Results 11 to 20 of about 13,659,719 (307)

N-glycosylation in sugarcane

Genetics and Molecular Biology, 2001
The N-linked glycosylation of secretory and membrane proteins is the most complex posttranslational modification known to occur in eukaryotic cells. It has been shown to play critical roles in modulating protein function.
Maia Ivan G., Leite Adilson
doaj   +5 more sources

Disruption of spike protein N-glycosylation induces its endoplasmic reticulum retention and attenuates SARS-CoV-2 infectivity [PDF]

Journal of Virology
The spike (S) protein of SARS-CoV-2 is extensively glycosylated, with N-glycosylation sites remaining highly conserved during viral evolution. While inhibiting N-glycosylation has been shown to significantly suppress SARS-CoV-2 infection, the underlying ...
Weili Kong, Jiali Zhang, Yingying Song, Jingjing Song, Yuebo Xu, Xinmu Xu, Haoyu Ma, Li Chen, Cong Zeng   +8 more
doaj   +2 more sources

Platelets and Defective N-Glycosylation [PDF]

International Journal of Molecular Sciences, 2020
N-glycans are covalently linked to an asparagine residue in a simple acceptor sequence of proteins, called a sequon. This modification is important for protein folding, enhancing thermodynamic stability, and decreasing abnormal protein aggregation within the endoplasmic reticulum (ER), for the lifetime and for the subcellular localization of proteins ...
Mammadova-Bach, Elmina, Jaeken, Jaak, Gudermann, Thomas, Braun, Attila   +3 more
openaire   +2 more sources

N-Glycosylation at Asn291 Stabilizes TIM-4 and Promotes the Metastasis of NSCLC

Frontiers in Oncology, 2022
T-cell immunoglobulin domain and mucin domain 4 (TIM-4) is a transmembrane protein that promotes epithelial-mesenchymal transition (EMT), migration and invasion of non-small cell lung cancer (NSCLC) cells.
Siyuan Chen, Yuzhen Wang, Wen Liu, Yan Liang, Yingchun Wang, Zhuanchang Wu, Liyun Xu, Xiaohong Liang, Chunhong Ma, Lifen Gao   +9 more
doaj   +1 more source

The essential endoplasmic reticulum chaperone Rot1 is required for protein N- and O-glycosylation in yeast [PDF]

, 2012
Rot1 is an essential yeast protein originally shown to be implicated in such diverse processes such as β-1,6-glucan synthesis, actin cytoskeleton dynamics, or lysis of autophagic bodies.
Lehle, L., Palamarczyk, G., Palamarczyk, Grazyna, Pasikowska, M., Pasikowska, Monika, Grazyna Palamarczyk, Monika Pasikowska, Ludwig Lehle, Lehle, Ludwig   +8 more
core   +2 more sources

Glycosylation of viral proteins: Implication in virus–host interaction and virulence

Virulence, 2022
Glycans are among the most important cell molecular components. However, given their structural diversity, their functions have not been fully explored. Glycosylation is a vital post-translational modification for various proteins.
Tingting Feng, Jinyu Zhang, Zhiqian Chen, Wen Pan, Zhengrong Chen, Yongdong Yan, Jianfeng Dai   +6 more
doaj   +1 more source

N-GlycoGo: Predicting Protein N-Glycosylation Sites on Imbalanced Data Sets by Using Heterogeneous and Comprehensive Strategy

IEEE Access, 2020
Glycosylation is the most complex post-modification effect of proteins. It participates in many biological processes in the human body and is closely related to many disease states.
Ching-Hsuan Chien, Chi-Chang Chang, Shih-Huan Lin, Chi-Wei Chen, Zong-Han Chang, Yen-Wei Chu   +5 more
doaj   +1 more source

DeepNGlyPred: A Deep Neural Network-Based Approach for Human N-Linked Glycosylation Site Prediction

Molecules, 2021
Protein N-linked glycosylation is a post-translational modification that plays an important role in a myriad of biological processes. Computational prediction approaches serve as complementary methods for the characterization of glycosylation sites. Most
Subash C. Pakhrin, Kiyoko F. Aoki-Kinoshita, Doina Caragea, Dukka B. KC   +3 more
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Influence of N-Glycosylation on Virus–Host Interactions in Halorubrum lacusprofundi

Viruses, 2023
N-glycosylation is a post-translational modification of proteins that occurs across all three domains of life. In Archaea, N-glycosylation is crucial for cell stability and motility, but importantly also has significant implications for virus–host ...
L. Johanna Gebhard, Zlata Vershinin, Tomás Alarcón-Schumacher, Jerry Eichler, Susanne Erdmann   +4 more
doaj   +1 more source

GlypNirO: An automated workflow for quantitative N- and O-linked glycoproteomic data analysis

Beilstein Journal of Organic Chemistry, 2020
Mass spectrometry glycoproteomics is rapidly maturing, allowing unprecedented insights into the diversity and functions of protein glycosylation. However, quantitative glycoproteomics remains challenging.
Toan K. Phung, Cassandra L. Pegg, Benjamin L. Schulz   +2 more
doaj   +1 more source