Relevant bibliographies by topics / MALDI

Academic literature on the topic 'MALDI'

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Published: 4 June 2021
Last updated: 25 May 2024

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Journal articles on the topic "MALDI"

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Osa, Morichika, Maria Cecilia Belo, Zita Dela Merced, Annavi Marie G. Villanueva, Jaira Mauhay, Alyannah Celis, Melissa Catli, et al. "Performance of MALDI–TOF Mass Spectrometry in the Philippines." Tropical Medicine and Infectious Disease 6, no. 3 (June 26, 2021): 112. http://dx.doi.org/10.3390/tropicalmed6030112.

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Identification of the causative pathogen in infectious diseases is important for surveillance and to guide treatment. In low- and middle-income countries (LMIC), conventional culture and identification methods, including biochemical methods, are reference-standard. Biochemical methods can lack sensitivity and specificity and have slow turnaround times, causing delays in definitive therapy. Matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI–TOF MS) is a rapid and accurate diagnostic method. Most studies comparing MALDI–TOF MS and biochemical methods are from high-income countries, with few reports from LMIC with tropical climates. The aim of this study was to assess the performance of MALDI–TOF MS compared to conventional methods in the Philippines. Clinical bacterial or fungal isolates were identified by both MALDI–TOF MS and automated (VITEK2) or manual biochemical methods in the San Lazaro Hospital, Metro Manila, the Philippines. The concordance between MALDI­–TOF MS and automated (VITEK2) or manual biochemical methods was analyzed at the species and genus levels. In total, 3530 bacterial or fungal isolates were analyzed. The concordance rate between MALDI–TOF MS and biochemical methods was 96.2% at the species level and 99.9% at the genus level. Twenty-three isolates could not be identified by MALDI–TOF MS. In this setting, MALDI–TOF MS was accurate compared with biochemical methods, at both the genus and the species level. Additionally, MALDI–TOF MS improved the turnaround time for results. These advantages could lead to improved infection management and infection control in low- and middle-income countries, even though the initial cost is high.
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KAWABATA, Shin-ichirou. "MALDI-TOFMS." Journal of the Japan Society of Colour Material 79, no. 6 (2006): 257–62. http://dx.doi.org/10.4011/shikizai1937.79.257.

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Kajiwara, Hideyuki. "MALDI biotyping." Nippon Shokuhin Kagaku Kogaku Kaishi 65, no. 11 (November 15, 2018): 541. http://dx.doi.org/10.3136/nskkk.65.541.

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Wisztorski, Maxence, Rémi Lemaire, Jonathan Stauber, Sonia Ait Menguellet, Olivia Jardin-Mathé, Robert Day, Michel Salzet, and Isabelle Fournier. "Imagerie MALDI." médecine/sciences 23 (March 2007): 31–38. http://dx.doi.org/10.1051/medsci/2007231s31.

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Chakrabarti, A. "MALDI-TOF." International Journal of Infectious Diseases 45 (April 2016): 26. http://dx.doi.org/10.1016/j.ijid.2016.02.090.

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Chin, Jefferson, Elizabeth Wood, Grace S. Peters, and Dieter M. Drexler. "Acoustic Sample Deposition MALDI-MS (ASD-MALDI-MS)." Journal of Laboratory Automation 21, no. 1 (February 2016): 204–7. http://dx.doi.org/10.1177/2211068215594769.

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Rim, John Hoon, Yangsoon Lee, Sung Kuk Hong, Yongjung Park, MyungSook Kim, Roshan D’Souza, Eun Suk Park, Dongeun Yong, and Kyungwon Lee. "Insufficient Discriminatory Power of Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry Dendrograms to Determine the Clonality of Multi-Drug-ResistantAcinetobacter baumanniiIsolates from an Intensive Care Unit." BioMed Research International 2015 (2015): 1–8. http://dx.doi.org/10.1155/2015/535027.

