Journal of the American Society for Mass Spectrometry最新文献

{"title":"Absorption Mode Broadband 2D MS for Proteomics and Metabolomics","authors":"Maria A. van Agthoven*,&nbsp;, ,&nbsp;Marek Polák,&nbsp;, ,&nbsp;Jan Fiala,&nbsp;, ,&nbsp;Claude Nelcy Ounounou,&nbsp;, ,&nbsp;Petr Halada,&nbsp;, ,&nbsp;Michael Palasser,&nbsp;, ,&nbsp;Anne Briot-Dietsch,&nbsp;, ,&nbsp;Alan Kádek,&nbsp;, ,&nbsp;Kathrin Breuker,&nbsp;, ,&nbsp;Petr Novák,&nbsp;, ,&nbsp;Carlos Afonso,&nbsp;, and ,&nbsp;Marc-André Delsuc,&nbsp;","doi":"10.1021/jasms.6c00007","DOIUrl":"10.1021/jasms.6c00007","url":null,"abstract":"<p >Two-dimensional mass spectrometry (2D MS) is a method for tandem mass spectrometry that enables the correlation between precursor and fragment ions without the need for ion isolation. On a Fourier transform ion cyclotron resonance mass spectrometer, the phase correction functions for absorption mode data processing were found to be linear in the precursor ion dimension and quadratic in the fragment ion dimension. Phase-corrected absorption mode data processing on limited data sets has previously shown improvements in signal-to-noise ratio (SNR) and resolving power by a factor of 2. Here, we have expanded phase-corrected absorption mode data processing to 2D mass spectra regardless of size and frequency range. We have applied phase-corrected absorption mode 2D MS to top-down analysis of variously oxidized ubiquitin proteoforms generated by fast photochemical oxidation of proteins (FPOP) and to an extract of ergot alkaloids. We show that phase-corrected absorption mode data processing significantly improves both the SNR and the resolving power of the 2D mass spectrum compared to standard magnitude mode in terms of sequence coverage in top-down proteomics, as well as the accuracy of precursor-fragment correlation in metabolomics.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 5","pages":"1207–1217"},"PeriodicalIF":2.7,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147759179","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}

{"title":"Roles of FXR in Lipid Biochemistry within Hepatocellular Carcinoma Using MALDI MSI","authors":"Kayle J. Bender,&nbsp;, ,&nbsp;Ying Hu,&nbsp;, ,&nbsp;Blanca R. Teodoro,&nbsp;, ,&nbsp;Chuo Ying Zhai,&nbsp;, ,&nbsp;Yu-Jui Yvonne Wan*,&nbsp;, and ,&nbsp;Elizabeth K. Neumann*,&nbsp;","doi":"10.1021/jasms.5c00365","DOIUrl":"10.1021/jasms.5c00365","url":null,"abstract":"<p >Hepatocellular carcinoma (HCC) is a common type of cancer with a high mortality rate, which is affected by the farnesoid X receptor (FXR) in the liver. FXR is a ligand-activated nuclear receptor involved in lipid metabolism and homeostasis. Matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI MSI) enables spatially resolved molecular analysis and is particularly suited to profiling lipid distributions within tissues. In this study, MALDI MSI was employed to investigate alterations in liver lipid composition associated with HCC and FXR expression with a focus on phosphatidylcholine (PC) species. Distinct spatial and compositional differences in PC lipids were observed between HCC and nontumorous regions. Furthermore, we hypothesize a role of PC(38:4) in HCC based on cell culture experiments in which Hep3B cells were incubated in the presence of PC(38:4).</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 5","pages":"1102–1112"},"PeriodicalIF":2.7,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/jasms.5c00365","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147759248","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}

{"title":"Faces of Mass Spectrometry/Jane Gale","authors":"Anne Brenner*,&nbsp; and ,&nbsp;J. D. Brookbank,&nbsp;","doi":"10.1021/jasms.6c00090","DOIUrl":"10.1021/jasms.6c00090","url":null,"abstract":"","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 5","pages":"1038–1040"},"PeriodicalIF":2.7,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147508623","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}

