Relevant bibliographies by topics / MALDI-MS/MS

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'MALDI-MS/MS'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "MALDI-MS/MS"

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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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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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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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Pashkova, Anna, Eugene Moskovets, and Barry L. Karger. "Coumarin Tags for Improved Analysis of Peptides by MALDI-TOF MS and MS/MS. 1. Enhancement in MALDI MS Signal Intensities." Analytical Chemistry 76, no. 15 (August 2004): 4550–57. http://dx.doi.org/10.1021/ac049638+.

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Yang, Hyo-Jik, Kyu Hwan Park, Seongjae Shin, Ji-hye Lee, Sehwan Park, Hyun Sik Kim, and Jeongkwon Kim. "Characterization of heme ions using MALDI-TOF MS and MALDI FT-ICR MS." International Journal of Mass Spectrometry 343-344 (June 2013): 37–44. http://dx.doi.org/10.1016/j.ijms.2013.03.014.

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Rappsilber, Juri, Marc Moniatte, Michael L. Nielsen, Alexandre V. Podtelejnikov, and Matthias Mann. "Experiences and perspectives of MALDI MS and MS/MS in proteomic research." International Journal of Mass Spectrometry 226, no. 1 (March 2003): 223–37. http://dx.doi.org/10.1016/s1387-3806(02)00976-4.

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Zhang, Nan, Nan Li, and Liang Li. "Liquid Chromatography MALDI MS/MS for Membrane Proteome Analysis." Journal of Proteome Research 3, no. 4 (August 2004): 719–27. http://dx.doi.org/10.1021/pr034116g.

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Schiller, Jurgen. "MALDI-TOF MS in lipidomics." Frontiers in Bioscience 12, no. 1 (2007): 2568. http://dx.doi.org/10.2741/2255.

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Haff, L., P. Juhasz, S. Martin, M. Roskey, I. Smirnov, W. Stanick, M. Vestal, and K. Waddell. "Oligonucleotide analysis by MALDI-MS." Analusis 26, no. 10 (December 1998): 26–30. http://dx.doi.org/10.1051/analusis:1998260026.

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Schuerenberg, Martin, Christine Luebbert, Holger Eickhoff, Markus Kalkum, Hans Lehrach, and Eckhard Nordhoff. "Prestructured MALDI-MS Sample Supports." Analytical Chemistry 72, no. 15 (August 2000): 3436–42. http://dx.doi.org/10.1021/ac000092a.

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Dissertations / Theses on the topic "MALDI-MS/MS"

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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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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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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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SQUEO, VALERIA. "Alterazioni del peptidoma serico di pazienti con tumore renale valutate tramite "label-free" (nLC-ESI-MS/MS) e "peptide profiling" (MALDI-MS/MS)." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2013. http://hdl.handle.net/10281/43783.

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Il progetto di questa ricerca è stato rivolto allo studio e alla caratterizzazione del peptidoma serico di soggetti sani e pazienti con carcinoma renale, così come alla diagnosi differenziale delle forme di tumore renale maligno da lesioni benigne. A questo proposito sono stati purificati, mediante tecnica ClinProt che utilizza microparticelle magnetiche funzionalizzate, il siero di un ampio numero di pazienti affetti da ccRCC e soggetti controllo, estendendo lo studio anche a pazienti affetti da non-ccRCC. Le analisi di profiling peptidico sono state condotte mediante SM MALDI-TOF seguita da elaborazione dei profili spettrali per all’individuazione di clusters con potenziale diagnostico. Inoltre si è cercato di identificare proteine/peptidi con alterata espressione serica. A questo scopo sono state effettuate analisi mediante tecnologia nLC-ESI MS/MS e MALDI-TOF MS/MS. I risultati del "profiling" tramite MALDI-TOF sono stati verificati utilizzando un approccio proteomico diverso basato su una quantificazione relativa label-free in nLC-ESI MS/MS.
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Kempka, Martin. "Improved mass accuracy in MALDI-TOF-MS analysis." Licentiate thesis, Stockholm : Division of Analytical Chemistry, Royal Institute of Technology, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-313.

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Kriegsmann, Mark. "MALDI MS Imaging zur Untersuchung von synovialem Gewebe." Doctoral thesis, Universitätsbibliothek Leipzig, 2013. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-118897.