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While pulsed-field gel electrophoresis (PFGE) is recognized as the gold standard method for clonality analysis, MALDI-TOF MS has recently been spotlighted as an alternative tool for species identification. Herein, we compared the dendrograms of multi-drug-resistant (MDR)Acinetobacter baumanniiisolates by using MALDI-TOF MS with those by using PFGE. We used direct colony and protein extraction methods for MALDI-TOF MS dendrograms. The isolates with identical PFGE patterns were grouped into different branches in MALDI-TOF MS dendrograms. Among the isolates that were classified as very close isolates in MALDI-TOF MS dendrogram, PFGE band patterns visually showed complete differences. We numeralized similarity among isolates by measuring distance levels. The Spearman rank correlation coefficient values were 0.449 and 0.297 between MALDI-TOF MS dendrogram using direct colony and protein extraction method versus PFGE, respectively. This study is the first paper focusing solely on the dendrogram function of MALDI-TOF MS compared with PFGE. Although MALDI-TOF MS is a promising tool to identify species in a rapid manner, our results showed that MALDI-TOF MS dendrograms could not substitute PFGE for MDRAcinetobacter baumanniiclonality analysis.
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NIRASAWA, TAKASHI. "MALDI-TOF-MS." Kagaku To Seibutsu 34, no. 4 (1996): 255–59. http://dx.doi.org/10.1271/kagakutoseibutsu1962.34.255.

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Kriegsmann, J., R. Casadonte, F. Zweynert, M. Kriegsmann, M. Otto, and S. Deininger. "MALDI-TOF-Bildgebung." Zeitschrift für Rheumatologie 72, no. 7 (August 16, 2013): 724–28. http://dx.doi.org/10.1007/s00393-013-1239-1.

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Chen, Xin-Fei, Xin Hou, Meng Xiao, Li Zhang, Jing-Wei Cheng, Meng-Lan Zhou, Jing-Jing Huang, Jing-Jia Zhang, Ying-Chun Xu, and Po-Ren Hsueh. "Matrix-Assisted Laser Desorption/Ionization Time of Flight Mass Spectrometry (MALDI-TOF MS) Analysis for the Identification of Pathogenic Microorganisms: A Review." Microorganisms 9, no. 7 (July 19, 2021): 1536. http://dx.doi.org/10.3390/microorganisms9071536.

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Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) has been used in the field of clinical microbiology since 2010. Compared with the traditional technique of biochemical identification, MALDI-TOF MS has many advantages, including convenience, speed, accuracy, and low cost. The accuracy and speed of identification using MALDI-TOF MS have been increasing with the development of sample preparation, database enrichment, and algorithm optimization. MALDI-TOF MS has shown promising results in identifying cultured colonies and rapidly detecting samples. MALDI-TOF MS has critical research applications for the rapid detection of highly virulent and drug-resistant pathogens. Here we present a scientific review that evaluates the performance of MALDI-TOF MS in identifying clinical pathogenic microorganisms. MALDI-TOF MS is a promising tool in identifying clinical microorganisms, although some aspects still require improvement.
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Dissertations / Theses on the topic "MALDI"

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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
Made available in DSpace on 2018-08-25T05:33:49Z (GMT). No. of bitstreams: 1 Rodrigues_LiviaRiberti_M.pdf: 1203619 bytes, checksum: a17baf81fa013532bd6c9d451b2336f2 (MD5) Previous issue date: 2014
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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Lai-Rowcroft, Lindsay Ling Gi. "Novel surfaces for MALDI-MS." Thesis, University of Manchester, 2013. https://www.research.manchester.ac.uk/portal/en/theses/novel-surfaces-for-maldims(331dd97a-881e-4ed0-908f-d5947f3ebeba).html.

