Relevant bibliographies by topics / Ion mobility mass spectrometry imaging

Academic literature on the topic 'Ion mobility mass spectrometry imaging'

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Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Ion mobility mass spectrometry imaging"

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Mesa Sanchez, Daniela, Steve Creger, Veerupaksh Singla, Ruwan T. Kurulugama, John Fjeldsted, and Julia Laskin. "Ion Mobility-Mass Spectrometry Imaging Workflow." Journal of the American Society for Mass Spectrometry 31, no. 12 (August 4, 2020): 2437–42. http://dx.doi.org/10.1021/jasms.0c00142.

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Jackson, Shelley N., Damon Barbacci, Thomas Egan, Ernest K. Lewis, J. Albert Schultz, and Amina S. Woods. "MALDI-ion mobility mass spectrometry of lipids in negative ion mode." Anal. Methods 6, no. 14 (2014): 5001–7. http://dx.doi.org/10.1039/c4ay00320a.

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McLean, John A., Whitney B. Ridenour, and Richard M. Caprioli. "Profiling and imaging of tissues by imaging ion mobility-mass spectrometry." Journal of Mass Spectrometry 42, no. 8 (2007): 1099–105. http://dx.doi.org/10.1002/jms.1254.

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Guillén-Alonso, Héctor, Ignacio Rosas-Román, and Robert Winkler. "The emerging role of 3D-printing in ion mobility spectrometry and mass spectrometry." Analytical Methods 13, no. 7 (2021): 852–61. http://dx.doi.org/10.1039/d0ay02290j.

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3D-printing enables the rapid prototyping of ion mobility (IMS) and mass spectrometry (MS) gadgets. The RepRap components are suitable for building cost-efficient robots and MS imaging systems. In this review, we present current trends.
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Bowman, Andrew P., James Sawicki, Nari N. Talaty, Wayne R. Buck, Junhai Yang, and David S. Wagner. "Evaluation of Quantitative Platforms for Single Target Mass Spectrometry Imaging." Pharmaceuticals 15, no. 10 (September 23, 2022): 1180. http://dx.doi.org/10.3390/ph15101180.

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(1) Imaging of pharmaceutical compounds in tissue is an increasingly important subsection of Mass Spectrometry Imaging (MSI). Identifying proper target engagement requires MS platforms with high sensitivity and spatial resolution. Three prominent categories of drugs are small molecule drugs, antibody-drug conjugate payloads, and protein degraders. (2) We tested six common MSI platforms for their limit of detection (LoD) on a representative compound for each category: a Matrix-Assisted Laser Desorption/Ionization (MALDI) Fourier Transform Ion Cyclotron, a MALDI-2 Time-of-Flight (ToF), a MALDI-2 Trapped Ion Mobility Spectrometry ToF, a Desorption Electrospray Ionization Orbitrap, and 2 Atmospheric Pressure-MALDI Triple Quadrupoles. Samples were homogenized tissue mimetic models of rat liver spiked with known concentrations of analytes. (3) We found that the AP-MALDI-QQQ platform outperformed all 4 competing platforms by a minimum of 2- to 52-fold increase in LoD for representative compounds from each category of pharmaceutical. (4) AP-MALDI-QQQ platforms are effective, cost-efficient mass spectrometers for the identification of targeted analytes of interest.
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Sans, Marta, Clara L. Feider, and Livia S. Eberlin. "Advances in mass spectrometry imaging coupled to ion mobility spectrometry for enhanced imaging of biological tissues." Current Opinion in Chemical Biology 42 (February 2018): 138–46. http://dx.doi.org/10.1016/j.cbpa.2017.12.005.

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Chouinard, Christopher D., Michael S. Wei, Christopher R. Beekman, Robin H. J. Kemperman, and Richard A. Yost. "Ion Mobility in Clinical Analysis: Current Progress and Future Perspectives." Clinical Chemistry 62, no. 1 (January 1, 2016): 124–33. http://dx.doi.org/10.1373/clinchem.2015.238840.

