International Journal of Mass Spectrometry最新文献

{"title":"3 MV accelerator mass spectrometry measurements of 36Cl using the Isobar Separator for Anions","authors":"Erin L. Flannigan ,&nbsp;William E. Kieser ,&nbsp;Carley A. Crann ,&nbsp;Christof Vockenhuber ,&nbsp;Barbara B.A. Francisco","doi":"10.1016/j.ijms.2025.117433","DOIUrl":"10.1016/j.ijms.2025.117433","url":null,"abstract":"<div><div>A second low-energy injection line containing the Isobar Separator for Anions (ISA), a radiofrequency quadrupole reaction cell system, was installed on the 3 MV tandem accelerator system at the A. E. Lalonde (AEL) accelerator mass spectrometry (AMS) Laboratory. The suppression of ³⁶S via anion-gas reaction with NO₂ was evaluated for measurements of ³⁶Cl reference materials and a dilution series, using a 3 MV AMS system. The dilution series, with ³⁶Cl/Cl ratios ranging from 10⁻¹¹ to 10⁻¹⁵, were measured in comparison with external measurement. ³⁶Cl/Cl blank levels of (7 ± 4) x10⁻¹⁵ were reached. While ISA-AMS is not currently able to achieve sufficient separation for most ³⁶Cl applications, these measurements show progress towards routine measurement of ³⁶Cl and demonstrate the steps required to validate such measurements on lower energy AMS systems.</div></div>","PeriodicalId":338,"journal":{"name":"International Journal of Mass Spectrometry","volume":"511 ","pages":"Article 117433"},"PeriodicalIF":1.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143642304","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Plasmid-encoded gene expression of pathogenic bacteria by antibiotic induction as detected by MALDI-TOF-TOF mass spectrometry and top-down proteomic analysis","authors":"Clifton K. Fagerquist ,&nbsp;Yanlin Shi ,&nbsp;Mahesh Koirala","doi":"10.1016/j.ijms.2025.117430","DOIUrl":"10.1016/j.ijms.2025.117430","url":null,"abstract":"<div><div>Three previously genomically sequenced Shiga toxin-producing <em>E. coli</em> (STEC) strains of serotypes O43:H2, O103:H11, O111:H8 were analyzed by antibiotic induction, MALDI-TOF-TOF mass spectrometry and top-down proteomic analysis. In addition to detection and identification of phage-encoded Shiga toxin, we identified plasmid-encoded immunity proteins for colicin E8 and colicin D. Protein biomarkers were identified from b- and y-type fragment ions generated by the <em>aspartic acid effect</em> (AAE) that favors backbone cleavage on the C-terminal side of aspartic acid (D), glutamic acid (E) and asparagine (N) residues. Our in-house software was used for protein biomarker identification. Consistent with our previous report, we observed an apparent enhancement of the AAE when the residue on the C-terminal side of D-, E− or N-residues is a glycine (G). <em>In silico</em> predicted protein structures revealed that these DG, EG, NG sites of backbone breakage often correspond to flexible linker regions of the backbone. Finally, each pathogenic strain carried one or more large plasmids as well as a 6–8 kb plasmid that contained the colicin gene and its cognate immunity gene. Immediately upstream of the colicin gene was an SOS/LexA box to which the repressor protein (LexA) binds and blocks expression of genes downstream. Upon initiation of the SOS response by antibiotic induction, LexA undergoes self-cleavage and detachment allowing downstream gene expression. Thus, the presence of these small plasmids, their genes and the mechanism of expression is consistent with antibiotic induction and top-down proteomic analysis.</div></div>","PeriodicalId":338,"journal":{"name":"International Journal of Mass Spectrometry","volume":"511 ","pages":"Article 117430"},"PeriodicalIF":1.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143526898","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Evaluating use of laser ablation quadrupole inductively coupled plasma mass spectrometry for low concentration lead isotope measurements","authors":"Sophia M. Wensman ,&nbsp;Alyssa E. Shiel ,&nbsp;Chris J. Russo ,&nbsp;Adam J.R. Kent","doi":"10.1016/j.ijms.2025.117429","DOIUrl":"10.1016/j.ijms.2025.117429","url":null,"abstract":"<div><div>Lead (Pb) concentrations and isotopic compositions in environmental samples can provide important insights into Pb sources, pathways, and distributions. However, low Pb levels in many environmental samples present challenges for precise Pb isotopic measurements. This