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Matrix assisted laser desorption/ionisation mass spectrometry (MALDI-MS) for small molecule analysis has been plagued with inherent problems associated with matrix interference. The matrix plays an important role in MALDI-MS where it has the ability to absorb UV energy from the laser employed and transfer it to the analyte, acts as a proton donor and protecting the analytes from being obliterated. For decades, research has been performed to eradicate matrix interference by matrix avoidance, finding alternative matrices, suppression through sample preparation methods and via chemical modification.In this investigation a number of the above mentioned approaches have been undertaken. First, a mesoporous silica powder, SBA-16, functionalised with a phenyl group to absorb UV from the MALDI-MS laser gave unfruitful results due to inhomogeneous dispersion of the SBA-16 powder. Therefore the same material was prepared but as a thin film and a homogeneously coated surface was generated with the phenyl group incorporated into the silica and this was compared with a conventional matrix, 2,5-dihydroxybenzoic acid (DHB). This was by far the most sensitive method which was accurate, with little background noise and importantly for small molecule analysis clear of matrix interference. Other surface systems were also tested such as graphene on copper and silver on copper, but the functionalised SBA-16 thin film remained the best. Graphite and 2B pencil were also investigated for MALDI-MS but were compared with conventional matrices (DHB and α-cyano-4-hydroxycinnamic acid (CHCA)) in a functional genomics study. The ability of all methods to find subtle phenotypic differences in various yeast strains was assessed with the help of multivariate data analysis (MVDA). Although DHB came out best, 2B pencil produce notably good separations that correlated nicely with the different genotypes. Therefore in addition to conventional matrices, 2B pencil should be considered for functional genomic studies when MALDI-MS is used as it is such a rapid and inexpensive method. Finally, chemical modifications were performed on amino acids where picolinic acid was used to attach a chromophore to the compounds, therefore, allowing UV absorption from the laser. Upon attaching the picolinate UV absorbing group, the amino acid compounds were detected LC-MS at an increased intensity of 10 to 100-fold. Moreover, enhanced separation in LC-MS was also observed.This project has successfully investigated alternative approaches to matrix-free MALDI-MS analysis. Functionalised SBA-16 thin films were by far the best method and this novel surface for MALDI-MS has the potential to transform small molecule analysis.
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Tandina, Fatalmoudou. "Mise au point et application de technologies innovantes pour l'étude des moustiques, de leur préférence trophique et de leur microbiote." Thesis, Aix-Marseille, 2018. http://www.theses.fr/2018AIXM0277/document.

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Les moustiques sont les principaux vecteurs incriminés dans la transmission d’agents pathogènes à l’homme. L’identification précise des espèces de moustiques est importante pour distinguer les espèces vectrices des non vectrices. La détermination de l’origine du repas sanguin des moustiques vecteurs est indispensable dans la compréhension du comportement des espèces vectrices. Nous avons mise à jour la littérature actuelle sur la faune Culicidienne du Mali. Ainsi, nous avons listé 106 espèces de moustiques actuellement enregistrée au Mali dont 28 Anophelinae et 78 Culicinae. Nous avons ensuite évalué l’efficacité du MALDI-TOF MS à identifier des moustiques collectés au Mali et déterminer leur source de repas sanguin. Nous avons confirmé la robustesse du MALDI-TOF MS à identifier un grand nombre de sang d’animaux. Nous avons artificiellement gorgé des femelles de An. gambiae et An. coluzzii sur différents types de sang d’animaux. Nous avons obtenu 100% d'identification correcte du repas de sang pour les spécimens collectés 1h à 24h après le gorgement. Ensuite nous avons expérimentalement gorgés An. gambiae, An. coluzzii et Ae. albopictus sur des repas de sang successif et mixte par MALDI-TOF MS. Nos résultats révèlent que le MALDI-TOF MS est tout à fait capable d’identifier le repas mixte. Mais en ce qui concerne le repas successif seul le dernier repas de sang est identifié. Enfin nous avons utilisé la culturomique et le MALDI-TOF pour l’étude du microbiote digestif de moustiques collectés sur le terrain au Mali et à Marseille. Cette approche a révélé une grande diversité du microbiote digestif des moustiques An. gambiae, Ae. albopictus et Cx. quinquefasciatus
Mosquitoes are the main vectors involved in the transmission of pathogens to humans. Accurate identification of mosquito species is crucial to distinguish between vector and non-vector species. The mosquito blood meal determination is fundamental in understanding the behavior of vector species. Thus, we have listed 106 mosquito species currently recorded in Mali, including 28 Anophelinae and 78 Culicinae. Then, we evaluated the effectiveness of MALDI-TOF MS for identified mosquitoes collected in Mali and to determine their blood meal source. The results obtained show the ability of MALDI-TOF MS to identify mosquitoes collected in Mali and their source of blood meal. Subsequently, we were able to confirm the robustness of MALDI-TOF MS to identify other animal blood samples. We artificially engorged Anopheles gambiae and Anopheles coluzzii on eight animal bloods samples. We obtained 100% correct identification of the blood source for samples taken 1 to 24 hours after feeding. Then, we experimentally engorged An. gambiae, An. coluzzii and Ae. albopictus on successive and mixed blood meals using MALDI-TOF MS. The results revealed that MALDI-TOF MS is able to identify mixed blood meals. In addition we used MALDI-TOF and culturomics for the microbiota study of the mosquito collected in the field, notably in Marseille and Mali. The culturomics approach revealed a great diversity of the digestive microbiota of the An. gambiae, Ae. albopictus and Cx. quinquefasciatus mosquitoes
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Krüger, Ralf. "Untersuchungen zum Einbau von Analytionen in MALDI-Matrizes sowie zur Ionisation und Adduktbildung in der MALDI-Massenspektrometrie." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=969681682.