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Abstract BACKGROUND Ion mobility spectrometry (IMS) is a rapid separation tool that can be coupled with several sampling/ionization methods, other separation techniques (e.g., chromatography), and various detectors (e.g., mass spectrometry). This technique has become increasingly used in the last 2 decades for applications ranging from illicit drug and chemical warfare agent detection to structural characterization of biological macromolecules such as proteins. Because of its rapid speed of analysis, IMS has recently been investigated for its potential use in clinical laboratories. CONTENT This review article first provides a brief introduction to ion mobility operating principles and instrumentation. Several current applications will then be detailed, including investigation of rapid ambient sampling from exhaled breath and other volatile compounds and mass spectrometric imaging for localization of target compounds. Additionally, current ion mobility research in relevant fields (i.e., metabolomics) will be discussed as it pertains to potential future application in clinical settings. SUMMARY This review article provides the authors' perspective on the future of ion mobility implementation in the clinical setting, with a focus on ambient sampling methods that allow IMS to be used as a “bedside” standalone technique for rapid disease screening and methods for improving the analysis of complex biological samples such as blood plasma and urine.
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Stauber, Jonathan, Luke MacAleese, Julien Franck, Emmanuelle Claude, Marten Snel, Basak Kükrer Kaletas, Ingrid M. V. D. Wiel, Maxence Wisztorski, Isabelle Fournier, and Ron M. A. Heeren. "On-tissue protein identification and imaging by MALDI-Ion mobility mass spectrometry." Journal of the American Society for Mass Spectrometry 21, no. 3 (March 2010): 338–47. http://dx.doi.org/10.1016/j.jasms.2009.09.016.

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Fu, Tingting, Janina Oetjen, Manuel Chapelle, Alexandre Verdu, Matthias Szesny, Arnaud Chaumot, Davide Degli-Esposti, et al. "In situ isobaric lipid mapping by MALDI-ion mobility separation-mass spectrometry imaging." Journal of Mass Spectrometry 55, no. 9 (June 21, 2020): e4531. http://dx.doi.org/10.1002/jms.4531.

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Neumann, Elizabeth K., Lukasz G. Migas, Jamie L. Allen, Richard M. Caprioli, Raf Van de Plas, and Jeffrey M. Spraggins. "Spatial Metabolomics of the Human Kidney using MALDI Trapped Ion Mobility Imaging Mass Spectrometry." Analytical Chemistry 92, no. 19 (July 15, 2020): 13084–91. http://dx.doi.org/10.1021/acs.analchem.0c02051.

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Dissertations / Theses on the topic "Ion mobility mass spectrometry imaging"

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Walton, Barbara Lynn. "A Study of Silver: an Alternative Maldi Matrix for Low Weight Compounds and Mass Spectrometry Imaging." Thesis, University of North Texas, 2014. https://digital.library.unt.edu/ark:/67531/metadc499981/.

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Soft-landing ion mobility has applicability in a variety of areas. The ability to produce material and collect a sufficient amount for further analysis and applications is the key goal of this technique. Soft-landing ion mobility has provided a way to deposit material in a controllable fashion, and can be tailored to specific applications. Changing the conditions at which soft-landing ion mobility occurs effects the characteristics of the resulting particles (size, distribution/coverage on the surface). Longer deposition times generated more material on the surface; however, higher pressures increased material loss due to diffusion. Larger particles were landed when using higher pressures, and increased laser energy at ablation. The utilization of this technique for the deposition of silver clusters has provided a solvent free matrix application technique for MALDI-MS. The low kinetic energy of incident ions along with the solvent free nature of soft-landing ion mobility lead to a technique capable of imaging sensitive samples and low mass analysis. The lack of significant interference as seen by traditional organic matrices is avoided with the use of metallic particles, providing a major enhancement in the ability to analyze low mass compounds by MALDI.
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Endres, Kevin J. "Mass Spectrometry Methods For Macromolecules: Polymer Architectures, Cross-Linking, and Surface Imaging." University of Akron / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=akron1553096604194835.

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Yuen, Wei Hao. "Ion imaging mass spectrometry." Thesis, University of Oxford, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.564395.

