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1

Neo, J., T. Lim, and Q. Lin. "Zebrafish Imaging: A MALDI MS Imaging Approach." Journal of Proteomics & Bioinformatics S2, no. 01 (July 2008): 204. http://dx.doi.org/10.4172/jpb.s1000150.

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2

Castellino, Stephen. "Visualizing drug disposition with MALDI imaging MS." Drug Metabolism and Pharmacokinetics 33, no. 1 (January 2018): S15. http://dx.doi.org/10.1016/j.dmpk.2017.11.074.

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3

Jackson, Shelley N., and Amina S. Woods. "Imaging of Noncovalent Complexes by MALDI-MS." Journal of The American Society for Mass Spectrometry 24, no. 12 (October 2, 2013): 1950–56. http://dx.doi.org/10.1007/s13361-013-0745-3.

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4

Israr, Muhammad Zubair, Dennis Bernieh, Andrea Salzano, Shabana Cassambai, Yoshiyuki Yazaki, and Toru Suzuki. "Matrix-assisted laser desorption ionisation (MALDI) mass spectrometry (MS): basics and clinical applications." Clinical Chemistry and Laboratory Medicine (CCLM) 58, no. 6 (June 25, 2020): 883–96. http://dx.doi.org/10.1515/cclm-2019-0868.

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AbstractBackgroundMatrix-assisted laser desorption ionisation (MALDI) mass spectrometry (MS) has been used for more than 30 years. Compared with other analytical techniques, it offers ease of use, high throughput, robustness, cost-effectiveness, rapid analysis and sensitivity. As advantages, current clinical techniques (e.g. immunoassays) are unable to directly measure the biomarker; rather, they measure secondary signals. MALDI-MS has been extensively researched for clinical applications, and it is set for a breakthrough as a routine tool for clinical diagnostics.ContentThis review reports on the principles of MALDI-MS and discusses current clinical applications and the future clinical prospects for MALDI-MS. Furthermore, the review assesses the limitations currently experienced in clinical assays, the advantages and the impact of MALDI-MS to transform clinical laboratories.SummaryMALDI-MS is widely used in clinical microbiology for the screening of microbial isolates; however, there is scope to apply MALDI-MS in the diagnosis, prognosis, therapeutic drug monitoring and biopsy imaging in many diseases.OutlookThere is considerable potential for MALDI-MS in clinic as a tool for screening, profiling and imaging because of its high sensitivity and specificity over alternative techniques.
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Ronci, Maurizio, Shiwani Sharma, Tim Chataway, Kathryn P. Burdon, Sarah Martin, Jamie E. Craig, and Nicolas H. Voelcker. "MALDI-MS-Imaging of Whole Human Lens Capsule." Journal of Proteome Research 10, no. 8 (August 5, 2011): 3522–29. http://dx.doi.org/10.1021/pr200148k.

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6

Kreye, F., G. Hamm, Y. Karrout, R. Legouffe, D. Bonnel, F. Siepmann, and J. Siepmann. "MALDI-TOF MS imaging of controlled release implants." Journal of Controlled Release 161, no. 1 (July 2012): 98–108. http://dx.doi.org/10.1016/j.jconrel.2012.04.017.

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7

Morisasa, Mizuki, Tomohiko Sato, Keisuke Kimura, Tsukasa Mori, and Naoko Goto-Inoue. "Application of Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry Imaging for Food Analysis." Foods 8, no. 12 (December 2, 2019): 633. http://dx.doi.org/10.3390/foods8120633.

