Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems. - Wikidata - wikimedia - TriplyDB

Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems.

Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems.

http://www.wikidata.org/entity/Q34598569

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Production of glycoprotein vaccines in Escherichia coli Polyisoprenol specificity in the Campylobacter jejuni N-linked glycosylation pathway Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry Cell factories for insulin production Recombinant expression of Streptococcus pneumoniae capsular polysaccharides in Escherichia coli.Structural context for proteinN-glycosylation in bacteria: The structure of PEB3, an adhesin fromCampylobacter jejuni Outer membrane vesicles displaying engineered glycotopes elicit protective antibodies A catalytically essential motif in external loop 5 of the bacterial oligosaccharyltransferase PglB Exploitation of bacterial N-linked glycosylation to develop a novel recombinant glycoconjugate vaccine against Francisella tularensis.Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation.Interaction between two putative glycosyltransferases is required for glycosylation of a serine-rich streptococcal adhesin.Recombinant glycans on an S-layer self-assembly protein: a new dimension for nanopatterned biomaterials Serogroup-specific bacterial engineered glycoproteins as novel antigenic targets for diagnosis of shiga toxin-producing-escherichia coli-associated hemolytic-uremic syndrome.Characterization of N-linked protein glycosylation in Helicobacter pullorum Targeted metabolic labeling of yeast N-glycans with unnatural sugars A combined method for producing homogeneous glycoproteins with eukaryotic N-glycosylation N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.The s-layer glycome-adding to the sugar coat of bacteria.Characterization of the structurally diverse N-linked glycans of Campylobacter species.The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB.Multimethodological approach to identification of glycoproteins from the proteome of Francisella tularensis, an intracellular microorganism.Interplay of the Wzx translocase and the corresponding polymerase and chain length regulator proteins in the translocation and periplasmic assembly of lipopolysaccharide o antigen.The expanding horizons of asparagine-linked glycosylation.A network-based approach to identify substrate classes of bacterial glycosyltransferases.Molecular basis of S-layer glycoprotein glycan biosynthesis in Geobacillus stearothermophilus Exploiting the Campylobacter jejuni protein glycosylation system for glycoengineering vaccines and diagnostic tools directed against brucellosis.Multiple post-translational modifications affect heterologous protein synthesis.Diversity in the protein N-glycosylation pathways within the Campylobacter genus Hijacking bacterial glycosylation for the production of glycoconjugates, from vaccines to humanised glycoproteins Post-translational modifications in the context of therapeutic proteins.Glycoengineered Outer Membrane Vesicles: A Novel Platform for Bacterial Vaccines Biosynthesis of Conjugate Vaccines Using an O-Linked Glycosylation System.Antibody therapeutics: isotype and glycoform selection.A Bacterial Glycoengineered Antigen for Improved Serodiagnosis of Porcine Brucellosis S-layer nanoglycobiology of bacteria.Broad spectrum O-linked protein glycosylation in the human pathogen Neisseria gonorrhoeae.Advances in Campylobacter biology and implications for biotechnological applications.Study of free oligosaccharides derived from the bacterial N-glycosylation pathway.N-linked glycosylation in bacteria: an unexpected application.

P2860

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P2860

Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems.

http://www.wikidata.org/entity/Q34598569

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2006 nî lūn-bûn

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2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2006年の論文

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Substrate specificity of bacte ...... terial and eukaryotic systems.

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Substrate specificity of bacte ...... terial and eukaryotic systems.

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Substrate specificity of bacte ...... terial and eukaryotic systems.

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PNAS.0509207103

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Proceedings of the National Academy of Sciences of the United States of America

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Substrate specificity of bacte ...... terial and eukaryotic systems.

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Bradley R Clarke

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Chris Whitfield

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Enrique D Vines

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Marcela Hernandez

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Markus Aebi

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Michael Kowarik

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Michael Wacker

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Nicola L Pohl

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P2860

In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation

Lipopolysaccharide endotoxins

Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase

Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state

Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis

Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

Cloning and characterization of the ALG3 gene of Saccharomyces cerevisiae.

Assembly of asparagine-linked oligosaccharides

The activity of a putative polyisoprenol-linked sugar translocase (Wzx) involved in Escherichia coli O antigen assembly is independent of the chemical structure of the O repeat

The oligosaccharyltransferase complex from yeast

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Mario F Feldman

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