The emerging role of mass spectrometry-based proteomics in drug discovery

Research output: Contribution to journalReviewResearchpeer-review

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The emerging role of mass spectrometry-based proteomics in drug discovery. / Meissner, Felix; Geddes-McAlister, Jennifer; Mann, Matthias; Bantscheff, Marcus.

In: Nature Reviews Drug Discovery, Vol. 21, 2022, p. 637-654.

Research output: Contribution to journalReviewResearchpeer-review

Harvard

Meissner, F, Geddes-McAlister, J, Mann, M & Bantscheff, M 2022, 'The emerging role of mass spectrometry-based proteomics in drug discovery', Nature Reviews Drug Discovery, vol. 21, pp. 637-654. https://doi.org/10.1038/s41573-022-00409-3

APA

Meissner, F., Geddes-McAlister, J., Mann, M., & Bantscheff, M. (2022). The emerging role of mass spectrometry-based proteomics in drug discovery. Nature Reviews Drug Discovery, 21, 637-654. https://doi.org/10.1038/s41573-022-00409-3

Vancouver

Meissner F, Geddes-McAlister J, Mann M, Bantscheff M. The emerging role of mass spectrometry-based proteomics in drug discovery. Nature Reviews Drug Discovery. 2022;21:637-654. https://doi.org/10.1038/s41573-022-00409-3

Author

Meissner, Felix ; Geddes-McAlister, Jennifer ; Mann, Matthias ; Bantscheff, Marcus. / The emerging role of mass spectrometry-based proteomics in drug discovery. In: Nature Reviews Drug Discovery. 2022 ; Vol. 21. pp. 637-654.

Bibtex

@article{818abe0fcd4f420695bb237b7595af15,
title = "The emerging role of mass spectrometry-based proteomics in drug discovery",
abstract = "System-wide methods to monitor protein activity are still underused in drug discovery. This Review discusses the potential of proteomics and chemoproteomics approaches for target identification, validation and identification of safety hazards.Proteins are the main targets of most drugs; however, system-wide methods to monitor protein activity and function are still underused in drug discovery. Novel biochemical approaches, in combination with recent developments in mass spectrometry-based proteomics instrumentation and data analysis pipelines, have now enabled the dissection of disease phenotypes and their modulation by bioactive molecules at unprecedented resolution and dimensionality. In this Review, we describe proteomics and chemoproteomics approaches for target identification and validation, as well as for identification of safety hazards. We discuss innovative strategies in early-stage drug discovery in which proteomics approaches generate unique insights, such as targeted protein degradation and the use of reactive fragments, and provide guidance for experimental strategies crucial for success.",
keywords = "QUANTITATIVE CHEMICAL PROTEOMICS, PROTEIN-INTERACTION LANDSCAPE, HIGH-THROUGHPUT SCREEN, SMALL-MOLECULE PROBES, TARGET IDENTIFICATION, DEACETYLASE INHIBITORS, TYROSINE KINASE, OFF-TARGET, SELECTIVE INHIBITOR, HUMAN INTERACTOME",
author = "Felix Meissner and Jennifer Geddes-McAlister and Matthias Mann and Marcus Bantscheff",
year = "2022",
doi = "10.1038/s41573-022-00409-3",
language = "English",
volume = "21",
pages = "637--654",
journal = "Nature Reviews. Drug Discovery",
issn = "1474-1776",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - The emerging role of mass spectrometry-based proteomics in drug discovery

AU - Meissner, Felix

AU - Geddes-McAlister, Jennifer

AU - Mann, Matthias

AU - Bantscheff, Marcus

PY - 2022

Y1 - 2022

N2 - System-wide methods to monitor protein activity are still underused in drug discovery. This Review discusses the potential of proteomics and chemoproteomics approaches for target identification, validation and identification of safety hazards.Proteins are the main targets of most drugs; however, system-wide methods to monitor protein activity and function are still underused in drug discovery. Novel biochemical approaches, in combination with recent developments in mass spectrometry-based proteomics instrumentation and data analysis pipelines, have now enabled the dissection of disease phenotypes and their modulation by bioactive molecules at unprecedented resolution and dimensionality. In this Review, we describe proteomics and chemoproteomics approaches for target identification and validation, as well as for identification of safety hazards. We discuss innovative strategies in early-stage drug discovery in which proteomics approaches generate unique insights, such as targeted protein degradation and the use of reactive fragments, and provide guidance for experimental strategies crucial for success.

AB - System-wide methods to monitor protein activity are still underused in drug discovery. This Review discusses the potential of proteomics and chemoproteomics approaches for target identification, validation and identification of safety hazards.Proteins are the main targets of most drugs; however, system-wide methods to monitor protein activity and function are still underused in drug discovery. Novel biochemical approaches, in combination with recent developments in mass spectrometry-based proteomics instrumentation and data analysis pipelines, have now enabled the dissection of disease phenotypes and their modulation by bioactive molecules at unprecedented resolution and dimensionality. In this Review, we describe proteomics and chemoproteomics approaches for target identification and validation, as well as for identification of safety hazards. We discuss innovative strategies in early-stage drug discovery in which proteomics approaches generate unique insights, such as targeted protein degradation and the use of reactive fragments, and provide guidance for experimental strategies crucial for success.

KW - QUANTITATIVE CHEMICAL PROTEOMICS

KW - PROTEIN-INTERACTION LANDSCAPE

KW - HIGH-THROUGHPUT SCREEN

KW - SMALL-MOLECULE PROBES

KW - TARGET IDENTIFICATION

KW - DEACETYLASE INHIBITORS

KW - TYROSINE KINASE

KW - OFF-TARGET

KW - SELECTIVE INHIBITOR

KW - HUMAN INTERACTOME

U2 - 10.1038/s41573-022-00409-3

DO - 10.1038/s41573-022-00409-3

M3 - Review

C2 - 35351998

VL - 21

SP - 637

EP - 654

JO - Nature Reviews. Drug Discovery

JF - Nature Reviews. Drug Discovery

SN - 1474-1776

ER -

ID: 302544584