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Food contains various compounds, and there are many methods available to analyze each of these components. However, the large amounts of low-molecular-weight metabolites in food, such as amino acids, organic acids, vitamins, lipids, and toxins, make it difficult to analyze the spatial distribution of these molecules. Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) imaging is a two-dimensional ionization technology that allows the detection of small metabolites in tissue sections without requiring purification, extraction, separation, or labeling. The application of MALDI-MS imaging in food analysis improves the visualization of these compounds to identify not only the nutritional content but also the geographical origin of the food. In this review, we provide an overview of some recent applications of MALDI-MS imaging, demonstrating the advantages and prospects of this technology compared to conventional approaches. Further development and enhancement of MALDI-MS imaging is expected to offer great benefits to consumers, researchers, and food producers with respect to breeding improvement, traceability, the development of value-added foods, and improved safety assessments.
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8

Ellis, S. R., J. Soltwisch, M. R. L. Paine, K. Dreisewerd, and R. M. A. Heeren. "Laser post-ionisation combined with a high resolving power orbitrap mass spectrometer for enhanced MALDI-MS imaging of lipids." Chemical Communications 53, no. 53 (2017): 7246–49. http://dx.doi.org/10.1039/c7cc02325a.

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Coupling laser post-ionisation with a high resolving power MALDI Orbitrap mass spectrometer has realised an up to ∼100-fold increase in the sensitivity and enhanced the chemical coverage for MALDI-MS imaging of lipids relative to conventional MALDI.
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9

Solon, Eric G., Alain Schweitzer, Markus Stoeckli, and Brendan Prideaux. "Autoradiography, MALDI-MS, and SIMS-MS Imaging in Pharmaceutical Discovery and Development." AAPS Journal 12, no. 1 (November 17, 2009): 11–26. http://dx.doi.org/10.1208/s12248-009-9158-4.

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10

Prentice, Boone M., Chad W. Chumbley, and Richard M. Caprioli. "High-speed MALDI MS/MS imaging mass spectrometry using continuous raster sampling." Journal of Mass Spectrometry 50, no. 4 (March 19, 2015): 703–10. http://dx.doi.org/10.1002/jms.3579.

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11

Prentice, Boone M., Chad W. Chumbley, and Richard M. Caprioli. "High-speed MALDI MS/MS imaging mass spectrometry using continuous raster sampling." Journal of Mass Spectrometry 51, no. 8 (July 20, 2016): 665. http://dx.doi.org/10.1002/jms.3798.

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12

Thomas, Aurélien, and Pierre Chaurand. "Advances in tissue section preparation for MALDI imaging MS." Bioanalysis 6, no. 7 (April 2014): 967–82. http://dx.doi.org/10.4155/bio.14.63.

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13

Aziz, Mina, Drew Sturtevant, Jordan Winston, Eva Collakova, John Jelesko, and Kent Chapman. "MALDI-MS Imaging of Urushiols in Poison Ivy Stem." Molecules 22, no. 5 (April 29, 2017): 711. http://dx.doi.org/10.3390/molecules22050711.

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14

Shariatgorji, Mohammadreza, Anna Nilsson, Elva Fridjonsdottir, Theodosia Vallianatou, Patrik Källback, Luay Katan, Jonas Sävmarker, et al. "Comprehensive mapping of neurotransmitter networks by MALDI–MS imaging." Nature Methods 16, no. 10 (September 23, 2019): 1021–28. http://dx.doi.org/10.1038/s41592-019-0551-3.

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15

Monroe, Eric B., Suresh P. Annangudi, Nathan G. Hatcher, Howard B. Gutstein, Stanislav S. Rubakhin, and Jonathan V. Sweedler. "SIMS and MALDI MS imaging of the spinal cord." PROTEOMICS 8, no. 18 (August 19, 2008): 3746–54. http://dx.doi.org/10.1002/pmic.200800127.

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16

Berry, Karin A. Zemski, Bilan Li, Susan D. Reynolds, Robert M. Barkley, Miguel A. Gijón, Joseph A. Hankin, Peter M. Henson, and Robert C. Murphy. "MALDI imaging MS of phospholipids in the mouse lung." Journal of Lipid Research 52, no. 8 (April 20, 2011): 1551–60. http://dx.doi.org/10.1194/jlr.m015750.

