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13 results on '"Oppermann, Madalina"'

2. The Human Melanoma Proteome Atlas—Complementing the melanoma transcriptome

Author

Betancourt, Lazaro Hiram, primary, Gil, Jeovanis, additional, Sanchez, Aniel, additional, Doma, Viktória, additional, Kuras, Magdalena, additional, Murillo, Jimmy Rodriguez, additional, Velasquez, Erika, additional, Çakır, Uğur, additional, Kim, Yonghyo, additional, Sugihara, Yutaka, additional, Parada, Indira Pla, additional, Szeitz, Beáta, additional, Appelqvist, Roger, additional, Wieslander, Elisabet, additional, Welinder, Charlotte, additional, de Almeida, Natália Pinto, additional, Woldmar, Nicole, additional, Marko‐Varga, Matilda, additional, Eriksson, Jonatan, additional, Pawłowski, Krzysztof, additional, Baldetorp, Bo, additional, Ingvar, Christian, additional, Olsson, Håkan, additional, Lundgren, Lotta, additional, Lindberg, Henrik, additional, Oskolas, Henriett, additional, Lee, Boram, additional, Berge, Ethan, additional, Sjögren, Marie, additional, Eriksson, Carina, additional, Kim, Dasol, additional, Kwon, Ho Jeong, additional, Knudsen, Beatrice, additional, Rezeli, Melinda, additional, Malm, Johan, additional, Hong, Runyu, additional, Horvath, Peter, additional, Szász, A. Marcell, additional, Tímár, József, additional, Kárpáti, Sarolta, additional, Horvatovich, Peter, additional, Miliotis, Tasso, additional, Nishimura, Toshihide, additional, Kato, Harubumi, additional, Steinfelder, Erik, additional, Oppermann, Madalina, additional, Miller, Ken, additional, Florindi, Francesco, additional, Zhou, Quimin, additional, Domont, Gilberto B., additional, Pizzatti, Luciana, additional, Nogueira, Fábio C. S., additional, Szadai, Leticia, additional, Németh, István Balázs, additional, Ekedahl, Henrik, additional, Fenyö, David, additional, and Marko‐Varga, György, additional

Published
2021
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3. The human melanoma proteome atlas—Defining the molecular pathology

Author

Betancourt, Lazaro Hiram, primary, Gil, Jeovanis, additional, Kim, Yonghyo, additional, Doma, Viktória, additional, Çakır, Uğur, additional, Sanchez, Aniel, additional, Murillo, Jimmy Rodriguez, additional, Kuras, Magdalena, additional, Parada, Indira Pla, additional, Sugihara, Yutaka, additional, Appelqvist, Roger, additional, Wieslander, Elisabet, additional, Welinder, Charlotte, additional, Velasquez, Erika, additional, de Almeida, Natália Pinto, additional, Woldmar, Nicole, additional, Marko‐Varga, Matilda, additional, Pawłowski, Krzysztof, additional, Eriksson, Jonatan, additional, Szeitz, Beáta, additional, Baldetorp, Bo, additional, Ingvar, Christian, additional, Olsson, Håkan, additional, Lundgren, Lotta, additional, Lindberg, Henrik, additional, Oskolas, Henriett, additional, Lee, Boram, additional, Berge, Ethan, additional, Sjögren, Marie, additional, Eriksson, Carina, additional, Kim, Dasol, additional, Kwon, Ho Jeong, additional, Knudsen, Beatrice, additional, Rezeli, Melinda, additional, Hong, Runyu, additional, Horvatovich, Peter, additional, Miliotis, Tasso, additional, Nishimura, Toshihide, additional, Kato, Harubumi, additional, Steinfelder, Erik, additional, Oppermann, Madalina, additional, Miller, Ken, additional, Florindi, Francesco, additional, Zhou, Qimin, additional, Domont, Gilberto B., additional, Pizzatti, Luciana, additional, Nogueira, Fábio C. S., additional, Horvath, Peter, additional, Szadai, Leticia, additional, Tímár, József, additional, Kárpáti, Sarolta, additional, Szász, A. Marcell, additional, Malm, Johan, additional, Fenyö, David, additional, Ekedahl, Henrik, additional, Németh, István Balázs, additional, and Marko‐Varga, György, additional

Published
2021
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6. A Selected Reaction Monitoring (SRM)-Based Method for Absolute Quantification of Aβ38, Aβ40, and Aβ42 in Cerebrospinal Fluid of Alzheimer's Disease Patients and Healthy Controls

Author

Pannee, Josef, primary, Portelius, Erik, additional, Oppermann, Madalina, additional, Atkins, Alan, additional, Hornshaw, Martin, additional, Zegers, Ingrid, additional, Höjrup, Peter, additional, Minthon, Lennart, additional, Hansson, Oskar, additional, Zetterberg, Henrik, additional, Blennow, Kaj, additional, and Gobom, Johan, additional

Published
2013
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10. Identification of foetal brain proteins by two-dimensional gel electrophoresis and mass spectrometry

Author

Oppermann, Madalina, primary, Cols, Neus, additional, Nyman, Tuula, additional, Helin, Jari, additional, Saarinen, Juhani, additional, Byman, Irene, additional, Toran, Núria, additional, Alaiya, Ayodele A., additional, Bergman, Tomas, additional, Kalkkinen, Nisse, additional, Gonzàlez-Duarte, Roser, additional, and Jörnvall, Hans, additional

Published
2000
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11. A Selected Reaction Monitoring (SRM)-Based Method for Absolute Quantification of Aβ38, Aβ40, and Aβ42 in Cerebrospinal Fluid of Alzheimer's Disease Patients and Healthy Controls.