{"title":"Mass Spectrometric Determination of Site-Specific O-Acetylation in Rhamnogalacturonan I Oligomers","authors":"Liyanage Devthilini Fernando,&nbsp;, ,&nbsp;Xu Yang,&nbsp;, ,&nbsp;Stephanie Archer-Hartmann,&nbsp;, ,&nbsp;Lubana Shahin,&nbsp;, ,&nbsp;Liang Zhang,&nbsp;, ,&nbsp;Breeanna R. Urbanowicz,&nbsp;, ,&nbsp;Christian Heiss,&nbsp;, and ,&nbsp;Parastoo Azadi*,&nbsp;","doi":"10.1021/jasms.5c00440","DOIUrl":"10.1021/jasms.5c00440","url":null,"abstract":"<p ><i>O</i>-acetylation, a common modification in rhamnogalacturonan I (RG-I), is critical for various biological processes, including plant growth, stress responses, and pathogen defense. Precise determination of the degree and specific positions of acetylation is therefore essential. To date, nuclear magnetic resonance (NMR) and tandem mass spectrometry have been employed to identify <i>O</i>-acetyl positions in pectin oligosaccharides. Although NMR is effective, it requires pure, high-concentration samples. Tandem mass spectrometry (MS), which uses smaller sample amounts, faces challenges due to <i>O</i>-acetyl migration between monosaccharide positions. The multiple steps in pectin sample analysis can further promote <i>O</i>-acetyl migration, especially near free hydroxyl groups. Moreover, during tandem MS, <i>O</i>-acetyl groups may detach, complicating the accurate tracking. This study presents an approach to lock <i>O</i>-acetyl groups by introducing trideuteroacetyl and propionyl substituents onto free hydroxyls of RG-I or partially acetylated RG-I. By combining matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) MS and electrospray ionization (ESI) MS with MS/MS or tandem mass spectrometry (MSⁿ), we devised a way to determine the monosaccharide sequence in the oligomer and the precise positions of <i>O</i>-acetyl groups in partially acetylated RG-I. This method enables the study of the regiospecificity of recombinant pectin <i>O</i>-acetyltransferases and can be applied to other oligosaccharides to determine acyl positions.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 5","pages":"1160–1172"},"PeriodicalIF":2.7,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/jasms.5c00440","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147571574","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}

{"title":"Mass Spectrometry-Based Proteomics Methods for Systematic Identification and Quantification of Protein O-Glycosylation in Complex Biological Samples","authors":"Longping Fu,&nbsp;, ,&nbsp;Xing Xu,&nbsp;, and ,&nbsp;Ronghu Wu*,&nbsp;","doi":"10.1021/jasms.6c00005","DOIUrl":"10.1021/jasms.6c00005","url":null,"abstract":"<p >Protein O-glycosylation is one of the most common and important modifications in human cells. It regulates protein folding, trafficking, stability, and interactions with other molecules, and its dysregulation is directly related to numerous diseases such as cancer and neurodegenerative diseases. Modern mass spectrometry (MS)-based proteomics provides a unique opportunity to systematically characterize O-glycosylated proteins. However, it is still extremely challenging due to the low abundance of many glycoproteins, the heterogeneity of O-glycans, and the complexity of biological samples. In this review, we discuss recent advances in MS-based proteomics methods designed to overcome the challenges for global and site-specific characterization of protein O-glycosylation. We begin with an overview of the biosynthetic pathways underlying the major classes of protein O-glycosylation. Then, we discuss different methods to enrich O-glycopeptides with diverse structures of O-glycans. Furthermore, various MS dissociation techniques for intact glycopeptide profiling are covered. In addition, different quantitative approaches are included for studying protein O-glycosylation in biological and biomedical research. We also discuss computational tools for intact O-glycopeptide identification, highlighting the challenges in search space requirement, false discovery rate control, and glycosylation site localization. The advancements of MS-based glycoproteomics are critical for gaining insights into the critical roles of protein O-glycosylation in biology and human disease.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 5","pages":"1041–1063"},"PeriodicalIF":2.7,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/jasms.6c00005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147615721","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}

{"title":"Changes to the JASMS Associate Editor Team: Farewell and Welcome","authors":"Jenny Brodbelt*,&nbsp;","doi":"10.1021/jasms.6c00098","DOIUrl":"10.1021/jasms.6c00098","url":null,"abstract":"","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 5","pages":"1035"},"PeriodicalIF":2.7,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147721276","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}