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17

de Almeida, Camila M., Fernanda E. Pinto, Nayara A. dos Santos, Lindamara M. de Souza, Bianca B. Merlo, Christopher J. Thompson, and Wanderson Romão. "Designer drugs analysis by LDI(+), MALDI(+) and MALDI(+) imaging coupled to FT-ICR MS." Microchemical Journal 149 (September 2019): 104002. http://dx.doi.org/10.1016/j.microc.2019.104002.

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18

Vidová, Veronika, Michael Volný, Karel Lemr, and Vladimír Havlíček. "Surface analysis by imaging mass spectrometry." Collection of Czechoslovak Chemical Communications 74, no. 7-8 (2009): 1101–16. http://dx.doi.org/10.1135/cccc2009028.

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A review of four MS-based techniques available for molecular surface imaging is presented. The main focus is on the commercially available mass spectrometry imaging techniques: secondary ion mass spectrometry (SIMS), matrix assisted laser desorption ionization mass spectrometry (MALDI-MS), desorption electrospray ionization mass spectrometry (DESI-MS) and laser ablation inductively-coupled plasma mass spectrometry (LA-ICP-MS). A short historical perspective is presented and traditional desorption ionization techniques are also briefly described. The four techniques are compared mainly with respect to their usage for imaging of biological surfaces. MALDI is evaluated as the most successful in life sciences and the only technique usable for imaging of large biopolymers. SIMS is less common but offers superior spatial lateral resolution and DESI is considered to be an emerging alternative approach in mass spectrometry imaging. LA-ICP ionization is unbeatable in terms of limits of detection but does not provide structural information. All techniques are considered extremely useful, representing a new wave of expansion of mass spectrometry into surface science and bioanalysis. A minireview with 121 references.
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19

Gustafsson, Johan O. R., James S. Eddes, Stephan Meding, Tomas Koudelka, Martin K. Oehler, Shaun R. McColl, and Peter Hoffmann. "Internal calibrants allow high accuracy peptide matching between MALDI imaging MS and LC-MS/MS." Journal of Proteomics 75, no. 16 (August 2012): 5093–105. http://dx.doi.org/10.1016/j.jprot.2012.04.054.

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20

Sui, Ping, Hiroyuki Watanabe, Konstantin Artemenko, Wei Sun, Georgy Bakalkin, Malin Andersson, and Jonas Bergquist. "Neuropeptide imaging in rat spinal cord with MALDI-TOF MS: Method development for the application in pain-related disease studies." European Journal of Mass Spectrometry 23, no. 3 (May 7, 2017): 105–15. http://dx.doi.org/10.1177/1469066717703272.

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Spinal cord as a connection between brain and peripheral nervous system is an essential material for studying neural transmission, especially in pain-related research. This study was the first to investigate pain-related neuropeptide distribution in rat spinal cord using a matrix-assisted laser desorption ionization-time of flight imaging mass spectrometry (MALDI TOF MS) approach. The imaging workflow was evaluated and showed that MALDI TOF MS provides efficient resolution and robustness for neuropeptide imaging in rat spinal cord tissue. The imaging result showed that in naive rat spinal cord the molecular distribution of haeme, phosphatidylcholine, substance P and thymosin beta 4 were well in line with histological features. Three groups of pain-related neuropeptides, which are cleaved from prodynorphin, proenkephalin and protachykinin-1 proteins were detected. All these neuropeptides were found predominantly localized in the dorsal spinal cord and each group had unique distribution pattern. This study set the stage for future MALDI TOF MS application to elucidate signalling mechanism of pain-related diseases in small animal models.
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21

Jiao, Jing, Aizhu Miao, Ying Zhang, Qi Fan, Yi Lu, and Haojie Lu. "Imaging phosphorylated peptide distribution in human lens by MALDI MS." Analyst 140, no. 12 (2015): 4284–90. http://dx.doi.org/10.1039/c5an00101c.

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22

Enomoto, Hirofumi. "Mass Spectrometry Imaging of Flavonols and Ellagic Acid Glycosides in Ripe Strawberry Fruit." Molecules 25, no. 20 (October 9, 2020): 4600. http://dx.doi.org/10.3390/molecules25204600.

