Academic literature on the topic 'MALDI mass spectrometry data'

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Journal articles on the topic "MALDI mass spectrometry data"

1

Ul’shina, D. V., D. A. Kovalev, I. V. Kuznetsova, O. V. Bobrysheva, T. L. Krasovskaya, and A. N. Kulichenko. "Software Solutions for Indication and Identification of Pathogenic Microoranisms Using Time-of-Flight Mass Spectrometry." Problems of Particularly Dangerous Infections, no. 3 (October 23, 2021): 40–50. http://dx.doi.org/10.21055/0370-1069-2021-3-40-50.

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The effectiveness of differentiation of bacterial pathogens using MALDI-TOF mass spectrometry depends on the quality of sample preparation, compliance with mass spectrometric analysis parameters and statistical approaches used, implemented by various modern software tools. The review provides a brief description of the most known software used in the processing and bioinformation analysis of time-of-flight mass spectrometry data. A list of computer platforms, programs and environments, both commercial and publicly available, is presented. The results of indication and identification of pathogens of particularly dangerous and natural-focal infections by MALDI-TOF mass spectrometry using publicly available software – programming language R, Mass-Up, MicrobeMS, licensed – MatLab, ClinProTools, as well as free web applications, including, Speclust, Ribopeaksare provided. The data on usage of such well-known platforms as MALDI BioTyper, SARAMIS Vitek-MS and Andromas (Andromas SAS, France) for inter- and intra-specific differentiation of closely related species are presented. Results of identification and differentiation of microorganisms applying MALDI-TOF mass spectrometry based on detection of specific proteins for cross-comparison – biomarkers – are given. The analysis shows that the programming language R environment is one of the publicly available universal platforms with an optimal combination of algorithms for processing and interpreting of a large array of mass spectrometric data.
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Курченко, Андрей. "MALDI MASS SPECTROMETRY - IN THE ASSESSMENT OF HUMAN MICROBIOTA. CURRENT STATE AND PERSPECTIVES." Immunology and Allergy: Science and Practice, no. 2 (July 29, 2020): 11–18. http://dx.doi.org/10.37321/immunology.2020.02-02.

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Mass spectrometry is a modern physicochemical method of analysis that allows for a qualitative and quantitative analysis of the composition of a substancebased on the preliminary ionization of its constituent atoms or molecules. One of the new methods of ionization, thanks to which the mass spectrometric study of macromolecules has become widespread, is matrix-activated laser desorption / ionization (MALDI), which is a pulsed laser irradiation of the substance under study mixed with a matrix.Тhe article presents modern data on the use of the MALDI mass- spectrometry method for conducting genus and species-specific identification of microorganisms in the practice of diagnostic laboratories. The advantages of MALDI-TOF identification in comparison with other methods of microbiota research are considered.The place of mass spectrometry in the system of laboratory diagnostics of various pathogens is indicated.
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Randolph, Timothy W., Bree L. Mitchell, Dale F. McLerran, Paul D. Lampe, and Ziding Feng. "Quantifying Peptide Signal in MALDI-TOF Mass Spectrometry Data." Molecular & Cellular Proteomics 4, no. 12 (September 29, 2005): 1990–99. http://dx.doi.org/10.1074/mcp.m500130-mcp200.

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Darie-Ion, Laura, Danielle Whitham, Madhuri Jayathirtha, Yashveen Rai, Anca-Narcisa Neagu, Costel C. Darie, and Brînduşa Alina Petre. "Applications of MALDI-MS/MS-Based Proteomics in Biomedical Research." Molecules 27, no. 19 (September 21, 2022): 6196. http://dx.doi.org/10.3390/molecules27196196.

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Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) is one of the most widely used techniques in proteomics to achieve structural identification and characterization of proteins and peptides, including their variety of proteoforms due to post-translational modifications (PTMs) or protein–protein interactions (PPIs). MALDI-MS and MALDI tandem mass spectrometry (MS/MS) have been developed as analytical techniques to study small and large molecules, offering picomole to femtomole sensitivity and enabling the direct analysis of biological samples, such as biofluids, solid tissues, tissue/cell homogenates, and cell culture lysates, with a minimized procedure of sample preparation. In the last decades, structural identification of peptides and proteins achieved by MALDI-MS/MS helped researchers and clinicians to decipher molecular function, biological process, cellular component, and related pathways of the gene products as well as their involvement in pathogenesis of diseases. In this review, we highlight the applications of MALDI ionization source and tandem approaches for MS for analyzing biomedical relevant peptides and proteins. Furthermore, one of the most relevant applications of MALDI-MS/MS is to provide “molecular pictures”, which offer in situ information about molecular weight proteins without labeling of potential targets. Histology-directed MALDI-mass spectrometry imaging (MSI) uses MALDI-ToF/ToF or other MALDI tandem mass spectrometers for accurate sequence analysis of peptide biomarkers and biological active compounds directly in tissues, to assure complementary and essential spatial data compared with those obtained by LC-ESI-MS/MS technique.
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Iles, Ray K., Jason K. Iles, Raminta Zmuidinaite, and Michael Roberts. "A How to Guide: Clinical Population Test Development and Authorization of MALDI-ToF Mass Spectrometry-Based Screening Tests for Viral Infections." Viruses 14, no. 9 (September 3, 2022): 1958. http://dx.doi.org/10.3390/v14091958.

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Applying MALDI-ToF mass spectrometry as a clinical diagnostic test for viruses is different from that of bacteria, fungi and other micro-organisms. This is because the systems biology of viral infections, the size and chemical nature of specific viral proteins and the mass spectrometry biophysics of how they are quantitated are fundamentally different. The analytical challenges to overcome when developing a clinical MALDI-ToF mass spectrometry tests for a virus, particularly human pathogenic enveloped viruses, are sample enrichment, virus envelope disruption, optimal matrix formulation, optimal MALDI ToF MS performance and optimal spectral data processing/bioinformatics. Primarily, the instrument operating settings have to be optimized to match the nature of the viral specific proteins, which are not compatible with setting established when testing for bacterial and many other micro-organisms. The capacity to be a viral infection clinical diagnostic instrument often stretches current mass spectrometers to their operational design limits. Finally, all the associated procedures, from sample collection to data analytics, for the technique have to meet the legal and operational requirement for often high-throughput clinical testing. Given the newness of the technology, clinical MALDI ToF mass spectrometry does not fit in with standard criteria applied by regulatory authorities whereby numeric outputs are compared directly to similar technology tests that have already been authorized for use. Thus, CLIA laboratory developed test (LDT) criteria have to be applied. This article details our experience of developing a SAR-CoV-2 MALDI-ToF MS test suitable for asymptomatic carrier infection population screening.
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Trede, Dennis, Jan Hendrik Kobarg, Janina Oetjen, Herbert Thiele, Peter Maass, and Theodore Alexandrov. "On the Importance of Mathematical Methods for Analysis of MALDI-Imaging Mass Spectrometry Data." Journal of Integrative Bioinformatics 9, no. 1 (March 1, 2012): 1–11. http://dx.doi.org/10.1515/jib-2012-189.

