Results 31 to 40 of about 15,085,302 (278)

Proteome and Glycoproteome Analyses Reveal the Protein N-Linked Glycosylation Specificity of STT3A and STT3B [PDF]

Cells, 2022
Ganglong Yang, Morihisa Fujita, Xiaodong Gao   +2 more
exaly   +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

NS1 Protein N-Linked Glycosylation Site Affects the Virulence and Pathogenesis of Dengue Virus [PDF]

Vaccines, 2023
Yuhua Li, Enyue Fang, Miao Li
exaly   +2 more sources

N-linked glycosylation enzymes in the diatom Thalassiosira oceanica exhibit a diel cycle in transcript abundance and favor for NXT-type sites

Scientific Reports, 2021
N-linked glycosylation is a posttranslational modification affecting protein folding and function. The N-linked glycosylation pathway in algae is poorly characterized, and further knowledge is needed to understand the cell biology of algae and the ...
Joerg Behnke, Alejandro M. Cohen, Julie LaRoche   +2 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

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

Store-Operated Calcium Entry in Breast Cancer Cells Is Insensitive to Orai1 and STIM1 N-Linked Glycosylation. [PDF]

Cancers (Basel), 2022
N-linked glycosylation is a post-translational modification that affects protein function, structure, and interaction with other proteins. The store-operated Ca2+ entry (SOCE) core proteins, Orai1 and STIM1, exhibit N-glycosylation consensus motifs ...
Sanchez-Collado J, Nieto-Felipe J, Jardin I, Bhardwaj R, Berna-Erro A, Salido GM, Smani T, Hediger MA, Lopez JJ, Rosado JA.   +9 more
europepmc   +3 more sources

The impact of PD-L1 N-linked glycosylation on cancer therapy and clinical diagnosis

Journal of Biomedical Science, 2020
N-linked glycosylation is one of the most abundant posttranslational modifications of membrane-bound proteins in eukaryotes and affects a number of biological activities, including protein biosynthesis, protein stability, intracellular trafficking ...
Ying-Nai Wang, Heng-Huan Lee, Jennifer L. Hsu, Dihua Yu, Mien-Chie Hung   +4 more
doaj   +1 more source

Modified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations

Communications Biology, 2021
Li et al. investigates the role of N-linked glycosylation for the function of mechanosensitive ion channel Piezo1. They show that disease-linked loss of function mutations in Piezo1 that are trafficking defective lack N-linked glycosylation.
Jinyuan Vero Li, Chai-Ann Ng, Delfine Cheng, Zijing Zhou, Mingxi Yao, Yang Guo, Ze-Yan Yu, Yogambha Ramaswamy, Lining Arnold Ju, Philip W. Kuchel, Michael P. Feneley, Diane Fatkin, Charles D. Cox   +12 more
doaj   +1 more source

SRD5A3 is required for converting polyprenol to dolichol and is mutated in a congenital glycosylation disorder. [PDF]

, 2010
N-linked glycosylation is the most frequent modification of secreted and membrane-bound proteins in eukaryotic cells, disruption of which is the basis of the congenital disorders of glycosylation (CDGs).
Hudson H. Freeze, Silhavy, J.L., Christian R.H. Raetz, Al-Gazali, Lihadh, Swistun, Dominika, Dusica Babovic-Vuksanovic, Guan, Z., Blümel, Peter, Sykut-Cegielska, J., Hans van Bokhoven, Bokhoven, J.H.L.M. van, Ludwig Lehle, Lehle, Ludwig, Wevers, R.A., Al-Gazali, L., Houliston, S., Dobyns, W.B., Bassam R. Ali, Lefeber, D.J., Ali, Bassam R., Raetz, Christian R.H., Dirk J. Lefeber, Guan, Ziqiang, Ron A. Wevers, Hans Hombauer, Maciej Adamowicz, Jolanta Sykut-Cegielska, Stephanie L. Bielas, Ng, B.G., Freeze, H.H., Ewa Swiezewska, Wevers, Ron A., William B. Dobyns, Gleeson, Joseph G., Bobby G. Ng, Cantagrel, Vincent, Ng, Bobby G., Swiezewska, Ewa, Lefeber, Dirk J., De Brouwer, Arjan P., Houliston, Scott, Adamowicz, M., Silhavy, Jennifer L., Lihadh Al-Gazali, Ziqiang Guan, Éva Morava, Dobyns, William B., Adamowicz, Maciej, Morava, E., Babovic-Vuksanovic, Dusica, Raetz, C.R., Vincent Cantagrel, Lehle, L., Hombauer, H., Scott Houliston, Freeze, Hudson H., Jennifer L. Silhavy, Swistun, D., Blumel, P., Babovic-Vuksanovic, D., Cantagrel, V., Gleeson, J.G., Peter Blümel, Sykut-Cegielska, Jolanta, Arjan P. De Brouwer, Morava, Éva, Joseph G. Gleeson, Brouwer, A.P.M. de, van Bokhoven, Hans, Swiezewska, E., Hombauer, Hans, Dominika Swistun, Bielas, S.L., Ali, B.R., Bielas, Stephanie L.   +74 more
core   +2 more sources