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Flavonols and ellagic acid glycosides are major phenolic compounds in strawberry fruit. They have antioxidant activity, show protective functions against abiotic and biotic stress, and provide health benefits. However, their spatial distribution in ripe fruit has not been understood. Therefore, matrix-assisted laser desorption/ionization (MALDI)-mass spectrometry imaging (MSI) was performed to investigate their distribution in fruit tissues. Using strawberry extract, five flavonols, namely, three kaempferols and two quercetins, and two ellagic acid glycosides, were tentatively identified by MALDI-tandem MS. To investigate the tentatively identified compounds, MALDI-MSI and tandem MS imaging (MS/MSI) analyses were performed. Kaempferol and quercetin glycosides showed similar distribution patterns. They were mainly found in the epidermis, while ellagic acid glycosides were mainly found in the achene and in the bottom area of the receptacle. These results suggested that the difference in distribution pattern between flavonols and ellagic acid glycosides depends on the difference between their aglycones. Seemingly, flavonols play a role in protective functions in the epidermis, while ellagic acid glycosides play a role in the achene and in the bottom side of the receptacle, respectively. These results demonstrated that MALDI-MSI is useful for distribution analysis of flavonols and ellagic acid glycosides in strawberry fruit.
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23

Chaurand, P. "MALDI Imaging MS, the Nuts and Bolts of the Technology." Journal of Proteomics & Bioinformatics S2, no. 01 (July 2008): 126. http://dx.doi.org/10.4172/jpb.s1000100.

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24

Hart, Philippa J., Simona Francese, Emmanuelle Claude, M. Nicola Woodroofe, and Malcolm R. Clench. "MALDI-MS imaging of lipids in ex vivo human skin." Analytical and Bioanalytical Chemistry 401, no. 1 (May 22, 2011): 115–25. http://dx.doi.org/10.1007/s00216-011-5090-4.

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25

Wang, Tao, Zongwei Cai, Yanyan Chen, Wang Ka Lee, Chak-Shing Kwan, Min Li, Albert S. C. Chan, Zhi-Feng Chen, Allen Ka Loon Cheung, and Ken Cham-Fai Leung. "MALDI-MS Imaging Analysis of Noninflammatory Type III Rotaxane Dendrimers." Journal of the American Society for Mass Spectrometry 31, no. 12 (August 3, 2020): 2488–94. http://dx.doi.org/10.1021/jasms.0c00198.

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26

Trim, Paul J., and Marten F. Snel. "Small molecule MALDI MS imaging: Current technologies and future challenges." Methods 104 (July 2016): 127–41. http://dx.doi.org/10.1016/j.ymeth.2016.01.011.

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27

Goodwin, Richard J. A., Jessica C. Dungworth, Stuart R. Cobb, and Andrew R. Pitt. "Time-dependent evolution of tissue markers by MALDI-MS imaging." PROTEOMICS 8, no. 18 (August 19, 2008): 3801–8. http://dx.doi.org/10.1002/pmic.200800201.

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28

Sage, Linda. "Research Profile: Imaging fixed and embedded tissues with MALDI MS." Journal of Proteome Research 6, no. 4 (April 2007): 1240. http://dx.doi.org/10.1021/pr070736w.

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29

Pagni, Fabio, Vincenzo L'Imperio, Fulvio Magni, and Isabella Piga. "MALDI-MS Imaging Application in Thyroid FNA: Challenges and Perspectives." Journal of the American Society of Cytopathology 7, no. 5 (September 2018): S27. http://dx.doi.org/10.1016/j.jasc.2018.06.066.

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30

Bodzon-Kulakowska, Anna, Roberta Arena, Przemyslaw Mielczarek, Kinga Hartman, Paulina Kozoł, Ewa Gibuła-Tarlowska, Tomasz P. Wrobel, et al. "Mouse single oocyte imaging by MALDI-TOF MS for lipidomics." Cytotechnology 72, no. 3 (April 9, 2020): 455–68. http://dx.doi.org/10.1007/s10616-020-00393-9.