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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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Collazo, Verena. "Reverse Sanger-Sequenzierung mittels MALDI-TOF-Massenspektrometrie." [S.l.] : [s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=964226871.

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Enebro, Jonas. "Characterization of carboxymethyl cellulose by MALDI-TOFMS /." Stockholm : [Fiber och polymerteknologi, Kungliga Tekniska högskolan], 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-4376.

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Leander, Ellinor. "Artidentifiering av mögelsvamp med MALDI-TOF MS." Thesis, Linnéuniversitetet, Institutionen för kemi och biomedicin (KOB), 2018. http://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-80166.

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Snabb och korrekt artidentifiering är avgörande för effektiv behandling av svampinfektioner, särskilt bland immunsupprimerade patienter. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) används rutinmässigt på kliniska laboratorier för identifiering av karaktäristiska proteinmönster hos bakterier och jästsvampar genom tolkning av proteinspektra i en masspektradatabas för korrekt artidentifiering. Mögelsvamparnas hårda cellvägg och heterogena växtsätt med varierande proteinuttryck beroende på mognadsstadie, försvårar identifiering med MALDI-TOF MS. Metodens tänkbara fördelar mot traditionella metoden mikroskopering är förkortade svarstider, säkrare artidentifiering av fler arter och mindre beroende av subjektiv morfologisk bedömning. Studiens syfte var att undersöka om MALDI-TOF MS kunde anpassas och användas för identifieringen av mögelsvamp i klinisk rutindiagnostik. Fyra referensstammar (Aspergillus niger, A. fumigatus, A.terreus, A.flavus) och ett kliniskt isolat (A.terreus) undersöktes. Preparationsmetoderna (I) fullständig myrsyraextraktion, (II) direktapplicering och (III) suspension i destillerat vatten användes för analys av sporer och frontmycel hos yngre och äldre mögelkulturer. Två olika masspektradatabaser för artidentifiering jämfördes; rutindatabasen BDAL och den specialiserade mögeldatabasen Filamentous Fungi Library. Även plocktekniken av mögelmaterial inför analys med MALDI-TOF MS utvärderades. Vid vissa tillfällen förbättrades artidentifieringen efter extraktion av mögelkulturerna, medan i andra fall var direktapplicering fullt tillräcklig. Mögelmaterial med mycket sporer tenderade ge något fler artidentifieringar i BDAL oavsett kulturernas ålder.  Filamentous Fungi Library tenderade i vissa fall ge bättre resultat jämfört med BDAL för yngre kulturer. Fler studier krävs för att utvärdera och optimera MALDI-TOF MS som metod för artidentifiering av mögelsvamp.
Rapid and accurate species identification is crucial for successful treatment of fungal infections, especially among immunosuppressed patients. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) is used routinely at clinical laboratories to identify characteristic protein patterns of bacteria and yeast by the interpretation of protein spectra in a database for accurate species identification. The hard cell wall of the mold and the heterogeneous growth with varying protein expression due to maturation, complicates identification with MALDI-TOF MS. The potential benefits of this method compared to microscopy as traditional method are shortened turn-around times, safer species identification of more species that is independent on subjective morphological assessment. The purpose of the study was to investigate whether MALDI-TOF MS could be adapted and used for the identification of molds in clinical routine diagnostics. Four reference strains (Aspergillus niger, A.fumigatus, A.terreus, A.flavus) and a clinical isolate (A.terreus) were examined. The preparation methods (I) complete formic acid extraction, (II) direct application and (III) suspension in distilled water were used for analysis of spores and frontmycelium from younger and older mold cultures. Two different masspektradatabases for species identification were compared; routine database BDAL and the specialized mold database, Filamentous Fungi Library. Also the collecting technique of mold prior to analysis with MALDI-TOF MS was evaluated. Sometimes, the species identification improved after extraction of mold cultures, while in other cases direct application was sufficient. Cultures with a lot of spores tended to give slightly more species identifications in BDAL regardless of the age of cultures. Filamentous Fungi Library, in some cases, tended to improve the performance compared to BDAL for younger cultures. More studies are required to evaluate and optimize MALDI-TOF MS as a method of mold identification.
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Stauber, Jonathan. "Imagerie MALDI : nouveaux développements et applications cliniques." Lille 1, 2007. https://pepite-depot.univ-lille.fr/LIBRE/Th_Num/2007/50376-2007-379.pdf.

