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Selymatra: A web application for protein‐profiling analysis of mass spectra
Surface enhanced laser desorption/ionization‐time of flight (SELDI‐TOF) mass spectrometry is a variant of the matrix‐assisted laser desorption/ionization‐time of flight (MALDI‐TOF) mass spectrometry. It is used in many cases especially for the analysis of protein profiling and for preliminary screen...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9912196/ https://www.ncbi.nlm.nih.gov/pubmed/34487563 http://dx.doi.org/10.1002/bab.2249 |
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author | Nardone, Davide Ciaramella, Angelo Cerreta, Mariangela Pulcrano, Salvatore Bellenchi, Gian C. Leone, Linda Manco, Giuseppe Febbraio, Ferdinando |
author_facet | Nardone, Davide Ciaramella, Angelo Cerreta, Mariangela Pulcrano, Salvatore Bellenchi, Gian C. Leone, Linda Manco, Giuseppe Febbraio, Ferdinando |
author_sort | Nardone, Davide |
collection | PubMed |
description | Surface enhanced laser desorption/ionization‐time of flight (SELDI‐TOF) mass spectrometry is a variant of the matrix‐assisted laser desorption/ionization‐time of flight (MALDI‐TOF) mass spectrometry. It is used in many cases especially for the analysis of protein profiling and for preliminary screening of biomarkers in complex samples. Unfortunately, these analyses are time consuming and protein identification is generally strictly limited. SELDI‐TOF analysis of mass spectra (SELYMATRA) is a web application (WA) developed to reduce these limitations by (i) automating the identification processes and (ii) introducing the possibility to predict proteins in complex mixtures from cells and tissues. The WA architectural pattern is the model‐view‐controller, commonly used in software development. The WA compares the mass value between two mass spectra (sample vs. control) to extract differences, and, according to the set parameters, it queries a local database to predict most likely proteins based on their masses and different expression amplification. The WA was validated in a cellular model overexpressing a tagged NURR1 receptor, being able to recognize the tagged protein in the profiling of transformed cells. A help page, including a description of parameters for WA use, is available on the website. |
format | Online Article Text |
id | pubmed-9912196 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-99121962023-02-11 Selymatra: A web application for protein‐profiling analysis of mass spectra Nardone, Davide Ciaramella, Angelo Cerreta, Mariangela Pulcrano, Salvatore Bellenchi, Gian C. Leone, Linda Manco, Giuseppe Febbraio, Ferdinando Biotechnol Appl Biochem Original Articles Surface enhanced laser desorption/ionization‐time of flight (SELDI‐TOF) mass spectrometry is a variant of the matrix‐assisted laser desorption/ionization‐time of flight (MALDI‐TOF) mass spectrometry. It is used in many cases especially for the analysis of protein profiling and for preliminary screening of biomarkers in complex samples. Unfortunately, these analyses are time consuming and protein identification is generally strictly limited. SELDI‐TOF analysis of mass spectra (SELYMATRA) is a web application (WA) developed to reduce these limitations by (i) automating the identification processes and (ii) introducing the possibility to predict proteins in complex mixtures from cells and tissues. The WA architectural pattern is the model‐view‐controller, commonly used in software development. The WA compares the mass value between two mass spectra (sample vs. control) to extract differences, and, according to the set parameters, it queries a local database to predict most likely proteins based on their masses and different expression amplification. The WA was validated in a cellular model overexpressing a tagged NURR1 receptor, being able to recognize the tagged protein in the profiling of transformed cells. A help page, including a description of parameters for WA use, is available on the website. John Wiley and Sons Inc. 2021-09-20 2022-10 /pmc/articles/PMC9912196/ /pubmed/34487563 http://dx.doi.org/10.1002/bab.2249 Text en © 2021 The Authors. Biotechnology and Applied Biochemistry published by Wiley Periodicals LLC on behalf of International Union of Biochemistry and Molecular Biology. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Original Articles Nardone, Davide Ciaramella, Angelo Cerreta, Mariangela Pulcrano, Salvatore Bellenchi, Gian C. Leone, Linda Manco, Giuseppe Febbraio, Ferdinando Selymatra: A web application for protein‐profiling analysis of mass spectra |
title | Selymatra: A web application for protein‐profiling analysis of mass spectra |
title_full | Selymatra: A web application for protein‐profiling analysis of mass spectra |
title_fullStr | Selymatra: A web application for protein‐profiling analysis of mass spectra |
title_full_unstemmed | Selymatra: A web application for protein‐profiling analysis of mass spectra |
title_short | Selymatra: A web application for protein‐profiling analysis of mass spectra |
title_sort | selymatra: a web application for protein‐profiling analysis of mass spectra |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9912196/ https://www.ncbi.nlm.nih.gov/pubmed/34487563 http://dx.doi.org/10.1002/bab.2249 |
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