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31

Yagnik, Gargey, Ziying Liu, Kenneth J. Rothschild, and Mark J. Lim. "Highly Multiplexed Immunohistochemical MALDI-MS Imaging of Biomarkers in Tissues." Journal of the American Society for Mass Spectrometry 32, no. 4 (February 25, 2021): 977–88. http://dx.doi.org/10.1021/jasms.0c00473.

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32

Jones, E. Ellen, Wujuan Zhang, Xueheng Zhao, Cristine Quiason, Stephanie Dale, Sheerin Shahidi-Latham, Gregory A. Grabowski, Kenneth D. R. Setchell, Richard R. Drake, and Ying Sun. "Tissue Localization of Glycosphingolipid Accumulation in a Gaucher Disease Mouse Brain by LC-ESI-MS/MS and High-Resolution MALDI Imaging Mass Spectrometry." SLAS DISCOVERY: Advancing the Science of Drug Discovery 22, no. 10 (July 17, 2017): 1218–28. http://dx.doi.org/10.1177/2472555217719372.

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To better understand regional brain glycosphingolipid (GSL) accumulation in Gaucher disease (GD) and its relationship to neuropathology, a feasibility study using mass spectrometry and immunohistochemistry was conducted using brains derived from a GD mouse model (4L/PS/NA) homozygous for a mutant GCase (V394L [4L]) and expressing a prosaposin hypomorphic (PS-NA) transgene. Whole brains from GD and control animals were collected using one hemisphere for MALDI FTICR IMS analysis and the other for quantitation by LC-ESI-MS/MS. MALDI IMS detected several HexCers across the brains. Comparison with the brain hematoxylin and eosin (H&E) revealed differential signal distributions in the midbrain, brain stem, and CB of the GD brain versus the control. Quantitation of serial brain sections with LC-ESI-MS/MS supported the imaging results, finding the overall HexCer levels in the 4L/PS-NA brains to be four times higher than the control. LC-ESI-MS/MS also confirmed that the elevated hexosyl isomers were glucosylceramides rather than galactosylceramides. MALDI imaging also detected differential analyte distributions of lactosylceramide species and gangliosides in the 4L/PS-NA brain, which was validated by LC-ESI-MS/MS. Immunohistochemistry revealed regional inflammation, altered autophagy, and defective protein degradation correlating with regions of GSL accumulation, suggesting that specific GSLs may have distinct neuropathological effects.
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33

Müller, Max A., Dhaka R. Bhandari, and Bernhard Spengler. "Matrix-Free High-Resolution Atmospheric-Pressure SALDI Mass Spectrometry Imaging of Biological Samples Using Nanostructured DIUTHAME Membranes." Metabolites 11, no. 9 (September 15, 2021): 624. http://dx.doi.org/10.3390/metabo11090624.

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Applications of mass spectrometry imaging (MSI), especially matrix-assisted laser desorption/ionization (MALDI) in the life sciences are becoming increasingly focused on single cell analysis. With the latest instrumental developments, pixel sizes in the micrometer range can be obtained, leading to challenges in matrix application, where imperfections or inhomogeneities in the matrix layer can lead to misinterpretation of MS images. Thereby, the application of premanufactured, homogeneous ionization-assisting devices is a promising approach. Tissue sections were investigated using a matrix-free imaging technique (Desorption Ionization Using Through-Hole Alumina Membrane, DIUTHAME) based on premanufactured nanostructured membranes to be deposited on top of a tissue section, in comparison to the spray-coating of an organic matrix in a MALDI MSI approach. Atmospheric pressure MALDI MSI ion sources were coupled to orbital trapping mass spectrometers. MS signals obtained by the different ionization techniques were annotated using accurate-mass-based database research. Compared to MALDI MSI, DIUTHAME MS images captivated with higher signal homogeneities, higher contrast and reduced background signals, while signal intensities were reduced by about one order of magnitude, independent of analyte class. DIUTHAME membranes, being applicable only on tissue sections thicker than 50 µm, were successfully used for mammal, insect and plant tissue with a high lateral resolution down to 5 µm.
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34

