Results 21 to 30 of about 14,762,033 (298)
Prediction Of O-Glycosylation Site Using Pre-Trained Language Model And Machine Learning [PDF]
International Journal of Intelligent Computing and Information Sciences, 2023 O-glycosylation is a typical type of protein post-translational modifications (PTMs), which is linked to several diseases and has significant roles in many biological processes.
Alhasan Alkuhlani +3 more
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Sugar Type Discrimination in O-glycosylation Based on Protein Primary Sequences
Journal of Biomechanical Science and Engineering, 2013 Glycosylation is one of the most important protein post-translational modifications. O-glycosylation plays important roles in biological functions. There are several variations of O-glycosylation, with each having a different function.
Kenji ETCHUYA, Yuri MUKAI
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Frontiers in Physiology, 2021 Protein glycosylation is one of the most common and most important post-translational modifications. Despite the growing knowledge on N-glycosylation, the research on O-glycosylation is lagging behind.
Weidong Li +4 more
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A Chemoenzymatic Strategy toward Understanding O-GlcNAc Glycosylation in the Brain [PDF]
, 2007 Posttranslational modification to proteins represents a fundamental mechanism by which protein function is extended and elaborated. In the brain, modifications such as phosphorylation play critical roles in mediating neuronal communication and ...
Khidekel, Nelly
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O-glycosylation disorders pave the road for understanding the complex human O-glycosylation machinery [PDF]
Current Opinion in Structural Biology, 2019 Over 100 human Congenital Disorders of Glycosylation (CDG) have been described. Of these, about 30% reside in the O-glycosylation pathway. O-glycosylation disorders are characterized by a high phenotypic variability, reflecting the large diversity of O-glycan structures.
van Tol, W. +4 more
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Di-san junyi daxue xuebao, 2019 Objective To investigate the effect of β-N-acetylglucosamine (GlcNAc) on the mitogen-activated protein kinases (MAPKs) pathway in rat penile cavernosum smooth muscle cells.
LIU Boshen +3 more
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Frontiers in Plant Science, 2021 Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and ...
Richard Strasser +12 more
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Analysis of N-Glycosylation Sites in HIV glycoprotein 160 [PDF]
, 2011 HIV infection is a condition caused by the human immunodeficiency virus. The condition gradually destroys the immune system, which makes it harder for the body to fight infections. HIV presents a complex knot for scientists to unravel.
Rajendra Mandage
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O-Glycosylation of the V2 vasopressin receptor [PDF]
Glycobiology, 1999 The human V2 vasopressin receptor contains one consensus site for N-linked glycosylation at asparagine 22 in the predicted extracellular amino terminal segment of the protein. This segment also contains clusters of serines and threonines that are potential sites for O-glycosylation.
H, Sadeghi, M, Birnbaumer
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Protein glycosylation in the gram-negative gamma proteobacterium photorhabdus luminescens [PDF]
, 2011 The objective of this research was to investigate the possibility that Photorhabdus luminescens produces glycoproteins and thus contains a protein glycosylation system. P. luminescens is a pathogen of insects and a symbiont of soil nematodes.
Fox, Mary
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