Subject Areas on Research
- A predicted geranylgeranyl reductase reduces the ω-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii.
- AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein.
- AglQ is a novel component of the Haloferax volcanii N-glycosylation pathway.
- AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein.
- Assembling Glycan-Charged Dolichol Phosphates: Chemoenzymatic Synthesis of a Haloferax volcanii N-Glycosylation Pathway Intermediate.
- Different routes to the same ending: comparing the N-glycosylation processes of Haloferax volcanii and Haloarcula marismortui, two halophilic archaea from the Dead Sea.
- Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein.
- Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid.
- Gene Expression of Haloferax volcanii on Intermediate and Abundant Sources of Fixed Nitrogen.
- GlpR Is a Direct Transcriptional Repressor of Fructose Metabolic Genes in Haloferax volcanii.
- Glyco-engineering in Archaea: differential N-glycosylation of the S-layer glycoprotein in a transformed Haloferax volcanii strain.
- Lipid modification gives rise to two distinct Haloferax volcanii S-layer glycoprotein populations.
- Protein glycosylation as an adaptive response in Archaea: growth at different salt concentrations leads to alterations in Haloferax volcanii S-layer glycoprotein N-glycosylation.
- Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans.
- Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.
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