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Les avancées de la biologie moléculaire se sont également réalisées avec l’évolution des techniques d’imagerie dans les domaines de la génomique. La transcriptomique et plus récemment de la protéomique grâce ù l'essor d'un outil essentiel, la spectrométrie de masse. Cette technique a trouvé sa place pour générer des profils protéiques caractéristiques de l'état physiologique de la cellule, de fluides complexes tels que le sang ou les urines. Elle apparaît aujourd'hui comme un outil indissociable de la recherche en biologie et en médecine. Les nouveaux développements tendent à conduire la spectrométrie de masse vers l’imagerie moléculaire pour l'identification de pathologies, pour la distribution de médicament au sein d’un animal. Ou pour une utilisation en diagnostique et en pronostique. Cette technologie récente, demande qu'à être développée, améliorée, standardisée. C’est dans ce cadre que ma thèse intitulée « Imagerie MALDI nouveaux développements et applications cliniques » a été orientée. Les différents résultats ont permis de développer I’imagerie spécifique moléculaire MALDI, I’imagerie moléculaire MALDI de tissus fixés et paraffinés avec des applications à la fois dans le cadre de la maladie de Parkinson et le cancer de l’ovaire. L’évolution en filagramme de cette technologie d'imagerie moléculaire semble devoir se réaliser de paire avec les techniques d’imagerie non invasive pour devenir une nouvelle technologie en clinique
The recent innovations in molecular biology were realized with the evolution of the imaging techniques in the field of Genomics, Transcriptomics, and recently in Proteomics with an essential tool, the mass spectrometry. This imaging technique create characteristic protein profiles of the cellular states, and appears today as an undissociable tool for research in biology and medicine. The last developments look to emerge the mass spectrometry to a molecular imaging to identify pathologies, to observe the drugs distributions in tissues, or the diseases diagnosis or prognosis. This unique and recent technology should be developed, improved, and standardized. It's in this point of view the my PhD training named MALDI imaging new developments and clinical applications was defined. The different results obtained during my PhD were permits to create a concept of Specific Imaging Mass Spectrometry, to develop Molecular MALDI imaging of frozen and FFPE tissues with many applications in the research of specific biomarkers in Parkinson disease and ovarian cancer. The evolution of this unique molecular imaging technique should be in the next years a complementary method of others in vivo imaging technique
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Jacksén, Johan. "Improved techniques for CE-MALDI-MS off-line coupling and MALDI-MS analysis of primarily hydrophobic proteins and peptides." Licentiate thesis, KTH, Chemistry, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-4599.