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Halgunset, Anders. "Typing av Legionella pneumophila med MALDI-TOF MS." Thesis, Norges teknisk-naturvitenskapelige universitet, Institutt for bioteknologi, 2012. http://urn.kb.se/resolve?urn=urn:nbn:no:ntnu:diva-24697.

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Legionella pneumophila er fakultativ intracellulære bakterier som lever naturlig i akvatiske habitater. De kan replikere i makrofager og protozoer, bli overført til mennesker gjennom areosoler og føre til smitte. Ved eventuelle utbrudd er det viktig å kunne identifisere kilden, noe som i dag bli gjort ved å typebestemme L. pneumophila med sekvensbasert typing (SBT). Samtidig har matrix-assisted laser desorption/ionization ? time-of-flight (MALDI?TOF) mass spectrometry (MS) vist seg å kunne brukes til rask og effektiv identifisering av en rekke mikroorganismer på artsnivå, deriblant Legionella. Hos enkelte andre mikroorganismer har MALDI?TOF MS også vist å kunne skille mellom underarter. MALDI?TOF MS ble i denne oppgaven benyttet for å undersøke om det var mulig å skille L. pneumophila fra hverandre på stammenivå ved hjelp av MALDI Biotyper 3.0 programvare. Standardprotokollen anbefalt av Bruker Daltonics for proteinekstraksjon fra mikroorganismer ble tilpasset/optimalisert for bruk på L. pneumophila, slik at reproduserbare massespektre ble oppnådd. Evalueringen viste at proteinekstraksjon fra ca 2 µl biologisk materiale med 10 µl acetonnitrill og 10 µl maursyre, ga best scoreverdi opp mot Bruker Daltonics referansebibliotek. Den optimale temperaturen og varigheten for dyrkning ble vist å være henholdsvis 37 ˚C og 48 ± 2 timer. Det ble vist at lagring av skåler/kolonier med L. pneumophila ved 37 ˚C førte til forandringer i massespektrene, mens lagring ved 20 ˚C ikke medførte slike forandringer og at stabile massespektre ble oppnådd etter seks dagers lagring.Det ble bygget opp et referansebibliotek i MALDI Biotyper 3.0 bestående av referansespekter/referansetopplister (MSP) fra til sammen 48 Legionella spp. hvorav 41 var L. pneumophila -isolater. Med referansebiblioteket ble det vist at MSP (dannet ved standard innstillinger) for mange L. pneumophila var for like hverandre til å gi identifisering mot egne MSP. En klyngeanalyse ble brukt i sammenligning av L. pneumophila mellom SBT og MSP fra referansebiblioteket dannet med MALDI?TOF MS. Sammenligningen viste at diversiteten i proteinsammensetningen hos L. pneumophila, representert som MSP, ikke ga samme oppløselighet som gjennom sekvensvariasjonene fra genene i SBT -analysen.
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Trim, Paul James. "MALDI-MS imaging for direct drug distribution analysis." Thesis, Sheffield Hallam University, 2009. http://shura.shu.ac.uk/20455/.

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MALDI Imaging has gained huge interest in the past few years with an ever increasing population of specialists choosing to investigate samples using MALDI imaging, including growing interest and financial backing from pharma and contract research organisations. Presented within this thesis is the development and application of MALDI imaging techniques for a variety of analytical problems. The use of various software packages have been employed in the interpretation of the data acquired from MALDI experiments including, the use of statistical analysis for the identification of ion of interest from 6 distinct brain regions and also for the identification of ions of interest associated with small molecule tumour markers. The advantages of MALDI-IMS-MSI as a further separation stage within MALDI-MSI have been shown. Demonstrated is a method for MALDI-IMS-MS imaging of endogenous lipids in healthy tissue and tumours, also demonstrated is the application of MALDI-IMS-MS to xenobiotic distribution studies, it has been clearly shown that ion mobility separation within MALDI-MSI experiments can improve the analysis of xenobiotics by removing any interfering ions. With instrumentation development for MALDI a high repetition rate Nd:YVO4 laser has been assessed as a possible method for decreasing acquisition time.
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Sun, Zhen. "Studies of Atmospheric Pressure Visible-Wavelength MALDI-MS." University of Toledo / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1333747638.

