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Metabolic Mimics: The Disorders of N-Linked Glycosylation
Seminars in Pediatric Neurology, 2005N-linked glycosylation is essential for normal cellular function. Defects have now been described in eighteen genes that participate in the process. All give rise to complex multisystem diseases which, with a few exceptions, primarily involve the nervous system.
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N-Linked Protein Glycosylation in a Bacterial System
2009N-Linked protein glycosylation is conserved throughout the three domains of life and influences protein function, stability, and protein complex formation. N-Linked glycosylation is an essential process in Eukaryotes; however, although N-glycosylation affects multiple cellular processes in Archaea and Bacteria, it is not needed for cell survival ...
Harald, Nothaft +3 more
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Regulation of TRP channels by N-linked glycosylation
Seminars in Cell & Developmental Biology, 2006A subset of TRP channel proteins undergoes regulatory N-linked glycosylation. A glycosylation site in the first extracellular loop of TRPV5 is enzymatically cleaved by a secreted glucuronidase, indirectly regulating channel function. Members of the TRPC family share a similar site, although details about a regulatory role are lacking.
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N-Linked Glycosylation of Folded Proteins by the Bacterial Oligosaccharyltransferase
Science, 2006N-linked protein glycosylation is found in all domains of life. In eukaryotes, it is the most abundant protein modification of secretory and membrane proteins, and the process is coupled to protein translocation and folding. We found that in bacteria, N-glycosylation can occur independently of the protein translocation machinery.
Kowarik, Michael +7 more
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Effect of N-linked glycosylation on glycopeptide and glycoprotein structure
Current Opinion in Chemical Biology, 1999Asparagine-linked glycosylation is an enzyme-catalyzed, co-translational protein modification reaction that has the capacity to influence either the protein folding process or the stability of the native glycoprotein conjugate. Advances in both glycoconjugate chemical synthesis and glycoprotein expression methods have increased the availability of ...
Imperiali, B., O'Connor, S.
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Selective killing induced by an inhibitor of n-linked glycosylation
Journal of Cell Science, 1993ABSTRACT Treatment with a low dose (0.5 μg/ml) of tunicamycin (an inhibitor of N-linked glycosylation) blocked the cell cycle progression of both normal Balb/c 3T3 cells (A31) and their SV40-transformed derivatives (SVA31) specifically in early G1 (0-3 h after mitosis).
O, Larsson, M, Carlberg, A, Zetterberg
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Studying N-Linked Glycosylation of Receptor Tyrosine Kinases
2014Metabolic alterations have been identified as a frequent event in cancer. This is often associated with increased flux through glycolysis, and also a secondary pathway to glycolysis, hexosamine biosynthetic pathway (HBP). HBP provides substrate for N-linked glycosylation, which occurs in the endoplasmic reticulum and the Golgi apparatus.
Itkonen, Harri M, Mills, Ian G
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N-linked glycosylation of the C5a receptor.
Biochemistry and molecular biology international, 1994The recent cloning of the cDNA encoding the human C5a receptor reveals a single potential site for N-linked glycosylation. Previous studies have suggested the presence of at least one carbohydrate moiety in the C5a receptor. Enzymatic digestion with Endoglycosidase F confirmed this presence and a point mutation at the predicted site of glycosylation ...
J E, Pease, M D, Barker
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The conformational effects of N-linked glycosylation
Biochemical Society Transactions, 1993C J, Edge +3 more
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Structural Insight into the Mechanism of N-Linked Glycosylation by Oligosaccharyltransferase
Biomolecules, 2020Smita Mohanty
exaly