Enrichments of post-translational modifications in proteomic studies

Luisa Pieroni, Federica Iavarone, Alessandra Olianas, Viviana Greco, Claudia Desiderio, Claudia Martelli, Barbara Manconi, Maria Teresa Sanna, Irene Messana, Massimo Castagnola, Tiziana Cabras

Research output: Contribution to journalReview article

Abstract

More than 300 different protein post-translational modifications are currently known, but only a few have been extensively investigated because modified proteoforms are commonly present in sub-stoichiometry amount. For this reason, improvement of specific enrichment techniques is particularly useful for the proteomic characterization of post-translationally modified proteins. Enrichment proteomic strategies could help the researcher in the challenging issue to decipher the complex molecular cross-talk existing between the different factors influencing the cellular pathways. In this review the state of art of the platforms applied for the enrichment of specific and most common post-translational modifications, such as glycosylation and glycation, phosphorylation, sulfation, redox modifications (i.e. sulfydration and nitrosylation), methylation, acetylation, and ubiquitinylation, are described. Enrichments strategies applied to characterize less studied post-translational modifications are also briefly discussed.

Original languageEnglish
JournalJournal of Separation Science
DOIs
Publication statusAccepted/In press - Jan 1 2019

Fingerprint

Glycosylation
Proteins
Acetylation
Phosphorylation
Methylation
Stoichiometry
Proteomics
Oxidation-Reduction

Keywords

  • enrichment
  • post-translational modifications
  • proteomics

ASJC Scopus subject areas

  • Analytical Chemistry
  • Filtration and Separation

Cite this

Pieroni, L., Iavarone, F., Olianas, A., Greco, V., Desiderio, C., Martelli, C., ... Cabras, T. (Accepted/In press). Enrichments of post-translational modifications in proteomic studies. Journal of Separation Science. https://doi.org/10.1002/jssc.201900804

Enrichments of post-translational modifications in proteomic studies. / Pieroni, Luisa; Iavarone, Federica; Olianas, Alessandra; Greco, Viviana; Desiderio, Claudia; Martelli, Claudia; Manconi, Barbara; Sanna, Maria Teresa; Messana, Irene; Castagnola, Massimo; Cabras, Tiziana.

In: Journal of Separation Science, 01.01.2019.

Research output: Contribution to journalReview article

Pieroni, L, Iavarone, F, Olianas, A, Greco, V, Desiderio, C, Martelli, C, Manconi, B, Sanna, MT, Messana, I, Castagnola, M & Cabras, T 2019, 'Enrichments of post-translational modifications in proteomic studies', Journal of Separation Science. https://doi.org/10.1002/jssc.201900804
Pieroni L, Iavarone F, Olianas A, Greco V, Desiderio C, Martelli C et al. Enrichments of post-translational modifications in proteomic studies. Journal of Separation Science. 2019 Jan 1. https://doi.org/10.1002/jssc.201900804
Pieroni, Luisa ; Iavarone, Federica ; Olianas, Alessandra ; Greco, Viviana ; Desiderio, Claudia ; Martelli, Claudia ; Manconi, Barbara ; Sanna, Maria Teresa ; Messana, Irene ; Castagnola, Massimo ; Cabras, Tiziana. / Enrichments of post-translational modifications in proteomic studies. In: Journal of Separation Science. 2019.
@article{024c18712aa64c73b2c2e618262db54c,
title = "Enrichments of post-translational modifications in proteomic studies",
abstract = "More than 300 different protein post-translational modifications are currently known, but only a few have been extensively investigated because modified proteoforms are commonly present in sub-stoichiometry amount. For this reason, improvement of specific enrichment techniques is particularly useful for the proteomic characterization of post-translationally modified proteins. Enrichment proteomic strategies could help the researcher in the challenging issue to decipher the complex molecular cross-talk existing between the different factors influencing the cellular pathways. In this review the state of art of the platforms applied for the enrichment of specific and most common post-translational modifications, such as glycosylation and glycation, phosphorylation, sulfation, redox modifications (i.e. sulfydration and nitrosylation), methylation, acetylation, and ubiquitinylation, are described. Enrichments strategies applied to characterize less studied post-translational modifications are also briefly discussed.",
keywords = "enrichment, post-translational modifications, proteomics",
author = "Luisa Pieroni and Federica Iavarone and Alessandra Olianas and Viviana Greco and Claudia Desiderio and Claudia Martelli and Barbara Manconi and Sanna, {Maria Teresa} and Irene Messana and Massimo Castagnola and Tiziana Cabras",
year = "2019",
month = "1",
day = "1",
doi = "10.1002/jssc.201900804",
language = "English",
journal = "Journal of Separation Science",
issn = "1615-9306",
publisher = "Wiley-VCH Verlag",

}

TY - JOUR

T1 - Enrichments of post-translational modifications in proteomic studies

AU - Pieroni, Luisa

AU - Iavarone, Federica

AU - Olianas, Alessandra

AU - Greco, Viviana

AU - Desiderio, Claudia

AU - Martelli, Claudia

AU - Manconi, Barbara

AU - Sanna, Maria Teresa

AU - Messana, Irene

AU - Castagnola, Massimo

AU - Cabras, Tiziana

PY - 2019/1/1

Y1 - 2019/1/1

N2 - More than 300 different protein post-translational modifications are currently known, but only a few have been extensively investigated because modified proteoforms are commonly present in sub-stoichiometry amount. For this reason, improvement of specific enrichment techniques is particularly useful for the proteomic characterization of post-translationally modified proteins. Enrichment proteomic strategies could help the researcher in the challenging issue to decipher the complex molecular cross-talk existing between the different factors influencing the cellular pathways. In this review the state of art of the platforms applied for the enrichment of specific and most common post-translational modifications, such as glycosylation and glycation, phosphorylation, sulfation, redox modifications (i.e. sulfydration and nitrosylation), methylation, acetylation, and ubiquitinylation, are described. Enrichments strategies applied to characterize less studied post-translational modifications are also briefly discussed.

AB - More than 300 different protein post-translational modifications are currently known, but only a few have been extensively investigated because modified proteoforms are commonly present in sub-stoichiometry amount. For this reason, improvement of specific enrichment techniques is particularly useful for the proteomic characterization of post-translationally modified proteins. Enrichment proteomic strategies could help the researcher in the challenging issue to decipher the complex molecular cross-talk existing between the different factors influencing the cellular pathways. In this review the state of art of the platforms applied for the enrichment of specific and most common post-translational modifications, such as glycosylation and glycation, phosphorylation, sulfation, redox modifications (i.e. sulfydration and nitrosylation), methylation, acetylation, and ubiquitinylation, are described. Enrichments strategies applied to characterize less studied post-translational modifications are also briefly discussed.

KW - enrichment

KW - post-translational modifications

KW - proteomics

UR - http://www.scopus.com/inward/record.url?scp=85074774230&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85074774230&partnerID=8YFLogxK

U2 - 10.1002/jssc.201900804

DO - 10.1002/jssc.201900804

M3 - Review article

C2 - 31631532

AN - SCOPUS:85074774230

JO - Journal of Separation Science

JF - Journal of Separation Science

SN - 1615-9306

ER -