Author

Pannee, Josef, Portelius, Erik, Oppermann, Madalina, Atkins, Alan, Hornshaw, Martin, Zegers, Ingrid, Höjrup, Peter, Minthon, Lennart, Hansson, Oskar, Zetterberg, Henrik, Blennow, Kaj, and Gobom, Johan

Subjects
ALZHEIMER'S patients, CEREBROSPINAL fluid, DISEASES in older people, CLINICAL trials, SOLID phase extraction
Abstract

Cerebrospinal fluid (CSF) biomarkers for Alzheimer's disease (AD) are increasingly used in research centers, clinical trials, and clinical settings. However, their broad-scale use is hampered by lack of standardization across analytical platforms and by interference from binding of amyloid-β (Aβ) to matrix proteins as well as self-aggregation. Here, we report on a matrix effect-resistant method for the measurement of the AD-associated 42 amino acid species of Aβ (Aβ42), together with Aβ40 and Aβ38 in human CSF based on mass spectrometric quantification using selected reaction monitoring (SRM). Samples were prepared by solid-phase extraction and quantification was performed using stable-isotope labeled Aβ peptides as internal standards. The diagnostic performance of the method was evaluated on two independent clinical materials with research volunteers who were cognitively normal and AD patients with mild to moderate dementia. Analytical characteristics of the method include a lower limit of quantification of 62.5 pg/mL for Aβ42 and coefficients of variations below 10%. In a pilot study on AD patients and controls, we verified disease-association with decreased levels of Aβ42 similar to that obtained by ELISA and even better separation was obtained using the Aβ42/Aβ40 ratio. The developed assay is sensitive and is not influenced by matrix effects, enabling absolute quantification of Aβ42, Aβ40, and Aβ38 in CSF, while it retains the ability to distinguish AD patients from controls. We suggest this SRM-based method for Aβ peptide quantification in human CSF valuable for clinical research and trials. [ABSTRACT FROM AUTHOR]

Published
2013
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12. High precision measurement and fragmentation analysis for metabolite identification.

Author

Oppermann M, Damoc NE, Crone C, Moehring T, Muenster H, and Hornshaw M

Subjects
Citric Acid analysis, Molecular Weight, Phenylalanine analysis, Brassica chemistry, Chromatography, Liquid methods, Mass Spectrometry methods, Metabolome
Abstract

The degree of precision in measuring accurate masses in LC MS/MS-based metabolomics experiments is a determinant in the successful identification of the metabolites present in the original extract. Using the methods described here, complex broccoli extracts containing hundreds of small-molecule compounds (mass range 100-1,400 Da) can be profiled at resolutions up to 100,000 (full width half maximum, FWHM), useful for accurate and sensitive relative quantification experiments. Using external instrument calibration, analyte masses can be measured with high (sub-ppm to a maximum of 2 ppm) accuracy, leading to compound identifications based on elemental composition analysis. Unambiguous identification of four analytes (citric acid, chlorogenic acid, phenylalanine, and UDP-D: -glucose) is used to validate the performance of the different MS/MS fragmentation regimes. Identifications are carried out either via resonance excitation collision induced dissociation (CID) or via higher energy collision dissociation (HCD) experiments, and validated by infrared multiphoton dissociation (IRMPD) fragmentation of standards. Such results, obtained on both hybrid and non-hybrid systems from metabolite profiling and identification experiments, provide evidence that the strategies selected can be successfully applied to other LC-MS based projects for plant metabolomic studies.

Published
2012
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13. Dihydropyrimidinase related protein-2 as a biomarker for temperature and time dependent post mortem changes in the mouse brain proteome.

Author

Franzén B, Yang Y, Sunnemark D, Wickman M, Ottervald J, Oppermann M, and Sandberg K

Subjects
Animals, Biomarkers analysis, Carrier Proteins analysis, Chaperonin Containing TCP-1, Chaperonins analysis, Data Interpretation, Statistical, Databases, Protein, Electrophoresis, Gel, Two-Dimensional, Female, Image Processing, Computer-Assisted, Intercellular Signaling Peptides and Proteins, Intermediate Filament Proteins, Isoelectric Focusing, Mice, Mice, Inbred C57BL, Peptide Fragments analysis, Proteomics, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Temperature, Time Factors, Tubulin analysis, Brain metabolism, Brain Chemistry, Nerve Tissue Proteins analysis, Postmortem Changes, Proteome analysis
Abstract

Proteome analysis in the central nervous system area represents a large and important challenge in drug discovery. One major problem is to obtain representative and well characterized tissues of high quality for analysis. We have used brain tissues from normal mice to study the effect of post mortem time (up to 32 h) and temperature (4 degrees C and room temperature) on protein expression patterns. A number of proteins were identified using mass spectrometry and potential markers were localized. One of the proteins identified, dihydropyrimidinase related protein-2 (DRP-2), occurs as multiple spots in two-dimensional electrophoresis gels. The ratio between the truncated form of DRP-2 (fDRP-2) and full length DRP-2 is suggested as an internal control that can be used as a biomarker of post mortem time and post mortem temperature between unrelated brain protein samples. Results of this study may be useful in future efforts to detect disease specific alterations in proteomic studies of human post mortem brain tissues.

Published
2003
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