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dc.contributor.author Savaryn, John P.
dc.contributor.author Toby, Timothy K.
dc.contributor.author Catherman, Adam D.
dc.contributor.author Fellers, Ryan T.
dc.contributor.author LeDuc, Richard D.
dc.contributor.author Thomas, Paul M.
dc.contributor.author Friedewald, John J.
dc.contributor.author Salomon, Daniel R.
dc.contributor.author Abecassis, Michael M.
dc.contributor.author Kelleher, Neil L.
dc.date.accessioned 2016-03-21T14:17:56Z
dc.date.available 2016-03-21T14:17:56Z
dc.date.issued 2016-02-19
dc.identifier.citation Savaryn, Toby, et al. Comparative top down proteomics of peripheral blood mononuclear cells from kidney transplant recipients with normal kidney biopsies or acute rejection, Proteomics xxx (2016) xxx-xxx en
dc.identifier.uri http://hdl.handle.net/2022/20747
dc.description.abstract Recent studies utilizing transcriptomics, metabolomics, and bottom up proteomics have identified molecular signatures of kidney allograft pathology. Although these results make significant progress toward non-invasive differential diagnostics of dysfunction of a transplanted kidney, they provide little information on the intact, often modified, protein molecules present during progression of this pathology. Because intact proteins underpin diverse biological processes, measuring the relative abundance of their modified forms promises to advance mechanistic understanding, and might provide a new class of biomarker candidates. Here, we used top down proteomics to inventory the modified forms of whole proteins in peripheral blood mononuclear cells (PBMCs) taken at the time of kidney biopsy for 40 kidney allograft recipients either with healthy transplants or those suffering acute rejection. Supported by gas-phase fragmentation of whole protein ions during tandem mass spectrometry, we identified 344 proteins mapping to 2,905 distinct molecular forms (proteoforms). Using an initial implementation of a label-free approach to quantitative top down proteomics, we obtained evidence suggesting relative abundance changes in 111 proteoforms between the two patient groups. Collectively, our work is the first to catalog intact protein molecules in PBMCs and suggests differentially abundant proteoforms for further analysis. en
dc.description.sponsorship The following grants are acknowledged: National Institutes of Health P41 GM108569, R01 GM067193 to NLK, P01 AI112522 to NLK and MMA, and U19 A1063603 to DRS. en
dc.language.iso en_US en
dc.publisher Proteomics en
dc.rights THE WORK (AS DEFINED BELOW) IS PROVIDED UNDER THE TERMS OF THIS CREATIVE COMMONS PUBLIC LICENSE ("CCPL" OR "LICENSE"). THE WORK IS PROTECTED BY COPYRIGHT AND/OR OTHER APPLICABLE LAW. ANY USE OF THE WORK OTHER THAN AS AUTHORIZED UNDER THIS LICENSE OR COPYRIGHT LAW IS PROHIBITED. BY EXERCISING ANY RIGHTS TO THE WORK PROVIDED HERE, YOU ACCEPT AND AGREE TO BE BOUND BY THE TERMS OF THIS LICENSE. TO THE EXTENT THIS LICENSE MAY BE CONSIDERED TO BE A CONTRACT, THE LICENSOR GRANTS YOU THE RIGHTS CONTAINED HERE IN CONSIDERATION OF YOUR ACCEPTANCE OF SUCH TERMS AND CONDITIONS. en
dc.rights.uri http://creativecommons.org/licenses/by/3.0/ en
dc.subject Biomarker, Mass spectrometry, Proteoform, Proteomics, Transplant en
dc.title Comparative top down proteomics of peripheral blood mononuclear cells from kidney transplant recipients with normal kidney biopsies or acute rejection en
dc.type Dataset en
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