Solon, Eric G., Alain Schweitzer, Markus Stoeckli, and Brendan Prideaux. "Erratum to: Autoradiography, MALDI-MS, and SIMS-MS Imaging in Pharmaceutical Discovery and Development." AAPS Journal 12, no. 1 (December 18, 2009): 107. http://dx.doi.org/10.1208/s12248-009-9167-3.

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35

Svirkova, Anastasiya, Anna Turyanskaya, Lukas Perneczky, Christina Streli, and Martina Marchetti-Deschmann. "Multimodal imaging of undecalcified tissue sections by MALDI MS and μXRF." Analyst 143, no. 11 (2018): 2587–95. http://dx.doi.org/10.1039/c8an00313k.

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dos Santos, Nayara A., Lindamara M. de Souza, Fernanda E. Pinto, Clebson de J. Macrino, Camila M. de Almeida, Bianca B. Merlo, Paulo R. Filgueiras, Rafael S. Ortiz, Ronaldo Mohana-Borges, and Wanderson Romão. "LDI and MALDI-FT-ICR imaging MS in Cannabis leaves: optimization and study of spatial distribution of cannabinoids." Analytical Methods 11, no. 13 (2019): 1757–64. http://dx.doi.org/10.1039/c9ay00226j.

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37

Bradshaw, R., N. Denison, and S. Francese. "Implementation of MALDI MS profiling and imaging methods for the analysis of real crime scene fingermarks." Analyst 142, no. 9 (2017): 1581–90. http://dx.doi.org/10.1039/c7an00218a.

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38

Taira, Shu, Ryuzo Ikeda, Naohiko Yokota, Issey Osaka, Manabu Sakamoto, Mitsuro Kato, and Yuko Sahashi. "Mass Spectrometric Imaging of Ginsenosides Localization in Panax ginseng Root." American Journal of Chinese Medicine 38, no. 03 (January 2010): 485–93. http://dx.doi.org/10.1142/s0192415x10008007.

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We performed mass spectrometric imaging (MSI) to localize ginsenosides ( Rb 1, Rb 2 or Rc , and Rf ) in cross-sections of the Panax ginseng root at a resolution of 100 μm using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). Tandem mass spectrometry (MS/MS) of alkali metal-adducted ginsenoside ions revealed structural information of the corresponding saccharides and aglycone. MALDI-MSI confirmed that ginsenosides were located more in the cortex and the periderm than that in the medulla of a lateral root. In addition, it revealed that localization of ginsenosides in a root tip (diameter, 2.7 mm) is higher than that in the center of the root (diameter, 7.3 mm). A quantitative difference was detected between localizations of protopanaxadiol-type ginsenoside ( Rb 1, Rb 2, or Rc ) and protopanaxatriol-type ginsenoside ( Rf ) in the root. This imaging approach is a promising technique for rapid evaluation and identification of medicinal saponins in plant tissues.
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Quanico, J., J. Franck, J. P. Gimeno, R. Sabbagh, M. Salzet, R. Day, and I. Fournier. "Parafilm-assisted microdissection: a sampling method for mass spectrometry-based identification of differentially expressed prostate cancer protein biomarkers." Chemical Communications 51, no. 22 (2015): 4564–67. http://dx.doi.org/10.1039/c4cc08331h.

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40

Jaegger, C. F., F. Negrão, D. M. Assis, K. R. A. Belaz, C. F. F. Angolini, A. M. A. P. Fernandes, V. G. Santos, et al. "MALDI MS imaging investigation of the host response to visceral leishmaniasis." Molecular BioSystems 13, no. 10 (2017): 1946–53. http://dx.doi.org/10.1039/c7mb00306d.