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Summary In the last decade, matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS), also called as MALDI-imaging, has proven its potential in proteomics and was successfully applied to various types of biomedical problems, in particular to histopathological label-free analysis of tissue sections. In histopathology, MALDI-imaging is used as a general analytic tool revealing the functional proteomic structure of tissue sections, and as a discovery tool for detecting new biomarkers discriminating a region annotated by an experienced histologist, in particular, for cancer studies.A typical MALDI-imaging data set contains 108 to 109 intensity values occupying more than 1 GB. Analysis and interpretation of such huge amount of data is a mathematically, statistically and computationally challenging problem. In this paper we overview some computational methods for analysis of MALDI-imaging data sets. We discuss the importance of data preprocessing, which typically includes normalization, baseline removal and peak picking, and hightlight the importance of image denoising when visualizing IMS data.
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Creaser, Colin S., James C. Reynolds, Andrew J. Hoteling, William F. Nichols, and Kevin G. Owens. "Atmospheric Pressure Matrix-Assisted Laser Desorption/Ionisation Ion Trap Mass Spectrometry of Synthetic Polymers: A Comparison with Vacuum Matrix-Assisted Laser Desorption/Ionisation Time-of-Flight Mass Spectrometry." European Journal of Mass Spectrometry 9, no. 1 (February 2003): 33–44. http://dx.doi.org/10.1255/ejms.528.

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Atmospheric pressure matrix-assisted laser desorption/ionisation quadrupole ion trap (AP-MALDI/QIT) mass spectrometry has been investigated for the analysis of polyethylene glycol (PEG 1500) and a hyperbranched polymer (polyglycidol) in the presence of alkali–metal salts. Mass spectra of PEG 1500 obtained at atmospheric pressure showed dimetallated matrix/analyte adducts, in addition to the expected alkali–metal/PEG ions, for all matrix/alkali–metal salt combinations. The relative intensities of the desorbed ions were dependent on the matrix, the alkali–metal salt added to aid cationisation and the ion trap interface conditions [capillary temperature, in-source collisionally-induced dissociation (CID)]. These data indicate that the adducts are rapidly stabilised by collisional cooling enabling them to be transferred into the ion trap. Experiments using identical sample preparation conditions were carried out on a vacuum MALDI time-of-flight (ToF) mass spectrometer. In all cases, vacuum MALDI-ToF spectra showed only alkali–metal/PEG ions and no matrix/analyte adducts. The tandem mass spectrometry (MS/MS) capability of the ion trap has been demonstrated for a lithiated polyglycol yielding a rich fragment-ion spectrum. Analysis of the hyperbranched polymer polyglycidol by AP-MALDI/QIT reveals the characteristic ion series for these polymers as also observed under vacuum MALDI-ToF conditions.
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Kepper, Pamela, Richard Reinhardt, Andreas Dahl, Hans Lehrach, and Sascha Sauer. "Matrix-Assisted Laser Desorption/Ionization Mass Spectrometric Analysis of DNA on Microarrays." Clinical Chemistry 52, no. 7 (July 1, 2006): 1303–10. http://dx.doi.org/10.1373/clinchem.2006.067264.

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Abstract Background: Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry is a powerful tool in biomolecule analysis with a wide range of application possibilities, including genotyping of single-base variations (also known as single-nucleotide polymorphisms, or SNPs) for candidate gene studies and diagnostic typing of DNA markers. We tested a method that does not require stringent purification of the nucleic acids and/or the use of modification chemistry before mass spectrometry analysis. Methods: We used an alternative direct analysis approach that allows MALDI analysis of crude DNA samples printed on microscope slides densely coated with primary amino groups that efficiently bind negatively charged DNA. After simple washing of the slides, we applied MALDI matrix and used a conventional MALDI mass spectrometer to detect DNA products. Results: We analyzed crude oligonucleotide samples and performed automated genotyping of single-base variations in 72 DNA samples. Conclusion: This procedure offers an operational short-cut compared with standard MALDI procedures for preparation of oligonucleotides, including purification, and thus is an efficient tool for genotyping applications, particularly those requiring accurate, flexible, and rapid data generation and medium throughput.
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Dannhorn, Andreas, Emine Kazanc, Gregory Hamm, John G. Swales, Nicole Strittmatter, Gareth Maglennon, Richard J. A. Goodwin, and Zoltan Takats. "Correlating Mass Spectrometry Imaging and Liquid Chromatography-Tandem Mass Spectrometry for Tissue-Based Pharmacokinetic Studies." Metabolites 12, no. 3 (March 18, 2022): 261. http://dx.doi.org/10.3390/metabo12030261.

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Liquid chromatography-tandem mass spectrometry (LC-MS/MS) is a standard tool used for absolute quantification of drugs in pharmacokinetic (PK) studies. However, all spatial information is lost during the extraction and elucidation of a drugs biodistribution within the tissue is impossible. In the study presented here we used a sample embedding protocol optimized for mass spectrometry imaging (MSI) to prepare up to 15 rat intestine specimens at once. Desorption electrospray ionization (DESI) and matrix assisted laser desorption/ionization (MALDI) mass spectrometry imaging (MSI) were employed to determine the distributions and relative abundances of four benchmarking compounds in the intestinal segments. High resolution MALDI-MSI experiments performed at 10 µm spatial resolution allowed to determine the drug distribution in the different intestinal histological compartments to determine the absorbed and tissue bound fractions of the drugs. The low tissue bound drug fractions, which were determined to account for 56–66% of the total drug, highlight the importance to understand the spatial distribution of drugs within the histological compartments of a given tissue to rationalize concentration differences found in PK studies. The mean drug abundances of four benchmark compounds determined by MSI were correlated with the absolute drug concentrations. Linear regression resulted in coefficients of determination (R2) ranging from 0.532 to 0.926 for MALDI-MSI and R2 values ranging from 0.585 to 0.945 for DESI-MSI, validating a quantitative relation of the imaging data. The good correlation of the absolute tissue concentrations of the benchmark compounds and the MSI data provides a bases for relative quantification of compounds within and between tissues, without normalization to an isotopically labelled standard, provided that the compared tissues have inherently similar ion suppression effects.
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10

Ulshina, D. V., D. A. Kovalev, A. M. Zhirov, N. V. Zharinova, A. A. Khudoleev, O. I. Kogotkova, V. I. Efremenko, N. I. Evchenko, and A. N. Kulichenko. "FEATURES OF MASS-SPECTROMETRIC PROTEIN PROFILES OF STRAINS OF BRUCELLOSIS CAUSATIVE AGENT DURING PREPARATION OF CULTURE ON VARIOUS NUTRIENT MEDIA." Journal of microbiology epidemiology immunobiology, no. 1 (February 28, 2016): 29–34. http://dx.doi.org/10.36233/0372-9311-2016-1-29-34.