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This work investigates the applicability of fast detectors to the technique of microscope-mode imaging mass spectrometry. By ionising analyte from a large area of the sample, and projecting the desorbed ions by the use of ion optics through a time-of-flight mass spectrometer onto a two- dimensional detector, time- (and hence mass-) dependent distributions of ions may be imaged. To date, this method of imaging mass spectrometry has been limited by the ability to image only one mass window of interest per experimental cycle, limiting throughput and processing speed. Thus, the alternative microprobe-mode imaging mass spectrometry is currently the dominant method of analysis, with its superior mass resolution. The application of fast detectors to microscope-mode imaging lifts the restriction of the detection of a single mass window per experimental cycle, potentially decreasing acquisition time by a factor of the number of mass peaks of interest. Additional advantages include the reduction of sample damage by laser ablation, and the potential identification of coincident eo-fragments of different masses originating from the same parent molecule. Theoretical calculations and simulations have been performed confirming the suitability of conventional time-of-flight velocity-mapped ion imaging apparatus for imaging mass spectrometry. Only small modifications to the repeller plate and laser beam path, together with the adjustment of the accelerating potential field, were required to convert the apparatus to a wide (7 mm diameter) field-of-view ion microscope. Factors affecting the mass and spatial resolution were investigated with these theoretical calculations, with theoretical calculations predicting a spatial resolution of about 26μm and m/m of 93. Typical experimental data collected from velocity-mapped ion imaging experiments were collected, and characterised in order to provide specifications for a novel time-stamping detector, the Pixel Imaging Mass Spectrometry detector. From these data, the suitability of thresholding and centroiding on the new detector was determined. Initial experiments using desorptionjionisation on silicon and conventional charge-coupled device cameras confirmed the correct spatial-mapping of the apparatus. Matrix-assisted laser desorptionjionisation techniques (MALDI) were used in experiments to determine the spatial and mass resolutions attainable with the apparatus. Experimental spatial resolutions of 14.4 μm and m/m of 60 were found. The better experimental spatial resolution indicates a higher di- rectionality of initial velocities from MALDI desorption than used in the theoretical predictions, while the poorer mass resolution could be attributed to limitations imposed by the use of the phosphor screen. Proof-of-concept experiments using fast-framing cameras and the new time-stamping detectors confirmed the feasibility of multiple mass acquisition in time-of-flight microscope mode ion imaging. Mass-dependent distributions were acquired of different pigment distributions in each experimental cycle. Finally, spatial-mapped images of coronal mouse brain sections were acquired using both conventional and fast detectors. The apparatus was demonstrated to provide accurate spatial distributions with a wide field-of-view, and multiple mass distributions were acquired with each experimental cycle using the new time-stamping detector.
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Berezovskaya, Yana. "Investigation of protein-ion interactions by mass spectrometry and ion mobility mass spectrometry." Thesis, University of Edinburgh, 2012. http://hdl.handle.net/1842/7747.

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Protein‐ion interactions play an important role in biological systems. A considerable number of elements (estimated 25 – 30) are essential in higher life forms such as animals and humans, where they are integral part of enzymes involved in plethora of cellular processes. It is difficult to overestimate the importance of thorough understanding of how protein‐ion interplay affects living cell in order to be able to address therapeutic challenges facing humanity. Presented to the reader’s attention is a gas‐phase biophysical analysis of peptides’ and proteins’ interactions with biologically relevant ions (Zn2+ and I–). This investigation provides an insight into conformational changes of peptides and proteins triggered by ions. Mass spectrometry and ion mobility mass spectrometry are used in this work to probe peptide and protein affinities for a range of ions, along with conformational changes that take place as a result of binding. Observation of peptide and protein behaviour in the gas phase can inform the investigator about their behaviour in solution prior to ionisation and transfer from the former into the latter phase. Wherever relevant, the gas‐phase studies are complemented by molecular dynamics simulations and the results are compared to solution phase findings (spectroscopy). Two case studies of protein‐ion interactions are presented in this thesis. Firstly, sequence‐to‐structure relationships in proteins are considered via protein design approach using two synthetic peptide‐based systems. The first system is a synthetic consensus zinc finger sequence (vCP1) that is responsive to zinc: it adopts a zinc finger fold in the presence of Zn2+ by coordinating the metal ion by two cysteines and two histidines. This peptide has been selected as a reference for the zinc‐bound state and a simple model to refine the characterisation method in preparation for analysis of a more sophisticated second system – dual conformational switch. This second system (ZiCop) is designed to adopt either of the two conformations in response to a stimulus: zinc finger or coiled coil. The reversible switch between the two conformational states is controlled by the binding of zinc ion to the peptide. Interactions of both peptide systems with a number of other divalent metal cations (Co2+, Ca2+ and Cu2+) are considered also, and the differences in binding and switching behaviour are discussed. Secondly, protein‐salt interactions are investigated using three proteins (lysozyme, cytochrome c and BPTI) using variable temperature ion mobility mass spectrometry. Ion mobility measurements were carried out on these proteins with helium as the buffer gas at three different drift cell temperatures – ‘ambient’ (300 K), ‘cold’ (260 K) and ‘hot’ (360 K), and their conformational preferences in response to HI binding and temperature are discussed.
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Woods, Lucy Ann. "Characterising amyloid assembly using ion mobility spectrometry-mass spectrometry." Thesis, University of Leeds, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.590277.