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Due to the hydrophobic nature of integral membrane proteins (IMP) they give rise to several difficulties concerning handling and analysis, which is not the case for the most water soluble proteins. New analysis methods are needed, where the insolubility problems of the hydrophobic proteins due to aggregation and adhesion are tackled. Those problems also affect digestion performance and equipment compatibility for the analysis.

Protocols for analysis and separation specified for IMP are presented in Paper I and III.

The instrumentation used in this work was capillary electrophoresis (CE) and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). Both instruments are suitable for peptide/proteins analysis.

In Paper I, protocols for a CE separation of bacteriorhodopsin (BR) peptides as model IMP peptides are established. Also, a partially automated manufacturing procedure of a concentration MALDI-target is presented, suitable for fractions from CE. The MS analysis detected 9 out of 10 cyanogen bromide (CNBr) digested BR peptides. A novel technique for the off-line integration of CE to MALDI-MS using a closed-open-closed system is presented in Paper II, where the open part is a microcanal functioning as a MALDI target window. Investigation of the microcanal electro-osmotic flow (EOF) properties and band broadening characteristics was performed. A protein separation was obtained and detected with MALDI-MS analysis in the microcanal. Different protein digestion methods were evaluated using BR in Paper III through MALDI-MS. Several digestion methods as well as MS media were investigated alongside different MALDI matrices. For example, matrices as the hydrophobic 2,6-dihydroxyacetophenone (DHAP) and 2-Hydroxy-3-methoxybenzoic acid (2H3MBA) or 2-Hydroxy-5-methoxybenzoic acid (2H5MBA) mixed with DHB, appeared to be promising matrices for analysis of BR.


Med anledning av integrala membranproteiners (IMP) hydrofoba egenskaper uppstår flera svårigheter vid hantering och analys av IMP, vilket inte är fallet för vattenlösliga proteiner. Nya analysmetoder krävs, som löser löslighetsproblemen för de hydrofoba proteinerna som tex flockning och adsorbtion. Dessa problem påverkar även klyvningsgrad och kompatibilitet med analysutrustningen.

I Artikel I och Artikel III presenteras protokoll för analys och separation specifikt för IMP. Instrumenteringen som har använts i detta arbete är kapillärelektrofores (CE) och matris-assisterad laserdesorptions-joniserings-masspektrometri (MALDI-MS). Båda instrumenten är lämpade för peptid/protein analyser.

I Artikel I, presenteras protokoll för en CE separation av peptider från bacteriorhodopsin (BR), som användes som modellpeptider för IMP. En delvis automatiserat tillverkningsprocedur för en koncentrerande MALDI-platta, som är anpassad för CE fraktionerna beskrivs också. MS-analysen detekterade 9 av 10 BR-peptider från cyanobromid-klyvning (CNBr). En ny teknik för off line-integrering av CE till MALDI-MS genom ett slutet-öppet-slutet system presenteras i Artikel II, där den öppna delen är en mikrokanal som fungerar som detektionsfönster i MALDI. Undersökning av mikrokanalens egenskaper som tex det elektroosmotiska flödet (EOF) och bandbreddningen utvärderades. En proteinseparation genomfördes och detekterades med MALDI–MS i mikrokanalen. Olika proteinklyvningsmetoder för BR undersöktes i Artikel III med MALDI-MS. Flera proteinklyvningsmetoder samt MS-medier utvärderades tillsammans med olika MALDI-matriser. Den hydrofoba matrisen 2,6-dihydroxyacetophenone (DHAP) och 2-Hydroxy-3-methoxybenzoic acid (2H3MBA) eller 2-Hydroxy-5-methoxybenzoic acid (2H5MBA) blandade med DHB, visade sig exempelvis vara lovande matriser för BR-analyser.

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Books on the topic "MALDI"

1

Hillenkamp, Franz, and Jasna Peter-Katalinic, eds. MALDI MS. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.

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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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Cai, Zongwei, and Shuying Liu, eds. Applications of MALDI-TOF Spectroscopy. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-35665-0.

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Hosseini, Samira, and Sergio O. Martinez-Chapa. Fundamentals of MALDI-ToF-MS Analysis. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-2356-9.