study evaluates the use of laser ablation quadrupole inductively coupled plasma mass spectrometry (LA-Q-ICP-MS) combined with collisional focusing and an Aerosol Rapid Introduction System (ARIS) for measuring Pb isotopes in reference materials with variable Pb concentrations (0.3–11 μg g⁻¹) and environmental samples (i.e., Pacific oyster shells) with Pb concentrations below 1 μg g⁻¹. Accuracy and precision were assessed using three glass reference materials (BCR-2G, BHVO-2G, and GOR128-G). For ²⁰⁶Pb/²⁰⁷Pb and ²⁰⁸Pb/²⁰⁷Pb ratios, measurements were within 0.2 % and 2.8 % of reported values for all reference materials, with decreased accuracy associated with low count rates. The precision was 0.4%–1.8 % relative standard deviation (RSD) for certified reference materials. Analytical uncertainty was lower for reference materials (∼1.2 % RSD for ²⁰⁶Pb/²⁰⁷Pb and ∼1.3 % RSD for ²⁰⁸Pb/²⁰⁷Pb) compared to oyster shells (∼3.6 % RSD for ²⁰⁶Pb/²⁰⁷Pb and ∼3.8 % RSD for ²⁰⁸Pb/²⁰⁷Pb), likely due to low Pb concentrations and sample heterogeneity. While Pb isotopic measurements demonstrated good repeatability across parallel transects of the same oyster shell (r = 0.7), the higher analytical uncertainties (&gt;0.5 % RSD) limit reliable source identification or apportionment in these natural samples. In approaching new studies with the methods presented here, researchers will need to determine if for a given application the uncertainties on measured sample Pb isotope ratios are sufficiently small.</div></div>","PeriodicalId":338,"journal":{"name":"International Journal of Mass Spectrometry","volume":"511 ","pages":"Article 117429"},"PeriodicalIF":1.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143521266","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The development of a novel double-focusing thermal ionization mass spectrometer","authors":"Xianglong Yuan ,&nbsp;Xiaopan Shen ,&nbsp;Lubaiyang Liu ,&nbsp;Feiteng Li ,&nbsp;Lili Jiang ,&nbsp;Lihua Zhai ,&nbsp;Hu Deng ,&nbsp;Leixin Yan ,&nbsp;Zhiming Li","doi":"10.1016/j.ijms.2025.117408","DOIUrl":"10.1016/j.ijms.2025.117408","url":null,"abstract":"<div><div>Unlike traditional Thermal Ionization Mass Spectrometers (TIMS) with single-focusing magnetic mass analyzers (such as Triton, Phoenix, Nu TIMS, etc.), a newly developed Double-Focusing Thermal Ionization Mass Spectrometer (DF-TIMS) enhances the system stability by mitigating accelerating high-voltage noise and drift. Featuring a Nier-Johnson type double-focusing mass analyzer, the instrument includes a laminated magnet with a 250 mm radius and a cylindrical Electrostatic Analyzer (ESA) with a 350 mm radius, achieving a mass dispersion of 560 mm. It is equipped with of 16 Faraday cups and 4 full-size discrete dynode secondary electron multipliers (SEM), combined with variable dispersion double quadrupole zoom optics, allowing for multi-collection of isotopes with up to 20 % mass dispersion, such as isotopes of Lithium, Boron and Calcium. Additionally, a compact and advanced Retarding Filter enhances abundance sensitivity from &lt; 2 ppm to &lt; 5 ppb. Automated tuning and measurement improve efficiency for both positive and negative ions. With a 0.2 mm source slit and a 1 mm receiving slit, DF-TIMS achieves a resolution over 470 and a peak shape factor below 0.3. System stability is less than 15 ppm/30 min credit to the double-focusing design. Each Faraday cup operates with a dynamic range of 0–50 V, featuring Root Mean Square (RMS) noise (4s integration, 10¹¹ Ω high resistance) under 20 μV and baseline drift below 1 × 10⁻¹⁶ A/h. The instrument has been applied extensively, delivering internal precision and external precision for Strontium and Neodymium measurements under 5 ppm, meeting stringent isotopic ratio analysis requirements in nuclear science and geoscience.