Results 11 to 20 of about 162,600 (208)

Global identification of prokaryotic glycoproteins based on an Escherichia coli proteome microarray. [PDF]

PLoS ONE, 2012
Glycosylation is one of the most abundant protein posttranslational modifications. Protein glycosylation plays important roles not only in eukaryotes but also in prokaryotes.
Zong-Xiu Wang, Rui-Ping Deng, He-Wei Jiang, Shu-Juan Guo, Huang-Ying Le, Xiao-Dong Zhao, Chien-Sheng Chen, Ji-Bin Zhang, Sheng-Ce Tao   +8 more
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N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence.

PLoS Pathogens, 2019
Fungal pathogenesis depends on accurate secretion and location of virulence factors which drive host colonization. Protein glycosylation is a common posttranslational modification of cell wall components and other secreted factors, typically required for
Miriam Marín-Menguiano, Ismael Moreno-Sánchez, Ramón R Barrales, Alfonso Fernández-Álvarez, José Ignacio Ibeas   +4 more
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DC-SIGN Binding Contributed by an Extra N-Linked Glycosylation on Japanese Encephalitis Virus Envelope Protein Reduces the Ability of Viral Brain Invasion

Frontiers in Cellular and Infection Microbiology, 2018
The major structural envelope (E) protein of Japanese encephalitis virus (JEV) facilitates cellular binding/entry and is the primary target of neutralizing antibodies.
Jian-Jong Liang, Min-Wei Chou, Yi-Ling Lin, Yi-Ling Lin   +3 more
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Quantitative Analyses Reveal Novel Roles for N-Glycosylation in a Major Enteric Bacterial Pathogen

mBio, 2019
In eukaryotes, glycosylation plays a role in proteome stability, protein quality control, and modulating protein function; however, similar studies in bacteria are lacking.
Sherif Abouelhadid, Simon J. North, Paul Hitchen, Prerna Vohra, Cosmin Chintoan-Uta, Mark Stevens, Anne Dell, Jon Cuccui, Brendan W. Wren   +8 more
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Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host

Journal of Fungi, 2021
Protein glycosylation is a highly conserved post-translational modification among organisms. It plays fundamental roles in many biological processes, ranging from protein trafficking and cell adhesion to host–pathogen interactions. According to the amino
Manuela Gómez-Gaviria, Ana P. Vargas-Macías, Laura C. García-Carnero, Iván Martínez-Duncker, Héctor M. Mora-Montes   +4 more
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Effects of N-Glycosylation on the Structure, Function, and Stability of a Plant-Made Fc-Fusion Anthrax Decoy Protein

Frontiers in Plant Science, 2019
Protein N-glycosylation is an important post-translational modification and has influences on a variety of biological processes at the cellular and molecular level, making glycosylation a major study aspect for glycoprotein-based therapeutics. To achieve
Yongao Xiong, Kalimuthu Karuppanan, Austen Bernardi, Qiongyu Li, Vally Kommineni, Abhaya M. Dandekar, Carlito B. Lebrilla, Carlito B. Lebrilla, Roland Faller, Karen A. McDonald, Karen A. McDonald, Somen Nandi, Somen Nandi   +12 more
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Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes

Molecular Systems Biology, 2009
To further understand the roles of protein glycosylation in eukaryotes, we globally identified glycan‐containing proteins in yeast. A fluorescent lectin binding assay was developed and used to screen protein microarrays containing over 5000 proteins ...
Li A Kung, Sheng‐Ce Tao, Jiang Qian, Michael G Smith, Michael Snyder, Heng Zhu   +5 more
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N-Glycosylation can selectively block or foster different receptor–ligand binding modes

Scientific Reports, 2021
While DNA encodes protein structure, glycans provide a complementary layer of information to protein function. As a prime example of the significance of glycans, the ability of the cell surface receptor CD44 to bind its ligand, hyaluronan, is modulated ...
Joni Vuorio, Jana Škerlová, Milan Fábry, Václav Veverka, Ilpo Vattulainen, Pavlína Řezáčová, Hector Martinez-Seara   +6 more
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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
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O-glycosylation of SARS-CoV-2 spike protein by host O-glycosyltransferase strengthens its trimeric structure

Acta Biochimica et Biophysica Sinica
Protein O-glycosylation, also known as mucin-type O-glycosylation, is one of the most abundant glycosylation in mammalian cells. It is initially catalyzed by a family of polypeptide GalNAc transferases (ppGalNAc-Ts).
Xu Zhijue, Zhang Han, Tian Jiaqi, Ku Xin, Wei Rumeng, Hou Jingli, Zhang Can, Yang Fang, Zou Xia, Li Yang, Kaji Hiroyuki, Tao Sheng-Ce, Kuno Atsushi, Yan Wei, Da Lin-Tai, Zhang Yan   +15 more
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