Analysis of the rat hypothalamus proteome by data-independent label-free LC-MS/MS.
Studies of neuronal, endocrine, and metabolic disorders would be facilitated by characterization of the hypothalamus proteome. Protein extracts prepared from 16 whole rat hypothalami were measured by data-independent label-free nano LC-MS/MS. Peptide features were detected, aligned, and searched aga...
Príomhchruthaitheoirí: | , , , , , , , , |
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Formáid: | Journal article |
Teanga: | English |
Foilsithe / Cruthaithe: |
2012
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author | Stelzhammer, V Amess, B Martins-de-Souza, D Levin, Y Ozanne, SE Martin-Gronert, MS Urday, S Bahn, S Guest, P |
author_facet | Stelzhammer, V Amess, B Martins-de-Souza, D Levin, Y Ozanne, SE Martin-Gronert, MS Urday, S Bahn, S Guest, P |
author_sort | Stelzhammer, V |
collection | OXFORD |
description | Studies of neuronal, endocrine, and metabolic disorders would be facilitated by characterization of the hypothalamus proteome. Protein extracts prepared from 16 whole rat hypothalami were measured by data-independent label-free nano LC-MS/MS. Peptide features were detected, aligned, and searched against a rat Swiss-Prot database using ProteinLynx Global Server v.2.5. The final combined dataset comprised 21 455 peptides, corresponding to 622 unique proteins, each identified by a minimum of two distinct peptides. The majority of the proteins (69%) were cytosolic, and 16% were membrane proteins. Important proteins involved in neurological and synaptic function were identified including several members of the Ras-related protein family and proteins involved in glutamate biosynthesis. |
first_indexed | 2024-03-07T03:37:37Z |
format | Journal article |
id | oxford-uuid:bcd18b4a-53e4-457a-87d7-a371b5b09dd2 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T03:37:37Z |
publishDate | 2012 |
record_format | dspace |
spelling | oxford-uuid:bcd18b4a-53e4-457a-87d7-a371b5b09dd22022-03-27T05:27:18ZAnalysis of the rat hypothalamus proteome by data-independent label-free LC-MS/MS.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:bcd18b4a-53e4-457a-87d7-a371b5b09dd2EnglishSymplectic Elements at Oxford2012Stelzhammer, VAmess, BMartins-de-Souza, DLevin, YOzanne, SEMartin-Gronert, MSUrday, SBahn, SGuest, PStudies of neuronal, endocrine, and metabolic disorders would be facilitated by characterization of the hypothalamus proteome. Protein extracts prepared from 16 whole rat hypothalami were measured by data-independent label-free nano LC-MS/MS. Peptide features were detected, aligned, and searched against a rat Swiss-Prot database using ProteinLynx Global Server v.2.5. The final combined dataset comprised 21 455 peptides, corresponding to 622 unique proteins, each identified by a minimum of two distinct peptides. The majority of the proteins (69%) were cytosolic, and 16% were membrane proteins. Important proteins involved in neurological and synaptic function were identified including several members of the Ras-related protein family and proteins involved in glutamate biosynthesis. |
spellingShingle | Stelzhammer, V Amess, B Martins-de-Souza, D Levin, Y Ozanne, SE Martin-Gronert, MS Urday, S Bahn, S Guest, P Analysis of the rat hypothalamus proteome by data-independent label-free LC-MS/MS. |
title | Analysis of the rat hypothalamus proteome by data-independent label-free LC-MS/MS. |
title_full | Analysis of the rat hypothalamus proteome by data-independent label-free LC-MS/MS. |
title_fullStr | Analysis of the rat hypothalamus proteome by data-independent label-free LC-MS/MS. |
title_full_unstemmed | Analysis of the rat hypothalamus proteome by data-independent label-free LC-MS/MS. |
title_short | Analysis of the rat hypothalamus proteome by data-independent label-free LC-MS/MS. |
title_sort | analysis of the rat hypothalamus proteome by data independent label free lc ms ms |
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