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Aim. Carry out comparative analysis using time-of-flight mass-spectrometry with matrix laser desorption/ionization (MALDI-TOF MS) of protein profiles of brucellosis causative agents (Brucella melitensis Rev-1 and Brucella abortus 19BA), cultivated in various nutrient media: Albimi agar, brucellagar and erythrit-agar. Materials and methods. Vaccine strains: Brucella melitensis Rev-1 and Brucella abortus 19BA. Protein profiling in linear mode on Microflex «Bruker Daltonics» MALDI-TOF mass-spectrometer. Results. A number of characteristic features of brucella mass-spectra was detected: in particular, preservation of the total qualitative composition of protein profiles of cultures and significant differences in the intensity of separate peaks depending on the nutrient medium used. Conclusion. Based on the analysis of the data obtained, use of Albimi agar as the nutrient medium for preparation of brucella culture samples for mass-spectrometric analysis was shown to be optimal.
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Dissertations / Theses on the topic "MALDI mass spectrometry data"

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Momo, Remi Ako-Mbianyor. "MALDI-ToF mass spectrometry biomarker profiling via multivariate data analysis application in the biopharmaceutical bioprocessing industry." Thesis, University of Newcastle upon Tyne, 2013. http://hdl.handle.net/10443/1939.

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Matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-ToF MS) is a technique by which protein profiles can be rapidly produced from biological samples. Proteomic profiling and biomarker identification using MALDI-ToF MS have been utilised widely in microbiology for bacteria identification and in clinical proteomics for disease-related biomarker discovery. To date, the benefits of MALDI-ToF MS have not been realised in the area of mammalian cell culture during bioprocessing. This thesis explores the approach of ‘intact-cell’ MALDI-ToF MS (ICM-MS) combined with projection to latent structures – discriminant analysis (PLS-DA), to discriminate between mammalian cell lines during bioprocessing. Specifically, the industrial collaborator, Lonza Biologics is interested in adopting this approach to discriminate between IgG monoclonal antibody producing Chinese hamster ovaries (CHO) cell lines based on their productivities and identify protein biomarkers which are associated with the cell line productivities. After classifying cell lines into two categories (high/low producers; Hs/Ls), it is hypothesised that Hs and Ls CHO cells exhibit different metabolic profiles and hence differences in phenotypic expression patterns will be observed. The protein expression patterns correlate to the productivities of the cell lines, and introduce between-class variability. The chemometric method of PLS-DA can use this variability to classify the cell lines as Hs or Ls. A number of differentially expressed proteins were matched and identified as biomarkers after a SwissProt/TrEMBL protein database search. The identified proteins revealed that proteins involved in biological processes such as protein biosynthesis, protein folding, glycolysis and cytoskeleton architecture were upregulated in Hs. This study demonstrates that ICM-MS combined with PLS-DA and a protein database search can be a rapid and valuable tool for biomarker discovery in the bioprocessing industry. It may help in providing clues to potential cell genetic engineering targets as well as a tool in process development in the bioprocessing industry. With the completion of the sequencing of the CHO genome, this study provides a foundation for rapid biomarker profiling of CHO cell lines in culture during recombinant protein manufacturing.
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Rabe, Jan-Hinrich [Verfasser], and Carsten [Akademischer Betreuer] Hopf. "Multimodal FTIR Microscopy-guided Acquisition and Interpretation of MALDI Mass Spectrometry Imaging Data / Jan-Hinrich Rabe ; Betreuer: Carsten Hopf." Heidelberg : Universitätsbibliothek Heidelberg, 2018. http://d-nb.info/1177385341/34.

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uk, siricordcc@yahoo co, and Cornelia Charito Siricord. "Detection of Phytophthora species by MALDI-TOF mass spectrometry." Murdoch University, 2005. http://wwwlib.murdoch.edu.au/adt/browse/view/adt-MU20070717.125452.

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Phytophthora diseases have caused worldwide economic, social and environmental impacts for decades. Once their presence is confirmed, they are difficult to eradicate. To reduce and manage the damage inflicted by the pathogen, fast and reliable disease management protocols are required. Tests that enable the rapid and reliable identification of the pathogen assist greatly in disease management. Phytophthora species are traditionally not only detected by baiting but also by plating of symptomatic tissue on selective media. Species can be identified by the characteristics of the mycelium growing out of the bait. However, the method is low throughput, labour intensive, and prone to false negatives. An alternative approach would be to detect the pathogen by the presence of its DNA. This involves amplification of the pathogen DNA using Polymerase Chain Reaction (PCR) and detection of the amplification product. Detection is usually by agarose gel electrophoresis. However, this is also a labour intensive process involving pouring, loading, running, and staining of the gels. The aim of this thesis is to explore the use of Matrix Assisted Laser Desorption/ Ionisation Time-of-Flight (MALDI-TOF) mass spectrometry for detection of PCR products. This procedure enables the analysis of large numbers of samples within a very short time-frame as the average time for analysis of each sample is in the order of milliseconds. The assay involves annealing an extension (genotyping) primer to the PCR product and its extension by a single nucleotide. The nature of the nucleotide added differentiates species as does the site to which the primer anneals. Multiple extension (genotyping) primers can be used together in a single reaction for detection of multiple species. In this project four genotyping primers (GPs) were designed from the ITS regions of Phytophthora palmivora, Phytophthora cinnamomi, Phytophthora citricola, and Phytophthora cambivora. The extension primers were tested for their specificity on the DNA of the target species. The four primers designed were specific for their intended targets except for GPpalm3 which in addition to being extended by ddT when tested with DNA from P. palmivora, was also extended by ddC when tested with DNA from other species of Phytophthora or Pythium. These primers were also tested for their ability to detect multiple Phytophthora species in a single reaction (multiplexing). Mixtures of primers were added to mixed DNA templates and the primer extension reaction carried out. The primers were designed so that their masses were sufficiently different for them to be identified from a mixture. Six replicates were analysed for each reaction. In general only about 1-3 of the six replicates gave a positive reaction. This indicates that there may be some interference between primers, or that the presence of all four nucleotides interfered with the primer extension reaction. Increasing either the amount of enzyme, the amount of nucleotides or both did not improve the results. The sensitivity of detection was tested by the addition of different amounts of mycelium to soil. The detection sensitivity depended on the primer pair used for PCR amplification. The ITS1/2 primer pair was more sensitive than the ITS1/4 pair. The limit of detection was 1 ìg mycelium g soil-1. However using nested PCR, levels of sensitivity comparable to those obtained using the ITS1/2 primer pair could be achieved. Primers to other regions of the genome such as the beta cinnamomin elicitin gene gave very low levels of sensitivity compared to the ITS primers. In comparison with DNA detection we found that the limit of detection using baiting was 4 ìg mycelium g soil-1. Results below this limit were unreliable. The method suffered from the additional disadvantage that it took a long time in comparison to DNA detection. DNA detection methods do not distinguish between living and dead organisms in the soil. However it can be hypothesised that DNA is unlikely to persist for any significant length of time in soil. To test this, we added plasmid DNA to soil and tested the persistence of this DNA using a variety of methods such as precipitation of labelled DNA, southern blotting and PCR amplification. It was found that in general, in soils from different ecosystems, the bulk of the DNA was undetectable after 24 hours. The rate of DNA breakdown differed with the soil type. In some soils, the added DNA was not detected even after 2 hours, whereas in others it could be observed after 10 hours. The detection depended on the method. Southern blotting showed that although DNA could be observed at 10 hours, by 24 hours it was completely degraded. In contrast a PCR product could be obtained from the soil extracts up to 24 hours. In a separate experiment, plasmid DNA was detectable over a 24 hour incubation period in 5 soil samples from 5 different sites. The results suggest that DNA is degraded rapidly in soil and is unlikely to persist longer than 24 hours. The results in this thesis demonstrate that MALDI-TOF MS is a suitable alternative to agarose gel electrophoresis for analysis of PCR products. The technique is rapid, differentiates species from mixtures, is high-throughput and amenable to automation. Implementation will require further research to automate the primer extension assay to reduce the sensitivity to impurities in the DNA and to design parameters for sampling asymptomatic material.
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4