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Sorensen, Christina M. "ESI-MS and MALDI-TOF-MS for the characterization and analysis of metallo-oligomers and proteins." Laramie, Wyo. : University of Wyoming, 2005. http://proquest.umi.com/pqdweb?did=1031044031&sid=4&Fmt=2&clientId=18949&RQT=309&VName=PQD.

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Books on the topic "MALDI-MS/MS"

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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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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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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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F, Hillenkamp, and Peter-Katalinić Jasna, eds. MALDI MS: A practical guide to instrumentation, methods and applications. Weinheim: Wiley-VCH, 2007.

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

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Hillenkamp, Franz, and Jasna Peter‐Katalinić, eds. MALDI MS. Wiley, 2007. http://dx.doi.org/10.1002/9783527610464.

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Shah, Haroun N., and Saheer E. Gharbia. MALDI-TOF and Tandem MS for Clinical Microbiology. Wiley & Sons, Incorporated, John, 2017.

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Shah, Haroun N., and Saheer E. Gharbia. MALDI-TOF and Tandem MS for Clinical Microbiology. Wiley & Sons, Limited, John, 2017.

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Shah, Haroun N., and Saheer E. Gharbia. MALDI-TOF and Tandem MS for Clinical Microbiology. Wiley & Sons, Incorporated, John, 2017.

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(Editor), Franz Hillenkamp, and Jasna Peter-Katalinic (Editor), eds. MALDI MS: A Practical Guide to Instrumentation, Methods and Applications. Wiley-VCH, 2007.

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Book chapters on the topic "MALDI-MS/MS"

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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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Li, Liang. "MALDI-MS for Polymer Characterization." In MALDI MS, 313–65. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.ch8.

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Conference papers on the topic "MALDI-MS/MS"

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Lopez-Cortes, Xaviera A., Cesar A. Astudillo, Camila Gonzalez, and Sebastian Maldonado. "Semi-supervised learning for MS MALDI-TOF data." In 2021 IEEE Latin American Conference on Computational Intelligence (LA-CCI). IEEE, 2021. http://dx.doi.org/10.1109/la-cci48322.2021.9769825.

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Huang, Hung-Hsiang, Heng-Huan Lee, Pei-Lun Tsai, and Kay-Hooi Khoo. "DISTINCTIVE FEATURES OF MALDI-Q-TOF MS AND MS/MS ANALYSIS OF PERMETHYLATED GLYCANS FOR FACILE GLYCOMIC SEQUENCING." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.398.

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Rusnáková, Lenka, and Josef Havel. "Nano-gold applications in MALDI TOF MS of peptides." In XIIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2011. http://dx.doi.org/10.1135/css201113120.

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Jianqiu Zhang, Honghui Wang, Anthony Suffredini, Denise Gonzales, Elias Gonzalez, Yufei Huang, and Xiaobo Zhou. "Bayesian peak detection for Pro-TOF MS MALDI data." In ICASSP 2008 - 2008 IEEE International Conference on Acoustics, Speech and Signal Processing. IEEE, 2008. http://dx.doi.org/10.1109/icassp.2008.4517696.

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Kornfeld, Rich, James W. Kenny, Scot R. Weinberger, Yi Yang, and Ron Orlando. "Glycoprotein analysis using enzymatic digestion and MALDI-TOF MS." In Photonics West '96, edited by Gerald E. Cohn, Steven A. Soper, and C. H. Winston Chen. SPIE, 1996. http://dx.doi.org/10.1117/12.237629.

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Mantena, Vamsi, Wenjuan Jiang, Jiang Li, and Rick McKenzie. "Prostate cancer biomarker identification using MALDI-MS DATA: Initial results." In 2009 IEEE/NIH Life Science Systems and Applications Workshop (LiSSA) Formerly known as LSSA and. IEEE, 2009. http://dx.doi.org/10.1109/lissa.2009.4906723.

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Huilong Yang, Baoyou Liu, Yuyou Wang, and Limei Han. "MALDI-TOF MS progress and its application in Environmental Science." In 2011 International Conference on Remote Sensing, Environment and Transportation Engineering (RSETE). IEEE, 2011. http://dx.doi.org/10.1109/rsete.2011.5965161.

