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Journal ArticleDOI

Mechanisms and principles of N-linked protein glycosylation.

Flavio Schwarz, +1 more
- 01 Oct 2011 - 
- Vol. 21, Iss: 5, pp 576-582
TLDR
This review discusses the highly conserved processes at the basis of this unique general protein modification system, characterized by a high structural diversity of N-linked glycans found among different species and by a large number of proteins that are glycosylated.
About
This article is published in Current Opinion in Structural Biology.The article was published on 2011-10-01. It has received 595 citations till now. The article focuses on the topics: Glycosylation & Oligosaccharyltransferase.

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Citations
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Journal ArticleDOI

Vertebrate protein glycosylation: diversity, synthesis and function

TL;DR: Improvements in analytical methodologies for dissecting glycan structural diversity, along with recent developments in biochemical and genetic approaches for studying glycan biosynthesis and catabolism have provided a greater understanding of the biological contributions of these complex structures in vertebrates.
Journal ArticleDOI

N-linked protein glycosylation in the ER.

TL;DR: This article summarizes the current knowledge of the N-glycosylation pathway in the ER that results in the covalent attachment of an oligosaccharide to asparagine residues of polypeptide chains and focuses on the model organism Saccharomyces cerevisiae.
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Plant Cell Wall–Degrading Enzymes and Their Secretion in Plant-Pathogenic Fungi

TL;DR: Differences between the CWDE arsenal of plant-pathogenic and non-plant- Pathogenic fungi are discussed, the importance of individual enzyme families for pathogenesis is highlighted, the secretory pathway that transports CWDEs out of the fungal cell is illustrated, and transcriptional regulation of expression of CWDE genes in both saprophytic and phytopathogenic fungi is reported.
Journal ArticleDOI

Mechanisms Controlling PD-L1 Expression in Cancer

TL;DR: Current knowledge of PD-L1 regulatory mechanisms at the transcriptional, posttranscriptional,post-translational, and extracellular levels are provided, and the implications of these findings in cancer diagnosis and immunotherapy are discussed.
References
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Journal ArticleDOI

Precision Mapping of an In Vivo N-Glycoproteome Reveals Rigid Topological and Sequence Constraints

TL;DR: A "filter aided sample preparation" (FASP)-based method in which glycopeptides are enriched by binding to lectins on the top of a filter and mapped 6367 N-glycosylation sites on 2352 proteins in four mouse tissues and blood plasma using high-accuracy mass spectrometry reveals that the sites always orient toward the extracellular space or toward the lumen of ER, Golgi, lysosome, or peroxisome.
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Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites : implications for protein engineering

TL;DR: It is indicated that non-glycosylated sites tend to be found more frequently towards the C termini of glycoproteins, and that proline residues in positions X and Y in the consensus Asn-X-Thr/Ser-Y strongly reduce the likelihood of N-linked glycosylation.
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The dolichol pathway of N-linked glycosylation

TL;DR: It is suggested that N-linked glycosylation in eukaryotes and in archaea share a common evolutionary origin and the function of the lipid carrier dolichol in oligosaccharide assembly is discussed.
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A Genetic Approach to Mammalian Glycan Function

TL;DR: The study of glycans has entered an era of renaissance that coincides with the acquisition of complete genome sequences for multiple organisms and an increased focus upon how posttranslational modifications to protein contribute to the complexity of events mediating normal and disease physiology.
Journal ArticleDOI

Effect of glycosylation on protein folding: A close look at thermodynamic stabilization

TL;DR: A thermodynamic analysis showed that the origin of the enhanced protein stabilization by glycosylation is destabilization of the unfolded state rather than stabilization of the folded state, which is likely to be relevant to other protein polymeric conjugate systems that regularly occur in the cell as posttranslational modifications or for biotechnological purposes.
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