Biochimica et Biophysica Acta - General Subjects, volume 1861, issue 12, pages 3096-3108
Unusual glycosylation of proteins: Beyond the universal sequon and other amino acids
Publication type: Journal Article
Publication date: 2017-12-01
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor: 3
ISSN: 00063002, 03044165, 18728006
Biochemistry
Molecular Biology
Biophysics
Abstract
Glycosylation of proteins is the most common, multifaceted co- and post-translational modification responsible for many biological processes and cellular functions. Significant alterations and aberrations of these processes are related to various pathological conditions, and often turn out to be disease biomarkers. Conventional N-glycosylation occurs through the recognition of the consensus sequon, asparagine (Asn)-X-serine (Ser)/threonine (Thr), where X is any amino acid except for proline, with N-acetylglucosamine (GlcNAc) as the first glycosidic linkage. Usually, O-glycosylation adds a glycan to the hydroxyl group of Ser or Thr beginning with N-acetylgalactosamine (GalNAc).Protein glycosylation is further governed by additional diversifications in sequon and structure, which are yet to be fully explored. This review mainly focuses on the occurrence of N-glycosylation in non-consensus motifs, where Ser/Thr at the +2 position is substituted by other amino acids. Additionally, N-glycosylation is also observed in other amide/amine group-containing amino acids. Similarly, O-glycosylation occurs at hydroxyl group-containing amino acids other than serine/threonine. The neighbouring amino acids and local structural features around the potential glycosylation site also play a significant role in determining the extent of glycosylation. All of these phenomena that yield glycosylation at the atypical sites are reported in a variety of biological systems, including different pathological conditions.Therefore, the discovery of more novel sequence patterns for N- and O-glycosylation may help in understanding the functions of complex biological processes and cellular functions. Taken together, all these information provided in this review would be helpful for the biological readers.
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Dutta D., MANDAL C. Unusual glycosylation of proteins: Beyond the universal sequon and other amino acids // Biochimica et Biophysica Acta - General Subjects. 2017. Vol. 1861. No. 12. pp. 3096-3108.
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Dutta D., MANDAL C. Unusual glycosylation of proteins: Beyond the universal sequon and other amino acids // Biochimica et Biophysica Acta - General Subjects. 2017. Vol. 1861. No. 12. pp. 3096-3108.
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TY - JOUR
DO - 10.1016/j.bbagen.2017.08.025
UR - https://doi.org/10.1016%2Fj.bbagen.2017.08.025
TI - Unusual glycosylation of proteins: Beyond the universal sequon and other amino acids
T2 - Biochimica et Biophysica Acta - General Subjects
AU - Dutta, Devawati
AU - MANDAL, CHHABINATH
PY - 2017
DA - 2017/12/01 00:00:00
PB - Elsevier
SP - 3096-3108
IS - 12
VL - 1861
SN - 0006-3002
SN - 0304-4165
SN - 1872-8006
ER -
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@article{2017_Dutta,
author = {Devawati Dutta and CHHABINATH MANDAL},
title = {Unusual glycosylation of proteins: Beyond the universal sequon and other amino acids},
journal = {Biochimica et Biophysica Acta - General Subjects},
year = {2017},
volume = {1861},
publisher = {Elsevier},
month = {dec},
url = {https://doi.org/10.1016%2Fj.bbagen.2017.08.025},
number = {12},
pages = {3096--3108},
doi = {10.1016/j.bbagen.2017.08.025}
}
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Dutta, Devawati, and CHHABINATH MANDAL. “Unusual glycosylation of proteins: Beyond the universal sequon and other amino acids.” Biochimica et Biophysica Acta - General Subjects, vol. 1861, no. 12, Dec. 2017, pp. 3096-3108. https://doi.org/10.1016%2Fj.bbagen.2017.08.025.