{"title":"Use of Ion Oscillation Phase Values for Peak Classification and Noise Filtering Efficiency Estimation in Orbitrap Mass Spectra of Natural Organic Matter","authors":"Alexander A. Potemkin*,&nbsp;, ,&nbsp;Mikhail A. Proskurnin,&nbsp;, and ,&nbsp;Dmitry S. Volkov*,&nbsp;","doi":"10.1021/jasms.5c00383","DOIUrl":"10.1021/jasms.5c00383","url":null,"abstract":"<p >An unprocessed high-resolution mass spectrum of natural organic matter contains tens of thousands of peaks, many of which are uninformative and associated with noise. Several noise filtering algorithms have been proposed in an attempt to remove them, but there is still no universal solution. Therefore, given the rapid development of high-resolution mass spectrometry and its increasing use in various scientific fields, it is essential to improve existing noise filtering algorithms and develop new ones. Previously proposed solutions have used peak properties such as intensity, mass-to-charge ratio, or peak reproducibility. In this paper, we propose using another physical property to eliminate noise: the phase values of ion oscillations. These values can be obtained from the Fourier transform of raw Orbitrap transient signals. Our newly developed noise filtering algorithm classifies mass spectrometry peaks into two groups based on the phase values at their maxima. Then it uses this information to calculate the appropriate intensity threshold. The algorithm was tested on mass spectra of humic substances and showed good agreement with methods previously reported in the literature. The results obtained using our algorithm indicate that signals with anomalous phase values are mostly uninformative or related to noise. Finally, we propose an algorithm for the evaluation of noise removal efficiency. It takes into account the ratio of the number of peaks with normal and anomalous phase values that will be removed at a given intensity threshold. The algorithm can be used to validate and correct noise level estimates obtained by other methods.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 5","pages":"1113–1123"},"PeriodicalIF":2.7,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147621416","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}

{"title":"Multi-Laboratory Assessment Reveals Variable Ion Species Profiles in Electrospray Ionization Mass Spectrometry.","authors":"Melanie T Odenkirk, Jacqueline M Chaparro, Nathan T Montgomery, Katrina L Leaptrot, Stacy D Sherrod, Jody C May, Henriëtte van Eekelen, Bert Schipper, Juliana Chaura, Gabriel Esteban Velez, Wimonphan Chathiran, Cole R Michel, Katrina A Doenges, Richard Reisdorph, Mari Maeda-Yamamoto, Luis Valdiviez, Uri Keshet, Jeremiah Wells, Scott Mackell, David Bell, Sebastian Tapia Leiva, Simon Partridge, Daniela Rago, Linda Ahonen, Yuki Ito, Margaret L Read, John C Evans, Macy J Gruszczynski, Leokadja Szalach, Stephen C Boyko, Steven Watkins, Rodrigo Ledesma Amaro, Oliver Fiehn, Nichole Reisdorph, Warangkana Srichamnong, Andres Jaramillo-Botero, Ric C H de Vos, Robert D Hall, John A McLean, Corey D Broeckling, Jessica E Prenni","doi":"10.1021/jasms.6c00011","DOIUrl":"https://doi.org/10.1021/jasms.6c00011","url":null,"abstract":"<p><p>Electrospray ionization (ESI) is a foundational technique in mass spectrometry (MS) widely applied to measure nonvolatile molecules in diverse chemical and biological samples. Yet variation in ESI-MS instrumentation, operating settings, and parameters such as solvent composition creates specific, local ionization environments that drive the formation of select ion species for individual analytes. As ESI continues to advance analytical discovery, understanding the extent to which variation in ion species formation impacts intra- and inter-experimental results is essential. Here, we assessed ion species formation by analyzing an internal retention time standard (IRTS) mixture across ten laboratories employing high-resolution ESI-MS instrumentation from four vendors (Agilent Technologies, ThermoFisher Scientific, Shimadzu Corporation, and Waters Corporation). Instrument vendors were considered not as a benchmark of performance, but as a practical framework to capture differences in source design, ion optics, and analyzer/detectors that are inherently coupled to commercial platforms. Despite the use of standardized extraction and chromatographic protocols, differences in instrument configuration, source conditions, and method execution resulted in variation in ion species formation across vendors, among laboratories using instruments from the same vendor, and even within individual laboratories. These findings demonstrate that, even with standardized methods, the collective influence of local ionization environments on ion species formation remains a critical obstacle for interpreting LC-MS small molecule data and improving reproducibility and comparability across studies.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147832067","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}