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Калинин, А. В., Е. А. Котенева, and О. И. Цыганкова. "Идентификация и дискриминация бактерий рода Bacillus методом MALDI-TOF MS." In VI Пущинская школа-конференция «Биохимия, физиология и биосферная роль микроорганизмов». ИД «Вода: химия и экология», 2019. http://dx.doi.org/10.18334/ibpm2019.25-27.

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Калинин, А. В., Е. А. Котенева, and О. И. Цыганкова. "Идентификация и дискриминация бактерий рода Bacillus методом MALDI-TOF MS." In VI Пущинская школа-конференция «Биохимия, физиология и биосферная роль микроорганизмов». ИД «Вода: химия и экология», 2019. http://dx.doi.org/10.18334/ibpm2019_25-27.

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Erhard, M., M. Metzner, D. Köhler-Repp, B. Köhler, and R. Storandt. "Infektionserreger beim Schwein – Analyse des kultivierbaren Mikrobioms mittels MALDI-TOF MS." In 20. Workshop des Arbeitskreises ‚Respiratorisches System‘ der Deutschen Veterinärmedizinischen Gesellschaft (DVG) in Kooperation mit der Deutschen Gesellschaft für Pneumologie und Beatmungsmedizin (DPG). Georg Thieme Verlag KG, 2017. http://dx.doi.org/10.1055/s-0037-1602728.

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Reports on the topic "MALDI-MS/MS"

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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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Fluhr, Robert, and Maor Bar-Peled. Novel Lectin Controls Wound-responses in Arabidopsis. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7697123.bard.

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Innate immune responses in animals and plants involve receptors that recognize microbe-associated molecules. In plants, one set of this defense system is characterized by large families of TIR–nucleotide binding site–leucine-rich repeat (TIR-NBS-LRR) resistance genes. The direct interaction between plant proteins harboring the TIR domain with proteins that transmit and facilitate a signaling pathway has yet to be shown. The Arabidopsis genome encodes TIR-domain containing genes that lack NBS and LRR whose functions are unknown. Here we investigated the functional role of such protein, TLW1 (TIR LECTIN WOUNDRESPONSIVE1). The TLW1 gene encodes a protein with two domains: a TIR domain linked to a lectin-containing domain. Our specific aim in this proposal was to examine the ramifications of the TL1-glycan interaction by; A) The functional characterization of TL1 activity in the context of plant wound response and B) Examine the hypothesis that wounding induced specific polysaccharides and examine them as candidates for TL-1 interactive glycan compounds. The Weizmann group showed TLW1 transcripts are rapidly induced by wounding in a JA-independent pathway and T-DNA-tagged tlw1 mutants that lack TLW1 transcripts, fail to initiate the full systemic wound response. Transcriptome methodology analysis was set up and transcriptome analyses indicates a two-fold reduced level of JA-responsive but not JA-independent transcripts. The TIR domain of TLW1 was found to interact directly with the KAT2/PED1 gene product responsible for the final b-oxidation steps in peroxisomal-basedJA biosynthesis. To identify potential binding target(s) of TL1 in plant wound response, the CCRC group first expressed recombinant TL1 in bacterial cells and optimized conditions for the protein expression. TL1 was most highly expressed in ArcticExpress cell line. Different types of extraction buffers and extraction methods were used to prepare plant extracts for TL1 binding assay. Optimized condition for glycan labeling was determined, and 2-aminobenzamide was used to label plant extracts. Sensitivity of MALDI and LC-MS using standard glycans. THAP (2,4,6- Trihydroxyacetophenone) showed minimal background peaks at positive mode of MALDI, however, it was insensitive with a minimum detection level of 100 ng. Using LC-MS, sensitivity was highly increased enough to detect 30 pmol concentration. However, patterns of total glycans displayed no significant difference between different extraction conditions when samples were separated with Dionex ICS-2000 ion chromatography system. Transgenic plants over-expressing lectin domains were generated to obtain active lectin domain in plant cells. Insertion of the overexpression construct into the plant genome was confirmed by antibiotic selection and genomic DNA PCR. However, RT-PCR analysis was not able to detect increased level of the transcripts. Binding ability of azelaic acid to recombinant TL1. Azelaic acid was detected in GST-TL1 elution fraction, however, DHB matrix has the same mass in background signals, which needs to be further tested on other matrices. The major findings showed the importance of TLW1 in regulating wound response. The findings demonstrate completely novel and unexpected TIR domain interactions and reveal a control nexus and mechanism that contributes to the propagation of wound responses in Arabidopsis. The implications are to our understanding of the function of TIR domains and to the notion that early molecular events occur systemically within minutes of a plant sustaining a wound. A WEB site (http://genome.weizmann.ac.il/hormonometer/) was set up that enables scientists to interact with a collated plant hormone database.
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Blumwald, Eduardo, and Avi Sadka. Citric acid metabolism and mobilization in citrus fruit. United States Department of Agriculture, October 2007. http://dx.doi.org/10.32747/2007.7587732.bard.