Wyatt, Mark Francis. "Analysis of acrylic polymers by MALDI-TOF mass spectrometry." Thesis, Durham University, 2001. http://etheses.dur.ac.uk/3962/.

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Poly(methyl methacrylate) (PMMA) homopolymers synthesised using 'classical' anionic methods and subsequently studied by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOF-MS) are discussed. Specifically, the attempts at different end-group functionalisation reactions, their varying degrees of success, and the characterisation of these functionalized polymers via MALDI are reported. Extra peaks were observed in the spectra of samples containing a tertiary amine end-group. A mechanism for the in situ elimination of H(_2)(g) involving these end-groups, which would fit the observations, is proposed. Two alternative, 'non-classical' routes to the desired materials were investigated, as difficulties in successfully performing capping reactions to give end functionalised PMMA were noted. The first method was a variation of standard anionic polymerisation that involved the use of lithium silanolates, which could be performed at a higher temperature than normal. The second was a controlled free-radical technique known as Reversible Addition-Fragmentation Chain Transfer (RAFT). A lack of control of the polymerisation to the desired degree was observed with the former method. A well-defined RAFT sample was observed to undergo in situ eliminadon also, for which a mechanism involving the dithioester end-group is proposed, and which is supported by MALDI-collision induced dissociation (CID) evidence. The synthesis of block copolymers of various compositions of MMA with r-butyl methacrylate (t-BMA) and hexyl methacrylate (HMA), along with their homopolymers, and their subsequent characterisation is reported. PHMA was analysed easily, in contrast to Pt-BMA. Only copolymers with a high PMMA content were analysed successfully and this has been rationalised in terms of the factors that affect cationisation. The characterisation of equimolar blends of various end-functionalised PMMA samples is reported also. Samples that favour the binding of a metal ion over protonation appear to have a higher ion yield. Once more, these observations are rationalised in terms of the factors that affect cationisation.
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5

Siricord, Cornelia Charito. "Detection of Phytophthora species by MALDI-TOF mass spectrometry." Thesis, Siricord, Cornelia Charito (2005) Detection of Phytophthora species by MALDI-TOF mass spectrometry. PhD thesis, Murdoch University, 2005. https://researchrepository.murdoch.edu.au/id/eprint/314/.

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Phytophthora diseases have caused worldwide economic, social and environmental impacts for decades. Once their presence is confirmed, they are difficult to eradicate. To reduce and manage the damage inflicted by the pathogen, fast and reliable disease management protocols are required. Tests that enable the rapid and reliable identification of the pathogen assist greatly in disease management. Phytophthora species are traditionally not only detected by baiting but also by plating of symptomatic tissue on selective media. Species can be identified by the characteristics of the mycelium growing out of the bait. However, the method is low throughput, labour intensive, and prone to false negatives. An alternative approach would be to detect the pathogen by the presence of its DNA. This involves amplification of the pathogen DNA using Polymerase Chain Reaction (PCR) and detection of the amplification product. Detection is usually by agarose gel electrophoresis. However, this is also a labour intensive process involving pouring, loading, running, and staining of the gels. The aim of this thesis is to explore the use of Matrix Assisted Laser Desorption/ Ionisation Time-of-Flight (MALDI-TOF) mass spectrometry for detection of PCR products. This procedure enables the analysis of large numbers of samples within a very short time-frame as the average time for analysis of each sample is in the order of milliseconds. The assay involves annealing an extension (genotyping) primer to the PCR product and its extension by a single nucleotide. The nature of the nucleotide added differentiates species as does the site to which the primer anneals. Multiple extension (genotyping) primers can be used together in a single reaction for detection of multiple species. In this project four genotyping primers (GPs) were designed from the ITS regions of Phytophthora palmivora, Phytophthora cinnamomi, Phytophthora citricola, and Phytophthora cambivora. The extension primers were tested for their specificity on the DNA of the target species. The four primers designed were specific for their intended targets except for GPpalm3 which in addition to being extended by ddT when tested with DNA from P. palmivora, was also extended by ddC when tested with DNA from other species of Phytophthora or Pythium. These primers were also tested for their ability to detect multiple Phytophthora species in a single reaction (multiplexing). Mixtures of primers were added to mixed DNA templates and the primer extension reaction carried out. The primers were designed so that their masses were sufficiently different for them to be identified from a mixture. Six replicates were analysed for each reaction. In general only about 1-3 of the six replicates gave a positive reaction. This indicates that there may be some interference between primers, or that the presence of all four nucleotides interfered with the primer extension reaction. Increasing either the amount of enzyme, the amount of nucleotides or both did not improve the results. The sensitivity of detection was tested by the addition of different amounts of mycelium to soil. The detection sensitivity depended on the primer pair used for PCR amplification. The ITS1/2 primer pair was more sensitive than the ITS1/4 pair. The limit of detection was 1 mcg mycelium g soil-1. However using nested PCR, levels of sensitivity comparable to those obtained using the ITS1/2 primer pair could be achieved. Primers to other regions of the genome such as the beta cinnamomin elicitin gene gave very low levels of sensitivity compared to the ITS primers. In comparison with DNA detection we found that the limit of detection using baiting was 4 mcg mycelium g soil-1. Results below this limit were unreliable. The method suffered from the additional disadvantage that it took a long time in comparison to DNA detection. DNA detection methods do not distinguish between living and dead organisms in the soil. However it can be hypothesised that DNA is unlikely to persist for any significant length of time in soil. To test this, we added plasmid DNA to soil and tested the persistence of this DNA using a variety of methods such as precipitation of labelled DNA, southern blotting and PCR amplification. It was found that in general, in soils from different ecosystems, the bulk of the DNA was undetectable after 24 hours. The rate of DNA breakdown differed with the soil type. In some soils, the added DNA was not detected even after 2 hours, whereas in others it could be observed after 10 hours. The detection depended on the method. Southern blotting showed that although DNA could be observed at 10 hours, by 24 hours it was completely degraded. In contrast a PCR product could be obtained from the soil extracts up to 24 hours. In a separate experiment, plasmid DNA was detectable over a 24 hour incubation period in 5 soil samples from 5 different sites. The results suggest that DNA is degraded rapidly in soil and is unlikely to persist longer than 24 hours. The results in this thesis demonstrate that MALDI-TOF MS is a suitable alternative to agarose gel electrophoresis for analysis of PCR products. The technique is rapid, differentiates species from mixtures, is high-throughput and amenable to automation. Implementation will require further research to automate the primer extension assay to reduce the sensitivity to impurities in the DNA and to design parameters for sampling asymptomatic material.
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6

