Misincorporation Proteomics Technologies: A Review

Overview

Journal Proteomes

Date 2021 Jan 26

PMID 33494504

Citations 3

Authors

Joel R Steele

Carly J Italiano

Connor R Phillips

Jake P Violi

Lisa Pu

Kenneth J Rodgers

Matthew P Padula

Affiliations

Soon will be listed here.

Abstract

Proteinopathies are diseases caused by factors that affect proteoform conformation. As such, a prevalent hypothesis is that the misincorporation of noncanonical amino acids into a proteoform results in detrimental structures. However, this hypothesis is missing proteomic evidence, specifically the detection of a noncanonical amino acid in a peptide sequence. This review aims to outline the current state of technology that can be used to investigate mistranslations and misincorporations whilst framing the pursuit as Misincorporation Proteomics (MiP). The current availability of technologies explored herein is mass spectrometry, sample enrichment/preparation, data analysis techniques, and the hyphenation of approaches. While many of these technologies show potential, our review reveals a need for further development and refinement of approaches is still required.

Citing Articles

Correction: Steele et al. Misincorporation Proteomics Technologies: A Review. 2021, , 2.

Steele J, Italiano C, Phillips C, Violi J, Pu L, Rodgers K Proteomes. 2022; 10(2).

PMID: 35736802 PMC: 9227081. DOI: 10.3390/proteomes10020022.

Azetidine-2-Carboxylic Acid-Induced Oligodendrogliopathy: Relevance to the Pathogenesis of Multiple Sclerosis.

Sobel R, Albertelli M, Hinojoza J, Eaton M, Grimes K, Rubenstein E J Neuropathol Exp Neurol. 2022; 81(6):414-433.

PMID: 35521963 PMC: 9123080. DOI: 10.1093/jnen/nlac028.

A Novel Method for Creating a Synthetic L-DOPA Proteome and In Vitro Evidence of Incorporation.

Steele J, Strange N, Rodgers K, Padula M Proteomes. 2021; 9(2).

PMID: 34073856 PMC: 8162537. DOI: 10.3390/proteomes9020024.

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