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From small molecules to macromolecules, mass spectrometry has evolved significantly over the past decade, progressing from a tool to identify chemical elements to a powerful technique able to elucidate structural information for large protein complexes. With the interfacing of ion mobility spectrometry to mass spectrometry (IMS-MS), mass spectrometric analyses now occupy an extra dimension, providing unrivalled separation and structural characterisation of lowly-populated species in heterogeneous mixtures. One biological system that has benefitted enormously from such advances is the study of in vitro amyloid formation. The ability of amyloidogenic proteins to assemble into insoluble fibrils is associated with over twenty-five different disease states. Beta-2 microglobulin (β2m) is one such protein able to assemble into amyloid fibrils in vitro, although assembly can only be initiated upon destabilisation of the native structure. Identifying which states initiate fibril formation is challenging. as few techniques are able to separate and characterise such transient species. In addition, recent research has identified a number of small molecule inhibitors of fibrillation and understanding their mechanism of action is a topic of current interest. Here, the power of IMS-MS has been harnessed to achieve the separation and characterisation of monomeric and oligomeric precursors of amyloid fibril formation of the protein β2m. Analysis of oligomeric species populated during fibril formation, in addition to the effects of small molecule inhibitors on oligomer population, has led to the identification of oligomeric species on-pathway to fibril formation. Further investigation into fibrils of different morphologies has also been conducted using IMS and limited proteolysis, Differences in oligomeric populations have been revealed, together with differences in fibril structure. Each of these results highlights how MS can be used to give insights into the mechanism of amyloid formation and highlight the potentials of this approach for screening for potential inhibitors of any assembly reaction.
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Zhou, Li. "Enhanced Electrospray Ionization for Mass Spectrometry and Ion Mobility Spectrometry." Diss., CLICK HERE for online access, 2006. http://contentdm.lib.byu.edu/ETD/image/etd1384.pdf.

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Ding, Luyi. "Studies of electrospray/ion mobility spectrometry/time-of-flight mass spectrometry." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0015/NQ48344.pdf.

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Chawner, Ross. "Combined tandem mass spectrometry and ion mobility spectrometry in proteome analyses." Thesis, University of Manchester, 2013. https://www.research.manchester.ac.uk/portal/en/theses/combined-tandem-mass-spectrometry-and-ion-mobility-spectrometry-in-proteome-analyses(3ba76f18-4703-4f6e-a97f-ee2b1dfb1deb).html.