{"title":"Mass Spectrometry-Based Spatial Imaging of the Cochlea","authors":"Roberto A. Ribas,&nbsp;, ,&nbsp;Qun Tang,&nbsp;, ,&nbsp;Scarlett I. Caffee,&nbsp;, ,&nbsp;Cameron J. Shedlock,&nbsp;, ,&nbsp;Tara R. Hawkinson,&nbsp;, ,&nbsp;Abigail K. Dragich,&nbsp;, ,&nbsp;Borhane E. C. Ziani,&nbsp;, ,&nbsp;Franca Bucco Paolasso,&nbsp;, ,&nbsp;Alyson P. Black,&nbsp;, ,&nbsp;Xin Ma,&nbsp;, ,&nbsp;Harshitha C. Kota,&nbsp;, ,&nbsp;Li Chen,&nbsp;, ,&nbsp;Gregory I. Frolenkov,&nbsp;, ,&nbsp;Derek B. Allison,&nbsp;, ,&nbsp;Matthew S. Gentry,&nbsp;, ,&nbsp;Ramon C. Sun,&nbsp;, and ,&nbsp;Craig W. Vander Kooi*,&nbsp;","doi":"10.1021/jasms.5c00436","DOIUrl":"10.1021/jasms.5c00436","url":null,"abstract":"<p >Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry Imaging (MALDI-MSI) is transforming spatial molecular studies. However, applying MALDI-MSI to small, anatomically complex tissues remains challenging. One such structure is the cochlea, the auditory part of the inner ear that is critical for hearing. To address these challenges, we developed and implemented a streamlined workflow for sample preparation and processing to obtain MALDI-MSI data on mouse cochlea. Sample acquisition was optimized to minimize time and processing steps, allowing use of flash-frozen neonatal mouse heads. This workflow enabled high spatial resolution metabolomic and lipidomic imaging of the sagittally cryosectioned mouse cochlea using <i>N</i>-(1-naphthyl) ethylenediamine dihydrochloride (NEDC) matrix via sublimation. Optimized NEDC sublimation allowed high signal-to-noise, reduced delocalization, and salt tolerance, allowing acquisition of 5 μm-resolution imaging data on a MALDI-MSI instrument. Sublimation was found to be superior to spraying as a method for matrix application due to its higher signal-to-noise, particularly for lipids and fatty acids, and improved spatial resolution. Diverse metabolites and lipids were measured throughout the cochlear region, revealing distinct spatial distributions. Clustering identified reproducible physiological regions, including the otic capsule and spiral ducts. High spatial resolution imaging revealed distinct tissues, cell types, and molecular signatures within the cochlea. These findings establish the utility of high spatial resolution MALDI-MSI for auditory research, enabling molecular mapping of cochlear function and dysfunction.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 5","pages":"1187–1195"},"PeriodicalIF":2.7,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/jasms.5c00436","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147607764","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}

{"title":"Toward Molecular Forensics of Agrochemicals with Orbitrap IRMS: Isotopic Fingerprints of Imidacloprid Sources and Elucidating Hydrolysis","authors":"Felix Niemann,&nbsp;, ,&nbsp;Nils J. Kuhlbusch,&nbsp;, ,&nbsp;Annika Gruhlke,&nbsp;, ,&nbsp;Sarah P. Rockel,&nbsp;, ,&nbsp;Robert G. H. Marks,&nbsp;, ,&nbsp;Klaus Kerpen,&nbsp;, ,&nbsp;Milen Nachev,&nbsp;, ,&nbsp;Maik A. Jochmann*,&nbsp;, ,&nbsp;Andreas Hilkert,&nbsp;, and ,&nbsp;Torsten C. Schmidt,&nbsp;","doi":"10.1021/jasms.5c00444","DOIUrl":"10.1021/jasms.5c00444","url":null,"abstract":"<p >Imidacloprid (IMI) is a widespread neonicotinoid insecticide of environmental concern because of its ecotoxicity and persistence. Tracing its commercial sources and environmental transformation is difficult with concentration-based approaches. We explored electrospray ionization Orbitrap isotope ratio mass spectrometry ((ESI) Orbitrap MS-Based Isotope Ratio Analysis) for compound- and fragment-specific stable isotope analysis of IMI at natural abundance. This approach enables direct measurement of ¹³C, ¹⁵N, ³⁷Cl, and multiple substituted isotopologue ratios. Experimental parameters were optimized to control sources of bias in isotopologue ratios. A dual-inlet bracketing protocol enabled normalization and drift correction. IMI from seven different commercial sources could be distinguished by their isotopic fingerprints. We demonstrate that principal component analysis (PCA) can exploit the expanded set of isotopic variables. Two PCAs with distinct variable sets were performed: a fragment-only, nonoverlapping isotopologue subset for source material attribution, and a combined molecular-average and fragment-level subset to maximize manufacturer discrimination. Alkaline hydrolysis (pH ≈ 12, 30 °C) based on compound-average δ¹³C and δ¹⁵N values measured by (ESI) Orbitrap MS-Based Isotope Ratio Analysis revealed significant carbon isotope fractionation (ε_C = −4.3 ± 1.4 ‰) and a statistically negligible nitrogen fractionation (ε_N = 0.6 ± 1.6 ‰), consistent with initial OH^– attack at the nitroimine carbon as the primary pathway. (ESI) Orbitrap MS-Based Isotope Ratio Analysis can elucidate transformation mechanisms in analytically challenging polar analytes. The chemometric approach of using MS¹/MS² data can be transferred to other (agro-)chemicals either to enhance isotopic discrimination or to discover patterns.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 5","pages":"1196–1206"},"PeriodicalIF":2.7,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147637517","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}