Siricord, Cornelia Charito. "Detection of Phytophthora species by MALDI-TOF mass spectrometry." Siricord, Cornelia Charito (2005) Detection of Phytophthora species by MALDI-TOF mass spectrometry. PhD thesis, Murdoch University, 2005. http://researchrepository.murdoch.edu.au/314/.

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Abstract:
Phytophthora diseases have caused worldwide economic, social and environmental impacts for decades. Once their presence is confirmed, they are difficult to eradicate. To reduce and manage the damage inflicted by the pathogen, fast and reliable disease management protocols are required. Tests that enable the rapid and reliable identification of the pathogen assist greatly in disease management. Phytophthora species are traditionally not only detected by baiting but also by plating of symptomatic tissue on selective media. Species can be identified by the characteristics of the mycelium growing out of the bait. However, the method is low throughput, labour intensive, and prone to false negatives. An alternative approach would be to detect the pathogen by the presence of its DNA. This involves amplification of the pathogen DNA using Polymerase Chain Reaction (PCR) and detection of the amplification product. Detection is usually by agarose gel electrophoresis. However, this is also a labour intensive process involving pouring, loading, running, and staining of the gels. The aim of this thesis is to explore the use of Matrix Assisted Laser Desorption/ Ionisation Time-of-Flight (MALDI-TOF) mass spectrometry for detection of PCR products. This procedure enables the analysis of large numbers of samples within a very short time-frame as the average time for analysis of each sample is in the order of milliseconds. The assay involves annealing an extension (genotyping) primer to the PCR product and its extension by a single nucleotide. The nature of the nucleotide added differentiates species as does the site to which the primer anneals. Multiple extension (genotyping) primers can be used together in a single reaction for detection of multiple species. In this project four genotyping primers (GPs) were designed from the ITS regions of Phytophthora palmivora, Phytophthora cinnamomi, Phytophthora citricola, and Phytophthora cambivora. The extension primers were tested for their specificity on the DNA of the target species. The four primers designed were specific for their intended targets except for GPpalm3 which in addition to being extended by ddT when tested with DNA from P. palmivora, was also extended by ddC when tested with DNA from other species of Phytophthora or Pythium. These primers were also tested for their ability to detect multiple Phytophthora species in a single reaction (multiplexing). Mixtures of primers were added to mixed DNA templates and the primer extension reaction carried out. The primers were designed so that their masses were sufficiently different for them to be identified from a mixture. Six replicates were analysed for each reaction. In general only about 1-3 of the six replicates gave a positive reaction. This indicates that there may be some interference between primers, or that the presence of all four nucleotides interfered with the primer extension reaction. Increasing either the amount of enzyme, the amount of nucleotides or both did not improve the results. The sensitivity of detection was tested by the addition of different amounts of mycelium to soil. The detection sensitivity depended on the primer pair used for PCR amplification. The ITS1/2 primer pair was more sensitive than the ITS1/4 pair. The limit of detection was 1 mcg mycelium g soil-1. However using nested PCR, levels of sensitivity comparable to those obtained using the ITS1/2 primer pair could be achieved. Primers to other regions of the genome such as the beta cinnamomin elicitin gene gave very low levels of sensitivity compared to the ITS primers. In comparison with DNA detection we found that the limit of detection using baiting was 4 mcg mycelium g soil-1. Results below this limit were unreliable. The method suffered from the additional disadvantage that it took a long time in comparison to DNA detection. DNA detection methods do not distinguish between living and dead organisms in the soil. However it can be hypothesised that DNA is unlikely to persist for any significant length of time in soil. To test this, we added plasmid DNA to soil and tested the persistence of this DNA using a variety of methods such as precipitation of labelled DNA, southern blotting and PCR amplification. It was found that in general, in soils from different ecosystems, the bulk of the DNA was undetectable after 24 hours. The rate of DNA breakdown differed with the soil type. In some soils, the added DNA was not detected even after 2 hours, whereas in others it could be observed after 10 hours. The detection depended on the method. Southern blotting showed that although DNA could be observed at 10 hours, by 24 hours it was completely degraded. In contrast a PCR product could be obtained from the soil extracts up to 24 hours. In a separate experiment, plasmid DNA was detectable over a 24 hour incubation period in 5 soil samples from 5 different sites. The results suggest that DNA is degraded rapidly in soil and is unlikely to persist longer than 24 hours. The results in this thesis demonstrate that MALDI-TOF MS is a suitable alternative to agarose gel electrophoresis for analysis of PCR products. The technique is rapid, differentiates species from mixtures, is high-throughput and amenable to automation. Implementation will require further research to automate the primer extension assay to reduce the sensitivity to impurities in the DNA and to design parameters for sampling asymptomatic material.
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Rodrigues, Lívia Riberti 1988. "Análise de impurezas de formas farmacêuticas sólidas por MALDI Mass Spectrometry Imaging (MALDI-MSI)." [s.n.], 2014. http://repositorio.unicamp.br/jspui/handle/REPOSIP/312437.

