Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation

Research output: Contribution to journalJournal articleResearchpeer-review

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Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation. / Batth, Tanveer Singh; Tollenaere, Maxim A. X.; Rüther, Patrick Leopold; Gonzalez-Franquesa, Alba; Prabhakar, Bhargav Saligram; Bekker-Jensen, Simon Holst; Deshmukh, Atul Shahaji; Olsen, Jesper V.

In: Molecular and Cellular Proteomics, Vol. 18, No. 5, 2019, p. 1027-1035.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Batth, TS, Tollenaere, MAX, Rüther, PL, Gonzalez-Franquesa, A, Prabhakar, BS, Bekker-Jensen, SH, Deshmukh, AS & Olsen, JV 2019, 'Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation', Molecular and Cellular Proteomics, vol. 18, no. 5, pp. 1027-1035. https://doi.org/10.1074/mcp.TIR118.001270

APA

Batth, T. S., Tollenaere, M. A. X., Rüther, P. L., Gonzalez-Franquesa, A., Prabhakar, B. S., Bekker-Jensen, S. H., ... Olsen, J. V. (2019). Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation. Molecular and Cellular Proteomics, 18(5), 1027-1035. https://doi.org/10.1074/mcp.TIR118.001270

Vancouver

Batth TS, Tollenaere MAX, Rüther PL, Gonzalez-Franquesa A, Prabhakar BS, Bekker-Jensen SH et al. Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation. Molecular and Cellular Proteomics. 2019;18(5):1027-1035. https://doi.org/10.1074/mcp.TIR118.001270

Author

Batth, Tanveer Singh ; Tollenaere, Maxim A. X. ; Rüther, Patrick Leopold ; Gonzalez-Franquesa, Alba ; Prabhakar, Bhargav Saligram ; Bekker-Jensen, Simon Holst ; Deshmukh, Atul Shahaji ; Olsen, Jesper V. / Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation. In: Molecular and Cellular Proteomics. 2019 ; Vol. 18, No. 5. pp. 1027-1035.

Bibtex

@article{a81d6964f0194b44a488295153e260f8,
title = "Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation",
abstract = "Universal proteomics sample preparation is challenging due to the high heterogeneity of biological samples. Here we describe a novel mechanism that exploits the inherent instability of denatured proteins for non-specific immobilization on microparticles by protein aggregation capture. To demonstrate the general applicability of this mechanism, we analyzed phosphoproteomes, tissue proteomes, and interaction proteomes as well as dilute secretomes. The findings presents a practical, sensitive and cost-effective proteomics sample preparation method.",
author = "Batth, {Tanveer Singh} and Tollenaere, {Maxim A. X.} and R{\"u}ther, {Patrick Leopold} and Alba Gonzalez-Franquesa and Prabhakar, {Bhargav Saligram} and Bekker-Jensen, {Simon Holst} and Deshmukh, {Atul Shahaji} and Olsen, {Jesper V.}",
year = "2019",
doi = "10.1074/mcp.TIR118.001270",
language = "English",
volume = "18",
pages = "1027--1035",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology",
number = "5",

}

RIS

TY - JOUR

T1 - Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation

AU - Batth, Tanveer Singh

AU - Tollenaere, Maxim A. X.

AU - Rüther, Patrick Leopold

AU - Gonzalez-Franquesa, Alba

AU - Prabhakar, Bhargav Saligram

AU - Bekker-Jensen, Simon Holst

AU - Deshmukh, Atul Shahaji

AU - Olsen, Jesper V.

PY - 2019

Y1 - 2019

N2 - Universal proteomics sample preparation is challenging due to the high heterogeneity of biological samples. Here we describe a novel mechanism that exploits the inherent instability of denatured proteins for non-specific immobilization on microparticles by protein aggregation capture. To demonstrate the general applicability of this mechanism, we analyzed phosphoproteomes, tissue proteomes, and interaction proteomes as well as dilute secretomes. The findings presents a practical, sensitive and cost-effective proteomics sample preparation method.

AB - Universal proteomics sample preparation is challenging due to the high heterogeneity of biological samples. Here we describe a novel mechanism that exploits the inherent instability of denatured proteins for non-specific immobilization on microparticles by protein aggregation capture. To demonstrate the general applicability of this mechanism, we analyzed phosphoproteomes, tissue proteomes, and interaction proteomes as well as dilute secretomes. The findings presents a practical, sensitive and cost-effective proteomics sample preparation method.

U2 - 10.1074/mcp.TIR118.001270

DO - 10.1074/mcp.TIR118.001270

M3 - Journal article

VL - 18

SP - 1027

EP - 1035

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

SN - 1535-9476

IS - 5

ER -

ID: 214465266