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Proteomic studies aim to identify, quantify and characterise the full complement of proteins in a cell or organism under a defined set of conditions, and are important to our understanding of cellular mechanisms. However, such studies represent a major analytical challenge. A typical proteome analysis involves enzyme-mediated digestion of complex protein mixtures to yield an even more complex mixture of peptides. Combined reverse-phase liquid chromatography and tandem mass spectrometry is then traditionally utilised to ascertain sequence information from the characteristic peptide sequences. Analytical data derived for the peptides are employed as search terms in database searching of protein sequences derived from gene sequences. The extreme complexity of the peptide mixtures analysed means that additional novel approaches are required to fully interrogate the vast number of tandem mass spectra generated, assigning peptide identity and thereby helping to address demanding biological questions. The research reported here aims to further our understanding of both gas phase peptide/peptide fragment ion structure and peptide fragmentation behaviour using a combination of tandem mass spectrometry and ion mobility measurement.To facilitate the determination of peptide ion collision cross section, a novel standard, QCAL-IM, produced using the QconCAT strategy, has been developed to enable calibration of drift time in Travelling Wave Ion Mobility instruments. The standard facilitates empirical determination of the rotationally averaged collision cross section of any peptide/peptide fragment ion that lies within the calibration range encompassed. QCAL-IM was subsequently utilised to determine the collision cross section of a range of peptide ions produced by Lys-C and Lys-N proteolysis of ‘standard’ proteins. Data produced allowed the effect upon gas phase ion conformation through changing the location of the basic residue lysine within a peptide sequence to be assessed.The fragmentation behaviour of peptide ions produced by a variety of digestion regimes during both collision-induced dissociation (CID) and electron transfer dissociation (ETD) has also been extensively studied. The proteases trypsin and Lys-C are those typically utilised during proteomic studies and peptides produced by each have either the basic residues arginine or lysine at their carboxy-terminus. Secondary enzymatic treatment with the exoprotease carboxypeptidase B cleaves these basic residues from the C-terminus. Tandem mass spectrometric analysis of both tryptic/Lys-C peptides and their CBPB truncated analogue highlights that the dominant fragment ion series observed during both CID and ETD is determined, at least in part, by the location of such basic residues.Finally, studies were undertaken to investigate the factors which may promote/inhibit scrambling of peptide fragment ion sequence, which has recently been shown to take place during CID. The effect of modifying the gas phase basicity of the N-terminal amino acid residue is studied through a combination of derivatisation and synthesis of alternative peptide sequences. Increasing the gas phase basicity is shown to inhibit the observed sequence scrambling while promoting concomitant rearrangement/retention of a carboxyl oxygen at the C-terminus to give enhanced formation of bn+H2O product ion species.
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Koeniger, Stormy Lee Ann. "Multidimensional ion mobility spectrometry coupled to time-of-flight mass spectrometry." [Bloomington, Ind.] : Indiana University, 2006. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3230539.

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Thesis (Ph. D.)--Indiana University, Dept. of Chemistry, 2006.
Title from PDF t.p. (viewed Nov. 5, 2008). Source: Dissertation Abstracts International, Volume: 67-08, Section: B, page: 4395. Adviser: David E. Clemmer.
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Shliaha, Pavel Vyacheslavovich. "Investigation of protein abundance and localization by mass spectrometry and ion-mobility spectrometry-mass spectrometry methods." Thesis, University of Cambridge, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708661.

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Books on the topic "Ion mobility mass spectrometry imaging"

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Ashcroft, Alison E., and Frank Sobott, eds. Ion Mobility-Mass Spectrometry. Cambridge: Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886.

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Paglia, Giuseppe, and Giuseppe Astarita, eds. Ion Mobility-Mass Spectrometry. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0030-6.

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Cross, John H. Third International Workshop on Ion Mobility Spectrometry: Proceedings of an International Speciality Conference co-sponsored by Lyndon B. Johnson Space Center and KRUG Life Sciences, and held at Galveston, Texas, October 16-19, 1994. Edited by Lyndon B. Johnson Space Center and International Workshop on Ion Mobility Spectrometry (3rd : 1994 : Galveston, Texas). Houston, Texas: Lyndon B. Johnson Space Center, 1995.

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Wilkins, Charles L., and Sarah Trimpin. Ion Mobility Spectrometry - Mass Spectrometry. Taylor & Francis Group, 2010.

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Ion Mobility Spectrometry Mass Spectrometry Theory And Applications. CRC Press, 2010.

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Wilkins, Charles L., and Sarah Trimpin. Ion Mobility Spectrometry - Mass Spectrometry: Theory and Applications. Taylor & Francis Group, 2010.

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Ion Mobility Spectrometry - Mass Spectrometry: Theory and Applications. Taylor & Francis Group, 2017.

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Wilkins, Charles L., and Sarah Trimpin. Ion Mobility Spectrometry - Mass Spectrometry: Theory and Applications. Taylor & Francis Group, 2010.

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Ashcroft, Alison E., and Frank Sobott. Ion Mobility-Mass Spectrometry: Fundamentals and Applications. Royal Society of Chemistry, The, 2021.

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Ion Mobility-Mass Spectrometry: Methods and Protocols. Springer, 2020.

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Book chapters on the topic "Ion mobility mass spectrometry imaging"

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Oshikata, Motoji, Yuki Sugiura, Naohiko Yokota, and Mitsutoshi Setou. "MALDI Imaging with Ion-Mobility MS: Waters Corporation." In Imaging Mass Spectrometry, 221–31. Tokyo: Springer Japan, 2010. http://dx.doi.org/10.1007/978-4-431-09425-8_17.