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Orientador: Rodrigo Ramos Catharino
Texto em português e inglês
Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Ciências Médicas
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Resumo: Atualmente, as doenças cardiovasculares constituem uma das primeiras causas de mortes no Brasil e no mundo. Neste cenário, as estatinas constituem uma notável classe de medicamentos redutores de colesterol e têm sido associadas com uma expressiva diminuição da morbidade e mortalidade cardiovascular para pacientes em prevenção primária ou secundária da doença coronariana. Elas agem inibindo competitivamente a enzima HMG-CoA redutase, através da afinidade destes fármacos pelo sítio ativo da enzima. Esta enzima é responsável por catalisar a conversão do substrato HMG-CoA em mevalonato, um dos precursores do colesterol. A crescente necessidade e busca por medicamentos cada vez mais efetivos traz a preocupação na segurança destes produtos para seus usuários. Neste sentido, o conhecimento das impurezas e produtos de degradação torna-se necessário para garantir sua qualidade. Uma técnica muito utilizada para análises de impurezas e degradantes é a espectrometria de massas, pois é uma técnica sensível e seletiva e permite elucidar as estruturas químicas presentes na formulação do medicamento. Sendo assim, amostras de Atorvastatina cálcica foram analisadas pela técnica de espectrometria de massas por imagem (MALDI-MSI), permitindo a quantificação de impurezas do medicamento através da imagem da distribuição dessa impureza no comprimido. Dessa forma, é possível minimizar o preparo de amostra e obter um melhor conhecimento da formulação
Abstract: Currently, cardiovascular diseases constitute one of the first causes of deaths in Brazil and in the world. In this scenario, the statins are a notable class of medicines and cholesterol reducers have been associated with a significant reduction in cardiovascular morbidity and mortality for patients in primary or secondary prevention of coronary heart disease. They act by inhibiting competitively the enzyme HMG-CoA reductase, through the affinity of these drugs by the active site of the enzyme. This enzyme is responsible for catalyzing the conversion of HMG-CoA to mevalonate substrate, one of the precursors of cholesterol. The growing need and search for increasingly effective drugs brings the concern on the safety of these drugs for their users. In this sense, the knowledge of the impurities and degradation products becomes necessary to ensure their quality. A widely used technique for analysis of impurities and degrading is mass spectrometry, because it is a sensitive and selective technique and allows elucidating the chemical structures of the present formulation of the medicinal product. Thus, samples of Atorvastatin calcium were analyzed by the technique of mass spectrometry imaging (MALDI-MSI), which allows the quantification of impurities from the medicine through the image of the distribution of impurity in the tablet. That way, it is possible minimize sample preparation and get a better understanding of the formulation
Mestrado
Ciencias Biomedicas
Mestra em Ciências Médicas
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Allwood, Daniel Anthony. "Characterisation and ionisation modelling of matrices in MALDI mass spectrometry." Thesis, University of Hull, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.301477.

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Guan, Bing. "Characterization of Oligosaccharides and Nanoparticles by MALDI-TOF Mass Spectrometry." ScholarWorks@UNO, 2007. http://scholarworks.uno.edu/td/585.

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The possibilities of differentiating linkage positions and anomeric configurations of small oligosaccharides by negative ion mode MALDI using anion attachment followed by PSD are investigated. By careful initial adjustment of the focusing mirror ratios allowing acquisition of the peaks of interest within the same PSD segment, it is possible to obtain highly reproducible relative ion abundances. Discrimination of different linkage types is achieved by analysis of structurally-informative diagnostic peaks offered by PSD spectra of chloride adducts of oligosaccharides, whereas the relative peak intensities of selected diagnostic fragment pairs make differentiation of anomeric configuration possible. F- and Ac- cannot form anionic adducts with the oligosaccharides in significant yields. However, Br-, I- and NO3- anionic adducts consistently appear in higher abundances relative to [M - H]-, just like Cl-. Mildly acidic saccharides form both deprotonated molecules and anionic adducts, making it possible to simultaneously detect neutral and acidic oligosaccharides via anion attachment. PSD of [oligosaccharide + Cl]- yields structurally-informative fragment ions that retain the charge on the sugar molecule rather than solely forming Cl-, whereas PSD of Br-, I- and NO3- adducts of oligosaccharides yield the respective anions as the main product ions without offering structural information concerning the sugar. PSD of the chloride adduct of saccharides containing 1-2 linkages also yields chlorine-containing fragment ions. MALDI-TOF-MS and LDI-TOF-MS are shown to be useful for characterization of ultra-small titania nanoparticles. Peak maxima in MALDI-TOF mass spectra are found to correlate with nanoparticle size. The size distributions of TiO2 nanoparticles, obtained from MALDI- and LDI-TOF-MS are in good agreement with parallel TEM observations. PSD analysis of inorganic x nanomaterials is performed and valuable information about the structure of analytes has been obtained. A group of inorganic nitrate and perchlorate salts of forensic and health interest are investigated by LDI- and MALDI-TOF MS. In each case, a series of characteristic cluster ions are predominant in the negative-ion mode. The number and identity of metal atoms and anions in the recorded cluster ions can be positively identified by their m/z values, distinctive isotopic patterns and characteristic PSD fragmentation patterns.
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Kirmess, Kristopher Michael. "Investigation of Primary Ion Formation Mechanisms in UV-MALDI-MS Using Excited State Dynamics of Common MALDI Matrices." OpenSIUC, 2015. https://opensiuc.lib.siu.edu/dissertations/1110.

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The motivation of this dissertation is to provide insight towards primary ionization mechanisms within MALDI mass spectrometry. Albeit MALDI-MS is an extensively used analytical technique, the mechanism in which primary ions are created is still under scrutiny. Two current models of primary ionization exist which claim to elucidate the ion formation mechanisms within MALDI. In this work, excited state dynamics of MALDI matrices are shown to play an important role in the ionization mechanism. Upon inspection of the thermodynamic properties of commonly used MALDI matrices, no correlation was observed when plotted against their respective analyte ion yields. However, the excited state singlet lifetimes of these matrices seem to correlate well with their respective analyte ion yields. In the broadest sense, this correlation further supports the fact that photophysical properties of the matrix should be included in current UV-MALDI models. Investigation of a claim which stated singlet energy pooling reactions were absent in the MALDI matrix 2,4,6-trihydroxyacetophenone (THAP) resulted in the discovery of a new energy pooling mechanisms. Characteristic of aromatic ketones such as THAP, intersystem crossing is an efficient process in solution, which gives way to fluorescence in the solid state. Triplet pooling mechanisms from two neighboring THAP molecules are proposed and appear to be dependent on the preparation solvent used. These triplet pooling reactions are thought to play an important role in the primary ion formation mechanism within MALDI. To further investigate the theory of triplet species playing a vital role in MALDI ionization, the internal heavy-atom effect was employed to determine the effect of the triplet species. MALDI mass spectra and excited state decays of these heavy-atom substituted matrices were collected to demonstrate the relationship between triplet species and analyte ionization efficiency. Gas-phase thermodynamics and absorption at 337 nm were also examined to determine if these properties affected the analyte ion signal observed in the MALDI mass spectrum. Using the information collected from the previous study, an advanced MALDI matrix is synthesized. Addition of covalently bound iodine to the gold standard matrix, α-cyano-hydroxycinnamic acid, should drastically improve the performance of the non-substituted matrix due to the increase in triplet species present for pooling reactions. Sample preparation methods in MALDI are examined as are the effects of crystal morphology on the overall signal observed in the mass spectrum. Exciton hopping and pooling rates are highly dependent on intermolecular interactions, so it is expected that crystal packing will affect MALDI. As noted for THAP, preparation solvent plays a significant role in not only crystal morphology, but also the excited state dynamics for all matrices studied.
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Books on the topic "MALDI mass spectrometry data"