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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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Liang, Li, ed. MALDI mass spectrometry for synthetic polymers analysis. Hoboken: Wiley, 2010.

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Shah, Haroun N., and Saheer E. Gharbia, eds. MALDI-TOF and Tandem MS for Clinical Microbiology. Chichester, UK: John Wiley & Sons, Ltd, 2017. http://dx.doi.org/10.1002/9781118960226.

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Book chapters on the topic "MALDI"

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Morgan, Michael M., MacDonald J. Christie, Thomas Steckler, Ben J. Harrison, Christos Pantelis, Christof Baltes, Thomas Mueggler, et al. "MALDI." In Encyclopedia of Psychopharmacology, 749. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_4339.

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Hillenkamp, Franz, Thorsten W. Jaskolla, and Michael Karas. "The MALDI Process and Method." In MALDI MS, 1–40. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.ch1.

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Pham, Thang V., and Connie R. Jimenez. "Computational Analysis of High-Throughput MALDI-TOF-MS-Based Peptide Profiling." In MALDI MS, 411–30. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.ch10.

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Kostrzewa, Markus. "Biotyping of Microorganisms." In MALDI MS, 431–43. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.ch11.

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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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Hjernø, Karin, and Ole N. Jensen. "MALDI-MS in Protein Chemistry and Proteomics." In MALDI MS, 105–31. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.ch3.

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Spengler, Bernhard. "MALDI-Mass Spectrometry Imaging." In MALDI MS, 133–67. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.ch4.

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Berkenkamp, Stefan, Dirk van den Boom, and Daniele Fabris. "Analysis of Nucleic Acids, and Practical Implementations in Genomics and Genetics." In MALDI MS, 169–238. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.ch5.

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Perreault, Hélène, Erika Lattová, Dijana Šagi, and Jasna Peter-Katalinic. "MALDI-MS of Glycans and Glycoconjugates." In MALDI MS, 239–71. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.ch6.

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Schiller, Jürgen, and Beate Fuchs. "Lipids." In MALDI MS, 273–311. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.ch7.

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Conference papers on the topic "MALDI"

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Murray, Kermit K., Michelle D. Beeson, and David H. Russell. "Laser Ionization of Biomolecules in Solution." In Laser Applications to Chemical Analysis. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/laca.1994.tha.5.

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Many powerful laser based methods are unavailable for the analysis of molecules in solution. Techniques for the analysis of liquids are particularly important for the study of biomolecules, whose natural environment is a water solution. Mass spectrometry is a powerful analytical technique, but liquids and mass spectrometers are fundamentally incompatible. We have developed a technique for laser ionization of biomolecules in solution by applying matrix-assisted laser desorption ionization (MALDI) to liquid aerosols. In the typical MALDI experiment, the analyte biomolecule is deposited from solution onto a metal surface with a 100 to 50,000 molar excess of a suitable matrix, usually a UV absorbing organic acid.1 The solvents are allowed to evaporate and the sample is inserted into the source region of a mass spectrometer. Light from a pulsed laser is absorbed by the matrix causing both ablation of the surface and ionization of the intact biomolecule. In the aerosol MALDI experiment, 2,3 the analyte biomolecule is dissolved in a methanol solution with an ultraviolet absorbing matrix. The aerosol is sprayed into vacuum, desolvated, and ionized by pulsed UV laser radiation. The ions are mass separated in a time-of-flight (TOF) mass spectrometer. Aerosol MALDI mass spectra have been obtained for a variety of peptides and proteins with molecular weights as large as 80,000. We have used aerosol MALDI as a liquid chromatography detection method4 (LC/MS) and as a probe of aerosol and cluster chemistry.5 This paper gives a general description of aerosol MALDI and discusses some recent results for peptide and protein ionization.
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Kinsel, Gary R., Kent Gillig, Ricky Edmondson, and David H. Russell. "Fundamental Investigations of the Mechanism of Laser Desorption and Ionization in Matrix Assisted Laser Desorption / Ionization." In Laser Applications to Chemical Analysis. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/laca.1994.thb.1.