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Hale, Oliver J., Eva Illes-Toth, Emma K. Sisley, and Helen J. Cooper. "CHAPTER 11. Ion Mobility Spectrometry in Mass Spectrometry Imaging." In Ion Mobility-Mass Spectrometry, 272–306. Cambridge: Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00272.

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McLean, John A., Larissa S. Fenn, and Jeffrey R. Enders. "Structurally Selective Imaging Mass Spectrometry by Imaging Ion Mobility-Mass Spectrometry." In Methods in Molecular Biology, 363–83. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-746-4_21.

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Lietz, Christopher B., Alicia L. Richards, Darrell D. Marshall, Yue Ren, and Sarah Trimpin. "Matrix-Assisted Inlet Ionization and Solvent-Free Gas-Phase Separation Using Ion Mobility Spectrometry for Imaging and Electron Transfer Dissociation Mass Spectrometry of Polymers." In Mass Spectrometry in Polymer Chemistry, 85–118. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2012. http://dx.doi.org/10.1002/9783527641826.ch4.

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Woods, Amina S., and Shelley N. Jackson. "The Application and Potential of Ion Mobility Mass Spectrometry in Imaging MS with a Focus on Lipids." In Methods in Molecular Biology, 99–111. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-746-4_5.

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McLean, John A., J. Albert Schultz, and Amina S. Woods. "Ion Mobility-Mass Spectrometry." In Electrospray and MALDI Mass Spectrometry, 411–39. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2012. http://dx.doi.org/10.1002/9780470588901.ch12.

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Sugai, Toshiki. "Ion Mobility Spectrometry with Mass Spectrometry." In Fundamentals of Mass Spectrometry, 89–107. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-7233-9_6.

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Stroganova, Iuliia, and Anouk M. Rijs. "CHAPTER 9. Ion Spectroscopy Coupled to Ion Mobility–Mass Spectrometry." In Ion Mobility-Mass Spectrometry, 206–42. Cambridge: Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00206.

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Deslignière, E., O. Hernandez-Alba, and S. Cianférani. "CHAPTER 16. Advanced IM-MS-based Approaches for Protein Analysis: Collision-induced Unfolding (CIU) and Hyphenation of Liquid Chromatography to IM-MS." In Ion Mobility-Mass Spectrometry, 436–60. Cambridge: Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00436.

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Richardson, K., and K. Giles. "CHAPTER 4. Travelling Wave Ion Mobility Separation: Basics and Calibration." In Ion Mobility-Mass Spectrometry, 83–104. Cambridge: Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00083.

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Conference papers on the topic "Ion mobility mass spectrometry imaging"

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El-Shafie, Mahmoud Y., Sally Bebawi, Hussein H. Zomor, and Frank Gunzer. "Improvement of the ion transfer efficiency in ion mobility spectrometry-mass spectrometry." In 2016 IEEE Workshop on Environmental, Energy, and Structural Monitoring Systems (EESMS). IEEE, 2016. http://dx.doi.org/10.1109/eesms.2016.7504828.

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Ekeowa, Ugo I., Joanna Freeke, and David Lomas. "The Characterisation Of Alpha1-antitrypsin Polymerisation By Ion Mobility – Mass Spectrometry." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4985.

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Laudien, Robert, Rainer Schultze, and Jochen Wieser. "Fast detection of narcotics by single photon ionization mass spectrometry and laser ion mobility spectrometry." In Security + Defence, edited by Colin Lewis, Douglas Burgess, Roberto Zamboni, François Kajzar, and Emily M. Heckman. SPIE, 2010. http://dx.doi.org/10.1117/12.864697.

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Sarycheva, Anastasia, Anton Grigoryev, Evgeny N. Nikolaev, and Yury Kostyukevich. "Robust Simulation Of Imaging Mass Spectrometry Data." In 35th ECMS International Conference on Modelling and Simulation. ECMS, 2021. http://dx.doi.org/10.7148/2021-0192.

