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Nucleocytoplasmic O-glycosylation in protists

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TLDR
Cellular roles of nucleocytoplasmic glycans are interpreted in terms of current evidence for their effects on the conformation and dynamics of protist proteins, to serve as a guide for future studies to examine their broader significance.
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This article is published in Current Opinion in Structural Biology.The article was published on 2019-05-22 and is currently open access. It has received 13 citations till now. The article focuses on the topics: Glycosylation.

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Journal ArticleDOI

Demystifying the O-GlcNAc Code: A Systems View.

Junfeng Ma, +2 more
- 18 Mar 2022 - 
TL;DR: A comprehensive survey of O-GlcNAcylation in multiple species studied, including eukaryotes, fungi, plants, Caenorhabditis elegans, Drosophila melanogaster, murine, and human, and some viruses is provided.
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Comprehensive O-Glycosylation Analysis of the SARS-CoV-2 Spike Protein with Biomimetic Trp-Arg Materials.

TL;DR: In this paper, the authors designed a biomimetic materials, Trp-Arg (WR) monomer-grafted silica microspheres (designated as WR-SiO2), which can enrich N- and O-linked glycopeptides with high selectivity.
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Skp1 Dimerization Conceals Its F-Box Protein Binding Site

TL;DR: A nearly full-length version of Skp1 with the F97E substitution behaved as a stable monomer at concentrations up to 500 µM and actively bound a model FBP, mammalian Fbs1, which suggests that the dimeric state is not required forSkp1 to carry out a basic biochemical function.
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Skp1 isoforms are differentially modified by a dual function prolyl 4-hydroxylase/N-acety lglucosaminyltransferase in a plant pathogen

TL;DR: Findings indicate a widespread occurrence of theSkp1 modification pathway across protist phylogeny, suggest that both Gnt1 and PhyA are specific for Skp1, and indicate that the second Skp 1 provides a bypass mechanism for O2-regulation in Pythium and other protists that conserve this gene.
Journal Article

Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast

TL;DR: Yeast use O-linked mannose to modify nucleocytoplasmic proteins on evolutionary-conserved regions and sites normally occupied by O-GlcNAc in higher eukaryotes, revealing that the two different types of O-glycosylations serve the same important biological functions.
References
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Biomolecular condensates: organizers of cellular biochemistry

TL;DR: This work has shown that liquid–liquid phase separation driven by multivalent macromolecular interactions is an important organizing principle for biomolecular condensates and has proposed a physical framework for this organizing principle.
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The Top 10 oomycete pathogens in molecular plant pathology

TL;DR: A survey to query the community for their ranking of plant-pathogenic oomycete species based on scientific and economic importance received 263 votes from 62 scientists in 15 countries for a total of 33 species and the Top 10 species are provided.
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Systematic Functional Prioritization of Protein Posttranslational Modifications

TL;DR: This work compiled nearly 200,000 phosphorylation, acetylation, and ubiquitination sites from 11 eukaryotic species and developed methods to prioritize the functional relevance of these PTMs by predicting those that likely participate in cross-regulatory events, regulate domain activity, or mediate protein-protein interactions.
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The Extracellular Architecture of Adherens Junctions Revealed by Crystal Structures of Type I Cadherins

TL;DR: It is shown that a molecular layer seen in crystal structures of E- and N-cadherin ectodomains reported here and in a previous C-c cadherin structure corresponds to the extracellular architecture of adherens junctions, which are consistent with a model for junction assembly involving strong trans and weak cis interactions localized in the ectodome.
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2-Oxoglutarate-Dependent Oxygenases

TL;DR: An overview of the biochemistry of 2OGXs is given, providing examples linking to biological function, and how knowledge of their enzymology is being exploited in medicine, agrochemistry, and biocatalysis is outlined.
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