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41

Lay, Jackson O., Jennifer Gidden, Rohana Liyanage, Beth Emerson, and Bill Durham. "Rapid characterization of lipids by MALDI MS. Part 2: Artifacts, ion suppression, and TLC MALDI imaging." Lipid Technology 24, no. 2 (February 2012): 36–40. http://dx.doi.org/10.1002/lite.201200174.

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42

Robinson, Eve, Paul Giffen, Dave Hassall, Doug Ball, Heather Reid, Diane Coe, Simon Teague, et al. "Multimodal imaging of drug and excipients in rat lungs following an inhaled administration of controlled-release drug laden PLGA microparticles." Analyst 146, no. 10 (2021): 3378–90. http://dx.doi.org/10.1039/d0an02333g.

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The use of multimodal imaging techniques, in particular MALDI MS Imaging, TOF-SIMS and histopathology, to spatially map the distribution of drug and excipients (microparticles) in rat lung sections following inhaled administration is demonstrated.
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43

Patel, Ekta, Laura M. Cole, Robert Bradshaw, Afnan Batubara, Christopher A. Mitchell, Simona Francese, and Malcolm R. Clench. "MALDI-MS imaging for the study of tissue pharmacodynamics and toxicodynamics." Bioanalysis 7, no. 1 (January 2015): 91–101. http://dx.doi.org/10.4155/bio.14.280.

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44

Fournier, Isabelle, Maxence Wisztorski, and Michel Salzet. "Tissue imaging using MALDI-MS: a new frontier of histopathology proteomics." Expert Review of Proteomics 5, no. 3 (June 2008): 413–24. http://dx.doi.org/10.1586/14789450.5.3.413.

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45

Boskamp, Marcel S., and Jens Soltwisch. "Charge Distribution between Different Classes of Glycerophospolipids in MALDI-MS Imaging." Analytical Chemistry 92, no. 7 (March 8, 2020): 5222–30. http://dx.doi.org/10.1021/acs.analchem.9b05761.

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46

Kopp, C., M. Wisztorski, J. Revel, M. Mehiri, V. Dani, L. Capron, D. Carette, et al. "MALDI-MS and NanoSIMS imaging techniques to study cnidarian–dinoflagellate symbioses." Zoology 118, no. 2 (April 2015): 125–31. http://dx.doi.org/10.1016/j.zool.2014.06.006.

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47

Turker, Sarah D., Warwick B. Dunn, and John Wilkie. "MALDI-MS of drugs: Profiling, imaging, and steps towards quantitative analysis." Applied Spectroscopy Reviews 52, no. 1 (July 5, 2016): 73–99. http://dx.doi.org/10.1080/05704928.2016.1207659.

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48

Ruh, Hermelindis, Theresia Salonikios, Jens Fuchser, Matthias Schwartz, Carsten Sticht, Christina Hochheim, Bernhard Wirnitzer, Norbert Gretz, and Carsten Hopf. "MALDI imaging MS reveals candidate lipid markers of polycystic kidney disease." Journal of Lipid Research 54, no. 10 (July 12, 2013): 2785–94. http://dx.doi.org/10.1194/jlr.m040014.

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49

Bradshaw, R., G. Wilson, N. Denison, and S. Francese. "Application of MALDI MS imaging after sequential processing of latent fingermarks." Forensic Science International 319 (February 2021): 110643. http://dx.doi.org/10.1016/j.forsciint.2020.110643.

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50

Bednařík, Antonín, Markéta Machálková, Eugene Moskovets, Kateřina Coufalíková, Pavel Krásenský, Pavel Houška, Jiří Kroupa, Jarmila Navrátilová, Jan Šmarda, and Jan Preisler. "MALDI MS Imaging at Acquisition Rates Exceeding 100 Pixels per Second." Journal of The American Society for Mass Spectrometry 30, no. 2 (November 19, 2018): 289–98. http://dx.doi.org/10.1007/s13361-018-2078-8.

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