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The recent development of Matrix Assisted Laser Desorption / Ionization (MALDI) has sparked a revolution in the field of high molecular weight mass spectrometry.1 Time-of-flight (TOF) mass spectra of proteins weighing up to 300,000 Da are now routinely produced and this achievement has fostered a variety of bioanalytical applications which were previously unapproachable using conventional mass spectrometric techniques. These successful applications have burgeoned in spite of a poor understanding of the mechanism of analyte desorption and ionization under MALDI conditions. An improved understanding of the MALDI mechanism should aid in overcoming a number of limitations of the current state-of-the-art and forms the motivation for the work described.
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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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Ding, Li, Eizoh Kawatoh, Koichi Tanaka, Alan J. Smith, and Sumio Kumashiro. "High-efficiency MALDI-QIT-ToF mass spectrometer." In SPIE's International Symposium on Optical Science, Engineering, and Instrumentation, edited by Eric Munro. SPIE, 1999. http://dx.doi.org/10.1117/12.370125.

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SILVA, J. A. DA, L. NAGY, and L. G. AGUIAR. "CARACTERIZAÇÃO DE POLIÓIS INDUSTRIAIS POR MALDI-TOF." In Congresso Brasileiro de Engenharia Química em Iniciação Científica. São Paulo: Editora Blucher, 2017. http://dx.doi.org/10.5151/chemeng-cobeqic2017-312.

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NAOMI TAMI, MARIANA, RODRIGO RAMOS CATHARINO, and DIOGO N. OLIVEIRA. "Avaliação de corantes alimentares por MALDI-Imaging." In XXIV Congresso de Iniciação Científica da UNICAMP - 2016. Campinas - SP, Brazil: Galoa, 2016. http://dx.doi.org/10.19146/pibic-2016-50969.

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Jabbour, Rabih, Ashish Tripathi, Erik D. Emmons, Phillip G. Wilcox, Jason A. Guicheteau, Gregory Peterson, and Jared Decoste. "Advancements in MOF characterization for enhanced MALDI sensing." In Chemical, Biological, Radiological, Nuclear, and Explosives (CBRNE) Sensing XIX, edited by Augustus W. Fountain, Jason A. Guicheteau, and Chris R. Howle. SPIE, 2018. http://dx.doi.org/10.1117/12.2303501.

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Kolibal, J., and D. Howard. "Novel Algorithm for MALDI-TOF Baseline Drift Removal." In 2005 IEEE Symposium on Computational Intelligence in Bioinformatics and Computational Biology. IEEE, 2005. http://dx.doi.org/10.1109/cibcb.2005.1594946.

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Gerhard, Marc, Soren-Oliver Deininger, and Frank-Michael Schleif. "Statistical Classification and Visualization of MALDI-Imaging Data." In Twentieth IEEE International Symposium on Computer-Based Medical Systems. IEEE, 2007. http://dx.doi.org/10.1109/cbms.2007.99.

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Vadlamudi, Ayyappa, Shao-Hui Chuang, Xiaoyan Sun, Lisa Cazares, Julius Nyalwidhe, Dean Troyer, O. John Semmes, Jiang Li, and Frederic D. McKenzie. "Prostate cancer region prediction using MALDI mass spectra." In SPIE Medical Imaging, edited by Nico Karssemeijer and Ronald M. Summers. SPIE, 2010. http://dx.doi.org/10.1117/12.844494.

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Reports on the topic "MALDI"

1

Waite, J. H. Direct Analysis of Marine Interfaces: Mussels and MALDI. Fort Belvoir, VA: Defense Technical Information Center, January 2002. http://dx.doi.org/10.21236/ada397968.

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Gillman, Amelie R. Correlating MALDI and MRI Biomarkers of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2010. http://dx.doi.org/10.21236/ada540714.

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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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Puretzky, A. A., and D. B. Geohegan. LIF-imaging and gas-phase diagnostics of laser desorbed MALDI-matrix plumes. Office of Scientific and Technical Information (OSTI), July 1997. http://dx.doi.org/10.2172/563317.

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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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