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Mass spectrometry imaging (MSI) with high resolution in mass and space is an analytical method that produces distributions of ions on a sample surface. The algorithms for preprocessing and analysis of the raw data acquired from a mass spectrometer should be evaluated. To do that, the ion composition at every point of the sample should be known. This is possible via the employment of a simulated MSI dataset. In this work, we suggest a pipeline for a robust simulation of MSI datasets that resemble real data with an option to simulate the spectra acquired from any mass spectrometry instrument through the use of the experimental MSI datasets to extract simulation parameters.
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Ewing, K. J., J. Sanghera, S. W. Myers, A. M. Ervin, C. Carey, G. Gleason, L. Mosser, L. Levy, M. K. Hennessey, and R. Bulluck. "Applicability of ion mobility spectrometry for detection of quarantine pests in wood." In SPIE Commercial + Scientific Sensing and Imaging, edited by Moon S. Kim, Kuanglin Chao, and Bryan A. Chin. SPIE, 2016. http://dx.doi.org/10.1117/12.2223877.

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Kjellander, B. K. Charlotte, Leo J. van IJzendoorn, Arthur M. de Jong, Dirk J. Broer, Wouter J. H. van Gennip, Martien J. A. de Voigt, and Hans J. W. Niemantsverdriet. "Toward measuring concentration gradients in polymer-dispersed liquid crystals with secondary ion mass spectrometry." In Electronic Imaging 2004, edited by Liang-Chy Chien and Ming H. Wu. SPIE, 2004. http://dx.doi.org/10.1117/12.526549.

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von Helden, Gert, Gerard Meijer, Jan Horlebein, Eike Mucha, and Maike Lettow. "AN ION MOBILITY MASS SPECTROMETRY CRYOGENIC ION TRAP INSTRUMENT COUPLED TO THE FRITZ HABER INSTITUTE INFRARED FREE ELECTRON LASER." In 2021 International Symposium on Molecular Spectroscopy. Urbana, Illinois: University of Illinois at Urbana-Champaign, 2021. http://dx.doi.org/10.15278/isms.2021.rm09.

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Tarver, Edward E. "External second-gate Fourier transform ion mobility spectrometry: parametric optimization for detection of weapons of mass destruction." In Defense and Security, edited by Edward M. Carapezza. SPIE, 2004. http://dx.doi.org/10.1117/12.546800.

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Shi, Yuan, Kaitai Guo, Quan Yu, Xiaohao Wang, and Kai Ni. "Fluorescence quantum efficiency of three samples at atmosphere based on electrospray ionization and drift tube of ion mobility spectrometry." In Advanced Optical Imaging Technologies, edited by Xiao-Cong Yuan, Kebin Shi, and Michael G. Somekh. SPIE, 2018. http://dx.doi.org/10.1117/12.2326969.

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Hallegot, Philippe, C. Girod, M. M. LeBeau, and Riccardo Levi-Setti. "Direct high-spatial-resolution SIMS (secondary ion mass spectrometry) imaging of labeled nucleosides in human chromosomes." In Midwest - DL tentative, edited by Rudolph P. Guzik, Hans E. Eppinger, Richard E. Gillespie, Mary K. Dubiel, and James E. Pearson. SPIE, 1991. http://dx.doi.org/10.1117/12.25824.

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Reports on the topic "Ion mobility mass spectrometry imaging"

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Buratto, Steven K. Final Technical Report for DE-FG02-06ER15835: Chemical Imaging with 100nm Spatial Resolution: Combining High Resolution Flurosecence Microscopy and Ion Mobility Mass Spectrometry. Office of Scientific and Technical Information (OSTI), September 2013. http://dx.doi.org/10.2172/1091803.

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Bilbao Pena, Aivett. Algorithms and File Structure to Extend and Enhance Liquid Chromatography and Ion Mobility Mass Spectrometry Workflows - CRADA 465. Office of Scientific and Technical Information (OSTI), February 2021. http://dx.doi.org/10.2172/1867247.

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Russell, David H. Developing Ion Mobility-Mass Spectrometry for Structural Characterization of Complex Molecular Systems, Final Report/Product Number: DOE_ER-15520-3. Office of Scientific and Technical Information (OSTI), June 2017. http://dx.doi.org/10.2172/1430105.

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Bilbao Pena, Aivett. Algorithms and file structures to enhance software workflows for ion mobility mass spectrometry (IM-MS) - CRADA 410 Final Report. Office of Scientific and Technical Information (OSTI), April 2021. http://dx.doi.org/10.2172/1894883.

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