Quantitative characterization of O-GalNAc glycosylation

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Standard

Quantitative characterization of O-GalNAc glycosylation. / Čaval, Tomislav; de Haan, Noortje; Konstantinidi, Andriana; Vakhrushev, Sergey Y.

I: Current Opinion in Structural Biology, Bind 68, 2021, s. 135-141.

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Harvard

Čaval, T, de Haan, N, Konstantinidi, A & Vakhrushev, SY 2021, 'Quantitative characterization of O-GalNAc glycosylation', Current Opinion in Structural Biology, bind 68, s. 135-141. https://doi.org/10.1016/j.sbi.2020.12.010

APA

Čaval, T., de Haan, N., Konstantinidi, A., & Vakhrushev, S. Y. (2021). Quantitative characterization of O-GalNAc glycosylation. Current Opinion in Structural Biology, 68, 135-141. https://doi.org/10.1016/j.sbi.2020.12.010

Vancouver

Čaval T, de Haan N, Konstantinidi A, Vakhrushev SY. Quantitative characterization of O-GalNAc glycosylation. Current Opinion in Structural Biology. 2021;68:135-141. https://doi.org/10.1016/j.sbi.2020.12.010

Author

Čaval, Tomislav ; de Haan, Noortje ; Konstantinidi, Andriana ; Vakhrushev, Sergey Y. / Quantitative characterization of O-GalNAc glycosylation. I: Current Opinion in Structural Biology. 2021 ; Bind 68. s. 135-141.

Bibtex

@article{24329fd9628a4e5e981832fbaf96ee75,
title = "Quantitative characterization of O-GalNAc glycosylation",
abstract = "O-GalNAc type glycosylation is an abundant and complex protein modification. Recent developments in mass spectrometry resulted in significant success in quantitative analysis of O-GalNAc glycosylation. The analysis of released O-GalNAc type glycans expanded our horizons of understanding the glycome of various biological models. The site-specific analysis of glycosylation micro-heterogeneity of purified proteins opened perspectives for the improved design of glycoprotein therapeutics. Advanced gene editing and chemical technologies applied to O-glycoproteomics enabled to identify O-GalNAc glycosylation at unprecedented depth. Progress in the analysis of intact glycoproteins under native and reduced conditions enabled the monitoring of glycosylation proteoform variants. Despite of the astonishing results in quantitative O-GalNAc glycoproteomics, site-specific mapping of the full O-GalNAc structural repertoire in complex samples is yet a long way off. Here, we summarize the most common quantitative strategies in O-GalNAc glycoproteomics, review recent progress and discuss benefits and limitations of the various approaches in the field.",
author = "Tomislav {\v C}aval and {de Haan}, Noortje and Andriana Konstantinidi and Vakhrushev, {Sergey Y.}",
note = "Publisher Copyright: {\textcopyright} 2021 Elsevier Ltd",
year = "2021",
doi = "10.1016/j.sbi.2020.12.010",
language = "English",
volume = "68",
pages = "135--141",
journal = "Current Opinion in Structural Biology",
issn = "0959-440X",
publisher = "Elsevier Ltd. * Current Opinion Journals",

}

RIS

TY - JOUR

T1 - Quantitative characterization of O-GalNAc glycosylation

AU - Čaval, Tomislav

AU - de Haan, Noortje

AU - Konstantinidi, Andriana

AU - Vakhrushev, Sergey Y.

N1 - Publisher Copyright: © 2021 Elsevier Ltd

PY - 2021

Y1 - 2021

N2 - O-GalNAc type glycosylation is an abundant and complex protein modification. Recent developments in mass spectrometry resulted in significant success in quantitative analysis of O-GalNAc glycosylation. The analysis of released O-GalNAc type glycans expanded our horizons of understanding the glycome of various biological models. The site-specific analysis of glycosylation micro-heterogeneity of purified proteins opened perspectives for the improved design of glycoprotein therapeutics. Advanced gene editing and chemical technologies applied to O-glycoproteomics enabled to identify O-GalNAc glycosylation at unprecedented depth. Progress in the analysis of intact glycoproteins under native and reduced conditions enabled the monitoring of glycosylation proteoform variants. Despite of the astonishing results in quantitative O-GalNAc glycoproteomics, site-specific mapping of the full O-GalNAc structural repertoire in complex samples is yet a long way off. Here, we summarize the most common quantitative strategies in O-GalNAc glycoproteomics, review recent progress and discuss benefits and limitations of the various approaches in the field.

AB - O-GalNAc type glycosylation is an abundant and complex protein modification. Recent developments in mass spectrometry resulted in significant success in quantitative analysis of O-GalNAc glycosylation. The analysis of released O-GalNAc type glycans expanded our horizons of understanding the glycome of various biological models. The site-specific analysis of glycosylation micro-heterogeneity of purified proteins opened perspectives for the improved design of glycoprotein therapeutics. Advanced gene editing and chemical technologies applied to O-glycoproteomics enabled to identify O-GalNAc glycosylation at unprecedented depth. Progress in the analysis of intact glycoproteins under native and reduced conditions enabled the monitoring of glycosylation proteoform variants. Despite of the astonishing results in quantitative O-GalNAc glycoproteomics, site-specific mapping of the full O-GalNAc structural repertoire in complex samples is yet a long way off. Here, we summarize the most common quantitative strategies in O-GalNAc glycoproteomics, review recent progress and discuss benefits and limitations of the various approaches in the field.

U2 - 10.1016/j.sbi.2020.12.010

DO - 10.1016/j.sbi.2020.12.010

M3 - Review

C2 - 33508547

AN - SCOPUS:85099838649

VL - 68

SP - 135

EP - 141

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

SN - 0959-440X

ER -

ID: 299205078