1

Porta Siegel, Tiffany, ed. MALDI Mass Spectrometry Imaging. Cambridge: Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839165191.

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Cole, Richard B., ed. Electrospray and MALDI Mass Spectrometry. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470588901.

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Li, Liang, ed. Maldi Mass Spectrometry for Synthetic Polymer Analysis. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2009. http://dx.doi.org/10.1002/9780470567234.

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Pasch, Harald, and Wolfgang Schrepp. MALDI-TOF Mass Spectrometry of Synthetic Polymers. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-662-05046-0.

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Pasch, Harald. MALDI-TOF Mass Spectrometry of Synthetic Polymers. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003.

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Cole, Richard B. Electrospray and MALDI mass spectrometry: Fundamentals, instrumentation, practicalities, and biological applications. 2nd ed. Hoboken, N.J: Wiley, 2010.

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Cramer, Rainer, ed. Advances in MALDI and Laser-Induced Soft Ionization Mass Spectrometry. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-04819-2.

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L, Burlingame A., ed. Biological mass spectrometry. Amsterdam: Elsevier Academic Press, 2005.

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Rune, Matthiesen, ed. Mass spectrometry data analysis in proteomics. Totowa, N.J: Humana Press, 2007.

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Rune, Matthiesen. Mass Spectrometry Data Analysis in Proteomics. New Jersey: Humana Press, 2006. http://dx.doi.org/10.1385/1597452750.

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Book chapters on the topic "MALDI mass spectrometry data"

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Balluff, BENJAMIN. "Chapter 12. The Role of Informatics and Data Analysis in MALDI Mass Spectrometry Imaging." In MALDI Mass Spectrometry Imaging, 262–90. Cambridge: Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839165191-00262.

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Wallace, William E., Anthony J. Kearsley, and Charles M. Guttman. "New Approaches to Data Reduction in Mass Spectrometry." In Maldi Mass Spectrometry for Synthetic Polymer Analysis, 205–17. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2009. http://dx.doi.org/10.1002/9780470567234.ch9.

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Zhang, Lin, and Todd R. Sandrin. "Maximizing the Taxonomic Resolution of MALDI-TOF-MS-Based Approaches to Bacterial Characterization: From Culture Conditions Through Data Analysis." In Applications of Mass Spectrometry in Microbiology, 147–81. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-26070-9_6.

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Santos, Cledir, Paula Galeano, Reginaldo Lima Neto, Manoel Marques Evangelista Oliveira, and Nelson Lima. "MALDI-TOF MS and its requirements for fungal identification." In Trends in the systematics of bacteria and fungi, 119–40. Wallingford: CABI, 2021. http://dx.doi.org/10.1079/9781789244984.0119.

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Abstract Matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS) is now used as a routine technique for the fast and reliable identification of fungi at the species level and, currently, it represents an important phenotypic methodology based on proteomic profiles. The main limitations to MALDI-TOF MS for fungal identification are related to sample quality (e.g. quality of biological material such as rigidity or pigmentation of cell walls), sample preparation (e.g. the myriad of sample preparation methodologies that deliver different data sets to different MALDI-TOF MS databases) and the databases themselves (e.g. the 'black-box' commercial databases). This chapter presents an overview and discussion of the use of MALDI-TOF MS for fungal identification. The major known limitations of the technique for fungal taxonomy, and how to overcome these, are also discussed.
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He, Zengyou, Robert Z. Qi, and Weichuan Yu. "Bioinformatic Analysis of Data Generated from MALDI Mass Spectrometry for Biomarker Discovery." In Topics in Current Chemistry, 193–209. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/128_2012_365.

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Wilk, Agata, Marta Gawin, Katarzyna Frątczak, Piotr Widłak, and Krzysztof Fujarewicz. "On Stability of Feature Selection Based on MALDI Mass Spectrometry Imaging Data and Simulated Biopsy." In Advances in Intelligent Systems and Computing, 82–93. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-29885-2_8.

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Campi, Giulia, Giovanna Nicora, Giulia Fiorentino, Andrew Smith, Fulvio Magni, Silvia Garagna, Maurizio Zuccotti, and Riccardo Bellazzi. "A Topological Data Analysis Mapper of the Ovarian Folliculogenesis Based on MALDI Mass Spectrometry Imaging Proteomics." In Artificial Intelligence in Medicine, 43–47. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-77211-6_5.

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Del Prete, Eugenio, Diego d’Esposito, Maria Fiorella Mazzeo, Rosa Anna Siciliano, and Angelo Facchiano. "Comparative Analysis of MALDI-TOF Mass Spectrometric Data in Proteomics: A Case Study." In Computational Intelligence Methods for Bioinformatics and Biostatistics, 154–64. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-44332-4_12.

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López-Fernández, Hugo, Jose E. Araújo, Daniel Glez-Peña, Miguel Reboiro-Jato, Florentino Fdez-Riverola, and José L. Capelo-Martínez. "S2P: A Desktop Application for Fast and Easy Processing of 2D-Gel and MALDI-Based Mass Spectrometry Protein Data." In Advances in Intelligent Systems and Computing, 1–8. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60816-7_1.

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O'Connor, Peter B., Klaus Dreisewerd, Kerstin Strupat, and Franz Hillenkamp. "MALDI Mass Spectrometry Instrumentation." In MALDI MS, 41–104. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.ch2.

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Conference papers on the topic "MALDI mass spectrometry data"

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Oh, Jung Hun, Animesh Nandi, Prem Gurnani, Lynne Knowles, John Schorge, Kevin P. Rosenblatt, and Jean Gao. "Classification of Relapse Ovarian Cancer on MALDI-TOF Mass Spectrometry Data." In 2006 IEEE Symposium on Computational Intelligence and Bioinformatics and Computational Biology. IEEE, 2006. http://dx.doi.org/10.1109/cibcb.2006.331009.