</div></div>","PeriodicalId":338,"journal":{"name":"International Journal of Mass Spectrometry","volume":"510 ","pages":"Article 117408"},"PeriodicalIF":1.6,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143349790","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Rapid and accurate identification of microorganisms using ion mobility–mass spectrometry","authors":"Ahmed M. Hamid","doi":"10.1016/j.ijms.2025.117421","DOIUrl":"10.1016/j.ijms.2025.117421","url":null,"abstract":"<div><div>Accurate identification of microorganisms to the strain and substrain levels in clinical and environmental samples is essential to provide an appropriate antibiotherapy to the patients and reduce the prescription of broad-spectrum antimicrobials to minimize antibiotic resistance. Unfortunately, the current diagnosis methods are often slow, expensive, or laborious, which limits their use in resource-limited regions. Therefore, there is a strong unmet need for new technologies that can rapidly identify microorganisms in complex samples to complement the existing commercially available technologies. This Young Scientist Perspective demonstrates the value of combining the attributes of ion mobility-mass spectrometry and ambient ionization, enabling rapid and accurate discrimination of bacteria to the species level after only a 4-h culturing period and showing that various bacterial species can have different isomers and conformers of their biomarkers. However, to discriminate closely-related bacterial strains, we needed to include other separation techniques in our workflow, such as liquid chromatography. Also, we utilized whole organism fingerprints, which include metabolites, lipids, and peptides, using our optimized workflow and machine learning to analyze a wide set of <em>E. coli</em> strains in artificially contaminated urine samples. Moreover, the various challenges for routine identification of microorganisms using our optimized techniques in medical, environmental, and security fields and future outlooks are discussed.</div></div>","PeriodicalId":338,"journal":{"name":"International Journal of Mass Spectrometry","volume":"510 ","pages":"Article 117421"},"PeriodicalIF":1.6,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143437898","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Stepwise optimization of traveling wave profiles and inverse gating pattern in structure for lossless ion manipulation platform","authors":"Latif Mohsen ,&nbsp;Xi Chen ,&nbsp;Gandhi Viraj ,&nbsp;Hua Leyan ,&nbsp;Brian Clowers ,&nbsp;Carlos Larriba-Andaluz","doi":"10.1016/j.ijms.2025.117420","DOIUrl":"10.1016/j.ijms.2025.117420","url":null,"abstract":"<div><div>The Structure for Lossless Ion Manipulation (SLIM) platform is a powerful analytical separation tool allowing ultra-long serpentine separation path spanning hundreds of meters. In SLIM, transient fields called Traveling waves (T-wave) roll over the ions leading to separation, hence a Stepwise optimization of experimental operating conditions including amplitude, speed, and shape is essential. Here, we have characterized seven T-wave profiles including sine, triangle, square, ramp, reverse ramp, and two decreasing fields as a function of obtained resolution, resolving power and signal intensities. We found out that T-wave patterns with the most uniform electric field and least negative electric fields produce the highest resolution (reverse ramp). Both signal intensity and resolution are favorable at mid-range T-wave amplitude and speeds. The inverse gating could potentially improve the obtained resolutions as much as 35 %, in the case of reverse ramp, within 1.5 m of separation path.</div></div>","PeriodicalId":338,"journal":{"name":"International Journal of Mass Spectrometry","volume":"510 ","pages":"Article 117420"},"PeriodicalIF":1.6,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143403289","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Extraction anode lens effects in gas phase peptide cation-electron reactions","authors":"Steven A. DeFiglia ,&nbsp;Teresa Lee ,&nbsp;Neven N. Mikawy ,&nbsp;Carson W. Szot ,&nbsp;Kristina Håkansson","doi":"10.1016/j.ijms.2024.117390","DOIUrl":"10.1016/j.ijms.2024.117390","url":null,"abstract":"<div><div>Gas phase cation-electron reactions, from electron capture dissociation (ECD; &lt;1 eV electrons) to electron ionization dissociation (&gt;∼26 eV electrons), are highly beneficial for biomolecular structural characterization. These techniques offer high sequence coverage, labile posttranslational modification retention, and sidechain loss fragments which can differentiate isomeric residues. For optimum performance, careful tuning of electron energy, flux, and irradiation time is required to reach efficiency at a particular energy regime. The cathode bias voltage (CBV) is the primary determinant of electron energy, while several parameters including CBV, extraction