It outlines the historical development of the Orbitrap analyzer, the evolution of major instrument families, and the key technological innovations that enabled its widespread adoption. Particular emphasis is placed on hybrid and Tribrid architectures, democratization of HR/AM through benchtop platforms, extension to high‑mass and native analysis, and integration with ion mobility, advanced fragmentation methods, and emerging applications such as structural biology, isotope ratio measurements, and space research. The review concludes with a perspective on future directions and the anticipated role of Orbitrap instrumentation as the core workhorse in analytical laboratories worldwide.

The use of MALDI mass spectrometry for the analysis of carbohydrates and glycoconjugates is a well-established technique and this comprehensive review is the twelfth update of the original article published in 1999 and brings coverage of the literature to the end of 2024. Although still popular for glycoconjugate analysis, recent years have seen a slight drop in its usage with electrospray and LC-MS techniques becoming more widely used. The review follows the same general format as previous reviews. Much of the material relating to applications is presented in tabular form whereas papers relating to method development are discussed in more detail. The review is divided into three sections: (1) general aspects such as theory of the MALDI process, matrices, derivatization, MALDI imaging, fragmentation, quantification, and the use of computer software for structural identification. (2) Applications to various structural types such as oligo- and polysaccharides, glycoproteins, glycated proteins, glycolipids and natural products, and (3) other general areas such as medicine, biopharmaceuticals, industrial processes and glycan synthesis where MALDI is extensively used. As with previous reviews in this series, this review also includes a few papers that describe methods appropriate to analysis by MALDI, such as sample preparation, even though the ionization method is not MALDI. Much of this work is tabulated. MALDI is still an ideal technique for carbohydrate analysis, particularly in its rapidity, ease of use and its ability to produce single ions from each analyte. Improvements in the technique and range of applications show little sign of diminishing.

Identification of a chemical agent yields insights into its physicochemical properties. By examining the intrinsic characteristics and environment of a compound, information about its history can be gathered. The main objective of authentication/forensic approaches to chemicals is to trace the history of the compound's origin, regardless of its nature (e.g., environmental pollutants, drugs, or toxicants). This review presents several scientific fields that share a common objective: using mass spectrometry (MS) to obtain source information from diverse samples and chemicals. From targeted analysis to the full screening of non-targeted chemical space, direct and coupled MS approaches provide powerful capabilities for addressing source-determination concerns, as described in this review. Novel sampling and ionization methods have proven to have a significant impact on expanding MS applications across diverse sample types. This review covers the main methods for determining chemical origins, ranging from targeted confirmation of known compounds to non-targeted identification of unknown compounds under challenging experimental and matrix-related conditions.

The proteome is a dynamic landscape of proteoforms arising from genetic mutations, alternative splicing, and post-translational modifications (PTMs), which collectively drive biological function and disease phenotypes. Mass spectrometry (MS)-based proteomics has emerged as an essential technique for elucidating this molecular complexity. Although bottom-up proteomics enables deep protein identification and quantification through peptide-level analysis, it disrupts molecular connectivity and introduces a peptide-to-protein inference problem, which is suboptimal for proteoform analysis. Top-down proteomics (TDP) offers a complementary approach by analyzing intact proteins, preserving molecular connectivity, and enabling direct characterization and quantification of proteoforms. This capability is increasingly vital for understanding heterogeneous human diseases. Here, we review the evolving role of TDP in biomedical research, highlighting studies that revealed proteoform-level alterations, identified candidate biomarkers, and advanced our understanding of the roles of proteoforms in human diseases.

The high prevalence and substantial burden of kidney diseases necessitate advanced approaches to elucidate molecular mechanisms and promote precision medicine. Mass spectrometry (MS)-based proteomics has evolved into a widely used analytical platform, delivering high-sensitivity, high-throughput protein profiling capabilities that have contributed substantially to biomarker discovery, mechanistic dissection, and therapeutic target identification across a broad range of kidney diseases. This review provides a comprehensive overview of MS-based proteomics applications in kidney disease research, covering progress in biomarker identification, pathogenic mechanism interrogation, and clinical translation. It highlights methodological advances, emerging trends, and persistent challenges that shape the field. Existing literature has uncovered abundant disease-specific biomarkers and revealed key pathogenic pathways, including podocyte injury-associated protein interaction networks, dysregulated complement activation, and metabolic reprogramming, and have critically assessed their translational potential. Additionally, investigations into posttranslational modifications such as phosphorylation and glycosylation have provided valuable insights for targeted therapies. Collectively, these findings illustrate the contributions of MS-based proteomics to the characterization of disease molecular heterogeneity, the identification of key pathogenic drivers, and the development of precision medicine approaches. This review further addresses current challenges in clinical applications, including sample heterogeneity, data complexity, and standardization issues. We additionally emphasize the critical need for minimum reporting standards and multicenter harmonization to accelerate the clinical translation of renal proteomics. Future research should focus on integrating multiomics and artificial intelligence-driven data mining to enhance precise disease subtyping, dynamic monitoring, and personalized treatment strategies.