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RESSOM, HABTOM W., RENCY S. VARGHESE, LENKA GOLDMAN, CHRISTOPHER A. LOFFREDO, MOHAMED ABDEL-HAMID, ZUZANA KYSELOVA, YEHIA MECHREF, MILOS NOVOTNY, and RADOSLAV GOLDMAN. "ANALYSIS OF MALDI-TOF MASS SPECTROMETRY DATA FOR DETECTION OF GLYCAN BIOMARKERS." In Proceedings of the Pacific Symposium. WORLD SCIENTIFIC, 2007. http://dx.doi.org/10.1142/9789812776136_0022.

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Wijetunge, Chalini D., Isaam Saeed, Saman K. Halgamuge, Berin Boughton, and Ute Roessner. "Unsupervised learning for exploring MALDI imaging mass spectrometry ‘omics’ data." In 2014 7th International Conference on Information and Automation for Sustainability (ICIAfS). IEEE, 2014. http://dx.doi.org/10.1109/iciafs.2014.7069634.

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Lopez-Cortes, Xaviera A., Fabian Avila-Salas, Cristopher Orellana, and Leonardo S. Santos. "Strategy Based on Data Mining and MALDI-Mass Spectrometry for Control Disease of SRS in Salmo Salar." In 2018 IEEE International Conference on Automation/XXIII Congress of the Chilean Association of Automatic Control (ICA-ACCA). IEEE, 2018. http://dx.doi.org/10.1109/ica-acca.2018.8609735.

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Puapaiboon, Uraiwan, Jaran Jai-nhuknan, and James A. Cowan. "Exonuclease reactivity using MALDI-TOF mass spectrometry." In BiOS 2000 The International Symposium on Biomedical Optics, edited by Darryl J. Bornhop and Kai Licha. SPIE, 2000. http://dx.doi.org/10.1117/12.384247.

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Nelson, Christine M., Lin Zhu, Wei Tang, Lloyd M. Smith, Kevin Crellin, Jamal Berry, and Jack L. Beauchamp. "Fragmentation mechanisms of oligonucleotides in MALDI mass spectrometry." In Photonics West '96, edited by Gerald E. Cohn, Steven A. Soper, and C. H. Winston Chen. SPIE, 1996. http://dx.doi.org/10.1117/12.237612.

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Hunter, Joanna M., Hua Lin, Kristin A. Sannes, and Christopher H. Becker. "Frozen-solution MALDI mass spectrometry studies of DNA." In Photonics West '96, edited by Gerald E. Cohn, Steven A. Soper, and C. H. Winston Chen. SPIE, 1996. http://dx.doi.org/10.1117/12.237627.

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Kim, Hark Kyun, and In-Hoo Kim. "Histology-directed MALDI mass spectrometry for the diagnostic pathology." In SPIE Nanosystems in Engineering + Medicine, edited by Sang H. Choi, Jin-Ho Choy, Uhn Lee, and Vijay K. Varadan. SPIE, 2012. http://dx.doi.org/10.1117/12.1000001.

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Bahrke, Sven, Jon M. Einarsson, Johannes Gislason, Sophie Haebel, Matthias C. Letzel, Jasna Peter-Katalinic, and Martin G. Peter. "SEQUENCE ANALYSIS OF CHITOOLIGOSACCHARIDES BY MALDI PSD MASS SPECTROMETRY." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.544.

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Baluja, M. Quintela, K. Böhme, I. C. Fernández-No, S. Morandi, C. Franco, J. M. Gallardo, J. Barros-Velázquez, and Pilar Calo-Mata. "Rapid differentiation of Enterococcus species by MALDI-TOF mass spectrometry." In MICROBES IN APPLIED RESEARCH - Current Advances and Challenges. WORLD SCIENTIFIC, 2012. http://dx.doi.org/10.1142/9789814405041_0059.

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Reports on the topic "MALDI mass spectrometry data"

1

Wahl, Karen L., Kristin H. Jarman, Nancy B. Valentine, Mark T. Kingsley, Catherine E. Petersen, Sharon C. Wunschel, and Adam J. Saenz. Analysis of Hazardous Biological Materials by MALDI Mass Spectrometry. Office of Scientific and Technical Information (OSTI), December 1999. http://dx.doi.org/10.2172/15002705.

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Samaraweera, Himali, Sun Hee Moon, and Dong U. Ahn. Characterization of Phosvitin Phosphopeptides using MALDI-TOF Mass Spectrometry. Ames (Iowa): Iowa State University, January 2016. http://dx.doi.org/10.31274/ans_air-180814-1389.

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KL Wahl, KH Jarman, NB Valentine, MT Kingsley, CE Petersen, ST Cebula, and AJ Saenz. Analysis of hazardous biological material by MALDI mass spectrometry. Office of Scientific and Technical Information (OSTI), March 2000. http://dx.doi.org/10.2172/752459.

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Feenstra, Adam D. Technological Development of High-Performance MALDI Mass Spectrometry Imaging for the Study of Metabolic Biology. Office of Scientific and Technical Information (OSTI), December 2016. http://dx.doi.org/10.2172/1409181.

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Korte, Andrew R. Development of matrix-assisted laser desorption ionization-mass spectrometry imaging (MALDI-MSI) for plant metabolite analysis. Office of Scientific and Technical Information (OSTI), December 2014. http://dx.doi.org/10.2172/1226566.

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Sriram, Subramaniam. MALDI/Mass Spectrometry of Normal Appearing and Dystrophic Axons in Spinal Cord of Multiple Sclerosis (MS). Fort Belvoir, VA: Defense Technical Information Center, September 2012. http://dx.doi.org/10.21236/ada582356.

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Sriram, Subramaniam. MALDI/Mass Spectrometry of Normal Appearing" and Dystrophic Axons in Spinal Cord of Multiple Sclerosis (MS)". Fort Belvoir, VA: Defense Technical Information Center, September 2013. http://dx.doi.org/10.21236/ada592436.

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Sklarew, Debbie S., and Alexandre V. Mitroshkov. Review of Mass Spectrometry Data from Waste Tank Headspace Analyses. Office of Scientific and Technical Information (OSTI), February 2006. http://dx.doi.org/10.2172/878137.

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Dueas Fadic, Maria Emeilia. Advances in cellular and sub-cellular level localization of lipids and metabolites using two- and three dimensional high-spatial resolution MALDI mass spectrometry imaging. Office of Scientific and Technical Information (OSTI), December 2018. http://dx.doi.org/10.2172/1505180.

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Gutjahr, A., F. Phillips, P. W. Kubik, and D. Elmore. An improved method for statistical analysis of raw accelerator mass spectrometry data. Office of Scientific and Technical Information (OSTI), January 1987. http://dx.doi.org/10.2172/6329593.

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