anode lens voltage (LV), and cathode heating current determine electron flux. We present an in-depth examination of how the interplay of these parameters at variable irradiation times results in differing peptide cation-electron reaction regimes. A particularly interesting finding was the prominent high energy fragmentation pathways observed at low (∼−1.0 V) CBV and high (&gt;50 V) LV, as compared with conventional (∼5 V) LV for peptide ECD. Specifically, high LV resulted in tandem ionization, observed for both singly- and doubly protonated peptides, alongside increased sequence coverage for both charge states from complex spectra containing a multitude of <em>a/b/c′/d/w/x/y′/z•</em>-type terminal fragments as well as internal fragments and a large number of neutral losses. Electron flux and energy measurements as well as electron irradiation at constant flux showed that an increased number of higher energy electrons are present at high vs. low LV, i.e., the observed “lens effect” is likely due to the presence of high energy electrons under such conditions. This extraction anode lens effect may explain previous observations of unexpected internal fragments from ECD.</div></div>","PeriodicalId":338,"journal":{"name":"International Journal of Mass Spectrometry","volume":"509 ","pages":"Article 117390"},"PeriodicalIF":1.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143101187","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural differentiation of protein charge state conformers via gas-phase ion/ion cross-linking mass spectrometry","authors":"Woo-Young Kang,&nbsp;Arup Mondal,&nbsp;Alberto Perez,&nbsp;Boone M. Prentice","doi":"10.1016/j.ijms.2025.117410","DOIUrl":"10.1016/j.ijms.2025.117410","url":null,"abstract":"<div><div>Determining structures of multiply charged protein ions in mass spectrometry is critical for understanding the relationship between condensed-phase protein structures found in biological environments and gas-phase structures produced during electrospray ionization (ESI). The determination of collision cross-sections (CCSs) via ion mobility-mass spectrometry (IM-MS) has been used to study conformational changes as a function of protein charge state; however, this approach provides limited structural information on the overall topology of analytes. Recently developed gas-phase cross-linking mass spectrometry (XL-MS) performed via ion/ion reactions can probe local tertiary structures, providing an additional dimension to MS-based gas-phase structural biology studies. Herein, we demonstrate the conformational differentiation of alcohol-denatured, ESI-generated ubiquitin ions with varying charges (6+ through 11+) using gas-phase XL-MS. Gas-phase N-hydroxysulfosuccinimide (NHS) ester chemistry is performed using sodiated ethylene glycol bis(sulfosuccinimidyl succinate) (sulfo-EGS) cross-linkers to covalently modify neutral and charged basic amino acid residues. This method provides sufficient sensitivity to detect subtle conformational changes in local tertiary structures specific to each charge state. These results reveal that 6+ through 8+ charge states of ubiquitin adopt folded conformations, while the 9+ through 11+ charge states exhibit unfolded structures. This trend is consistent with the bimodal charge state distribution observed in the ESI mass spectrum of alcohol-denatured ubiquitin. Overall, this gas-phase XL-MS method enables the examination of conformational changes in gas-phase proteins of varying charge states at the local tertiary structural motif level, providing a novel gas-phase structural biology approach that complements existing MS-based methods.</div></div>","PeriodicalId":338,"journal":{"name":"International Journal of Mass Spectrometry","volume":"509 ","pages":"Article 117410"},"PeriodicalIF":1.