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Data Brief. 2018 Mar 31;18:1013-1021. doi: 10.1016/j.dib.2018.03.114. eCollection 2018 Jun.

Identification of multiple proteoforms biomarkers on clinical samples by routine Top-Down approaches.

Author information

1
University of Montpellier, LBPC, IRMB, CHU de Montpellier, 34000 Montpellier, France.
2
Bruker Daltonique, S.A, 34, rue de l'industrie, 67160 Wissembourg, France.
3
Centre Mémoire Ressources Recherche, CHU Montpellier, hôpital Gui de Chauliac, Université Montpellier I, Montpellier F-34000, France.
4
Bruker Daltonics Inc., 40 Manning Road, Billerica, MA 01821, USA.
5
Protein Metrics Inc., 1622 San Carlos Ave., San Carlos, CA 94070 USA.
6
Bruker Daltonik GmbH, Fahrenheitstrasse 4, 28359 Bremen, Germany.

Abstract

Top-Down approaches have an extremely high biological relevance, especially when it comes to biomarker discovery, but the necessary pre-fractionation constraints are not easily compatible with the robustness requirements and the size of clinical sample cohorts. We have demonstrated that intact protein profiling studies could be run on UHR-Q-ToF with limited pre-fractionation (Schmit et al., 2017) [1]. The dataset presented herein is an extension of this research. Proteoforms known to play a role in the pathophysiology process of Alzheimer's disease were identified as candidate biomarkers. In this article, mass spectrometry performance of these candidates are demonstrated.

KEYWORDS:

Alzheimer disease; Clinical proteomics; Top-Down label-free proteoform profiling; Ultra-high resolution Q-Tof

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