Mass spectrometry dataset on apo-SOD1 modifications induced by lipid aldehydes
Metal-deficient Cu,Zn-superoxide dismutase (apo-SOD1) is associated with the formation of SOD1 aggregates that accumulate in ALS disease. The data supplied in this article support the accompanying publication showing SOD1 modification and aggregation induced by lipid aldehydes [1]. Here, we present...
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| Format: | Article |
| Language: | English |
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Elsevier
2020-08-01
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| Series: | Data in Brief |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340920307447 |
| _version_ | 1818141641233399808 |
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| author | Lucas S. Dantas Alex Inague Adriano Britto Chaves-Filho Sayuri Miyamoto |
| author_facet | Lucas S. Dantas Alex Inague Adriano Britto Chaves-Filho Sayuri Miyamoto |
| author_sort | Lucas S. Dantas |
| collection | DOAJ |
| description | Metal-deficient Cu,Zn-superoxide dismutase (apo-SOD1) is associated with the formation of SOD1 aggregates that accumulate in ALS disease. The data supplied in this article support the accompanying publication showing SOD1 modification and aggregation induced by lipid aldehydes [1]. Here, we present the LC-MS/MS dataset on apo-SOD1 modification induced by seven different lipid aldehydes: 4-hydroxy-2-hexenal (HHE), 4-hydroxy-2-nonenal (HNE), 2-hexen-1-al (HEX), 2,4-nonadienal (NON), 2,4-decadienal (DEC) or secosterol aldehydes (SECO-A or SECO-B). Modified protein samples were digested with trypsin and sequenced by a LC coupled to a Q-TOF instrument. Protein sequencing and peptide modification analysis was performed by Mascot 2.6 (Matrix Science) and further validated by manual inspection. Mass spectrometry data (RAW files) obtained in this study have been deposited to MassIVE and the observed peptide-aldehyde adducts can be used in further studies exploring SOD1 modifications in vivo. |
| first_indexed | 2024-12-11T11:03:06Z |
| format | Article |
| id | doaj.art-ab0f0882096644ae9951865123a5dfd4 |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-11T11:03:06Z |
| publishDate | 2020-08-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-ab0f0882096644ae9951865123a5dfd42022-12-22T01:09:48ZengElsevierData in Brief2352-34092020-08-0131105850Mass spectrometry dataset on apo-SOD1 modifications induced by lipid aldehydesLucas S. Dantas0Alex Inague1Adriano Britto Chaves-Filho2Sayuri Miyamoto3Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, SP, BrazilDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, SP, BrazilDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, SP, BrazilCorresponding author.; Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, SP, BrazilMetal-deficient Cu,Zn-superoxide dismutase (apo-SOD1) is associated with the formation of SOD1 aggregates that accumulate in ALS disease. The data supplied in this article support the accompanying publication showing SOD1 modification and aggregation induced by lipid aldehydes [1]. Here, we present the LC-MS/MS dataset on apo-SOD1 modification induced by seven different lipid aldehydes: 4-hydroxy-2-hexenal (HHE), 4-hydroxy-2-nonenal (HNE), 2-hexen-1-al (HEX), 2,4-nonadienal (NON), 2,4-decadienal (DEC) or secosterol aldehydes (SECO-A or SECO-B). Modified protein samples were digested with trypsin and sequenced by a LC coupled to a Q-TOF instrument. Protein sequencing and peptide modification analysis was performed by Mascot 2.6 (Matrix Science) and further validated by manual inspection. Mass spectrometry data (RAW files) obtained in this study have been deposited to MassIVE and the observed peptide-aldehyde adducts can be used in further studies exploring SOD1 modifications in vivo.http://www.sciencedirect.com/science/article/pii/S2352340920307447PTMLipid aldehydesLipid electrophilesSecoaldehydesOxysterolSOD1 |
| spellingShingle | Lucas S. Dantas Alex Inague Adriano Britto Chaves-Filho Sayuri Miyamoto Mass spectrometry dataset on apo-SOD1 modifications induced by lipid aldehydes Data in Brief PTM Lipid aldehydes Lipid electrophiles Secoaldehydes Oxysterol SOD1 |
| title | Mass spectrometry dataset on apo-SOD1 modifications induced by lipid aldehydes |
| title_full | Mass spectrometry dataset on apo-SOD1 modifications induced by lipid aldehydes |
| title_fullStr | Mass spectrometry dataset on apo-SOD1 modifications induced by lipid aldehydes |
| title_full_unstemmed | Mass spectrometry dataset on apo-SOD1 modifications induced by lipid aldehydes |
| title_short | Mass spectrometry dataset on apo-SOD1 modifications induced by lipid aldehydes |
| title_sort | mass spectrometry dataset on apo sod1 modifications induced by lipid aldehydes |
| topic | PTM Lipid aldehydes Lipid electrophiles Secoaldehydes Oxysterol SOD1 |
| url | http://www.sciencedirect.com/science/article/pii/S2352340920307447 |
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