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143101186","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Determining organophosphorus pesticides in agriculture: A combined approach of ion-mobility spectrometry with robust principal component analysis and multivariate adaptive regression splines","authors":"Abdollah Azad,&nbsp;Mohammadreza Khanmohammadi Khorrami,&nbsp;Mahsa Mohammadi","doi":"10.1016/j.ijms.2025.117407","DOIUrl":"10.1016/j.ijms.2025.117407","url":null,"abstract":"<div><div>The high toxicity and widespread use of organophosphorus pesticides (OPPs) in agriculture make their accurate detection and quantification a critical challenge. Traditional analytical techniques like gas chromatography (GC) and high-performance liquid chromatography (HPLC) face limitations due to their cost, time-consuming procedures, and labor intensity. This study explores a novel analytical approach that utilizes robust principal component analysis (rPCA) and multivariate adaptive regression splines (MARS) to enable the determination of OPPs using ion mobility spectrometry (IMS). IMS data were compressed using rPCA to identify the principal components (PCs) that best capture the relevant information.</div><div>Kenard Stone algorithm was employed to create the calibration and test sets for model development and validation, respectively. The calibration set (containing 35 samples and 6 PCs) was used to train the rPCA-MARS model. Principal Component Regression (PCR) and Partial Least Squares Regression (PLS-R) models were compared for their ability to predict the quantitative values of OPPs to the rPCA-MARS model. The efficiency of the rPCA-MARS model was evaluated using several metrics: R-squared (R²), R² estimated by generalized cross-validation (R²_GCV), adjusted R-squared (R²_adj), sum of squared errors (SSE), and mean square error (MSE). The optimal rPCA-MARS model utilized 7 basis functions to effectively characterize the OPPs values.</div><div>The linear rPCA-MARS model for Ethion performs well on both the calibration and test sets. The piecewise-cubic rPCA-MARS model achieved excellent performance on the calibration set, with R² = 0.995, R²_adj = 0.994, and SSE = 0.368. The test set results were equally impressive, showing R² = 0.993, R²_adj = 0.993, and SSE = 0.220. The cubic rPCA-MARS model exhibited exceptional predictive performance and generalizability, achieving a low MSE of 0.012 and a high R²_GCV of 0.992. These results underscore the superior predictive capability of the rPCA-MARS framework for Ethion determination in this study. Building on the success with Ethion, the rPCA-MARS model shows promise for predicting concentrations of Malathion and Phosalone.This finding highlights the model's potential for broader applications in OPPs analysis in agriculture. This paves the way for developing rapid, cost-effective, and environmentally friendly methods for monitoring and managing OPPs within agricultural ecosystems.</div></div>","PeriodicalId":338,"journal":{"name":"International Journal of Mass Spectrometry","volume":"509 ","pages":"Article 117407"},"PeriodicalIF":1.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143101188","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Influence of mass spectrometry source settings on native protein ion mobility mass spectrometry measurements","authors":"Mack Shih,&nbsp;Patrick J. Faustino,&nbsp;Thomas F. O'Connor,&nbsp;Jinhui Zhang","doi":"10.1016/j.ijms.2025.117411","DOIUrl":"10.1016/j.ijms.2025.117411","url":null,"abstract":"<div><div>Ion mobility mass spectrometry is emerging as a useful tool to probe native protein structural information. Advance ion mobility methods like collision-induced unfolding (CIU) can be used to characterize proteins’ conformational dynamics. The impact of instrument source conditions on the native protein conformations is not well characterized or standardized. High values of drying gas temperature and gas flow parameters on the Agilent IM-QTOF instrument were shown to apply collision-induced unfolding (CIU) effects on protein ions ionized from physiological solution condition. Ion conformation heat maps of model proteins ubiquitin, myoglobin, and bovine serum albumin were obtained using a novel CIU method utilizing high drying gas temperature and varying drying gas flow. Protein charge states also increased as drying gas flow was increased at high temperature indicating a thermal heating element. Overall, drying gas temperature and gas flow on IM-QTOF and the associated impacts on ionic structure need to be considered when using ion mobility mass spectrometry technology to assess protein structure.</div></div>","PeriodicalId":338,"journal":{"name":"International Journal of Mass Spectrometry","volume":"509 ","pages":"Article 117411"},"PeriodicalIF":1.6,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143101209","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}