Results 51 to 60 of about 255,241 (301)
Targeting Glycosylation: A New Road for Cancer Drug Discovery.
Trends in Cancer, 2020 Cancer is a deadly disease that encompasses numerous cellular modifications. Among them, alterations in glycosylation are a proven reliable hallmark of cancer, with most biomarkers used in the clinic detecting cancer-associated glycans.
Ana Costa, D. Campos, C. Reis, C. Gomes
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Intramolecular glycosylation [PDF]
Beilstein Journal of Organic Chemistry, 2017 Carbohydrate oligomers remain challenging targets for chemists due to the requirement for elaborate protecting and leaving group manipulations, functionalization, tedious purification, and sophisticated characterization. Achieving high stereocontrol in glycosylation reactions is arguably the major hurdle that chemists experience.
Xiao G. Jia, Alexei V. Demchenko
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Linchuang shenzangbing zazhi, 2021 As one of the most important post-translational modifications, glycosylation plays a significant role in the functions of proteins.N-glycosylation exerts critical effects in different biological processes among various forms of glycosylation, whereas ...
任伟夫, 边琪
doaj
Glycosylation: mechanisms, biological functions and clinical implications
Signal Transduction and Targeted TherapyProtein post-translational modification (PTM) is a covalent process that occurs in proteins during or after translation through the addition or removal of one or more functional groups, and has a profound effect on protein function.
Mengyuan He, Xiangxiang Zhou, Xin Wang
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Cold Spring Harbor Perspectives in Biology, 2011 Glycosylation is a very common modification of protein and lipid, and most glycosylation reactions occur in the Golgi. Although the transfer of initial sugar(s) to glycoproteins or glycolipids occurs in the ER or on the ER membrane, the subsequent addition of the many different sugars that make up a mature glycan is accomplished in the Golgi.
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The impact of PD-L1 N-linked glycosylation on cancer therapy and clinical diagnosis
Journal of Biomedical Sciences, 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 +4 more
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Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation
Cells, 2021 The Golgi is the central organelle of the secretory pathway and it houses the majority of the glycosylation machinery, which includes glycosylation enzymes and sugar transporters. Correct compartmentalization of the glycosylation machinery is achieved by
Zinia D’Souza +3 more
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bioRxiv, 2020 The emergence of the COVID-19 pandemic caused by SARS-CoV-2 has created the need for development of new therapeutic strategies. Understanding the mode of viral attachment, entry and replication has become a key aspect of such interventions.
A. Shajahan +5 more
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Molecular Oncology, Volume 20, Issue 6, Page 1591-1611, June 2026.Etoposide induces DNA damage, activating p53‐dependent apoptosis via caspase‐3/7, which cleaves PARP1. Dammarenediol II enhances this apoptotic pathway by suppressing O‐GlcNAc transferase activity, further decreasing O‐GlcNAcylation. The reduction in O‐GlcNAc levels boosts p53‐driven apoptosis and influences the Akt/GSK3β/mTOR signaling pathway ...
Jaehoon Lee +8 more
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FEBS Open Bio, EarlyView.This paper reveals how human lactoferrin–albumin fusion (hLF‐HSA) potently suppresses lung adenocarcinoma cell migration. hLF‐HSA upregulates NHE7, leading to Golgi alkalization, disruption of the Golgi secretome, downregulation of MMP1, and reversal of EMT. These findings suggest a novel Golgi‐targeting strategy to suppress cancer cell migration.
Hana Nopia +3 more
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