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Accumulation of citric acid is a major determinant of maturity and fruit quality in citrus. Many citrus varieties accumulate citric acid in concentrations that exceed market desires, reducing grower income and consumer satisfaction. Citrate is accumulated in the vacuole of the juice sac cell, a process that requires both metabolic changes and transport across cellular membranes, in particular, the mitochondrial and the vacuolar (tonoplast) membranes. Although the accumulation of citrate in the vacuoles of juice cells has been clearly demonstrated, the mechanisms for vacuolar citrate homeostasis and the components controlling citrate metabolism and transport are still unknown. Previous results in the PIs’ laboratories have indicated that the expression of a large number of a large number of proteins is enhanced during fruit development, and that the regulation of sugar and acid content in fruits is correlated with the differential expression of a large number of proteins that could play significant roles in fruit acid accumulation and/or regulation of acid content. The objectives of this proposal are: i) the characterization of transporters that mediate the transport of citrate and determine their role in uptake/retrieval in juice sac cells; ii) the study of citric acid metabolism, in particular the effect of arsenical compounds affecting citric acid levels and mobilization; and iii) the development of a citrus fruit proteomics platform to identify and characterize key processes associated with fruit development in general and sugar and acid accumulation in particular. The understanding of the cellular processes that determine the citrate content in citrus fruits will contribute to the development of tools aimed at the enhancement of citrus fruit quality. Our efforts resulted in the identification, cloning and characterization of CsCit1 (Citrus sinensis citrate transporter 1) from Navel oranges (Citrus sinesins cv Washington). Higher levels of CsCit1 transcripts were detected at later stages of fruit development that coincided with the decrease in the juice cell citrate concentrations (Shimada et al., 2006). Our functional analysis revealed that CsCit1 mediates the vacuolar efflux of citrate and that the CsCit1 operates as an electroneutral 1CitrateH2-/2H+ symporter. Our results supported the notion that it is the low permeable citrateH2 - the anion that establishes the buffer capacity of the fruit and determines its overall acidity. On the other hand, it is the more permeable form, CitrateH2-, which is being exported into the cytosol during maturation and controls the citrate catabolism in the juice cells. Our Mass-Spectrometry-based proteomics efforts (using MALDI-TOF-TOF and LC2- MS-MS) identified a large number of fruit juice sac cell proteins and established comparisons of protein synthesis patterns during fruit development. So far, we have identified over 1,500 fruit specific proteins that play roles in sugar metabolism, citric acid cycle, signaling, transport, processing, etc., and organized these proteins into 84 known biosynthetic pathways (Katz et al. 2007). This data is now being integrated in a public database and will serve as a valuable tool for the scientific community in general and fruit scientists in particular. Using molecular, biochemical and physiological approaches we have identified factors affecting the activity of aconitase, which catalyze the first step of citrate catabolism (Shlizerman et al., 2007). Iron limitation specifically reduced the activity of the cytosolic, but not the mitochondrial, aconitase, increasing the acid level in the fruit. Citramalate (a natural compound in the juice) also inhibits the activity of aconitase, and it plays a major role in acid accumulation during the first half of fruit development. On the other hand, arsenite induced increased levels of aconitase, decreasing fruit acidity. We have initiated studies aimed at the identification of the citramalate biosynthetic pathway and the role(s) of isopropylmalate synthase in this pathway. These studies, especially those involved aconitase inhibition by citramalate, are aimed at the development of tools to control fruit acidity, particularly in those cases where acid level declines below the desired threshold. Our work has significant implications both scientifically and practically and is directly aimed at the improvement of fruit quality through the improvement of existing pre- and post-harvest fruit treatments.
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