Search Results - "Kandiba, Lina"

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  1. 1

    AglM and VNG1048G, Two Haloarchaeal UDP-Glucose Dehydrogenases, Show Different Salt-Related Behaviors by Kandiba, Lina, Eichler, Jerry

    Published in Life (Basel, Switzerland) (03-08-2016)
    “…Haloferax volcanii AglM and Halobacterium salinarum VNG1048G are UDP-glucose dehydrogenases involved in N-glycosylation in each species. Despite sharing >60%…”
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    Journal Article
  2. 2

    S-Layer Glycoproteins and Flagellins: Reporters of Archaeal Posttranslational Modifications by Jarrell, Ken F., Jones, Gareth M., Kandiba, Lina, Nair, Divya B., Eichler, Jerry

    Published in Archaea (01-01-2010)
    “…Many archaeal proteins undergo posttranslational modifications. S-layer proteins and flagellins have been used successfully to study a variety of these…”
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    Journal Article
  3. 3

    Analysis of putative nonulosonic acid biosynthesis pathways in Archaea reveals a complex evolutionary history by Kandiba, Lina, Eichler, Jerry

    Published in FEMS microbiology letters (01-08-2013)
    “…Abstract Sialic acids and the other nonulosonic acid sugars, legionaminic acid and pseudaminic acid, are nine carbon-containing sugars that can be detected as…”
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    Journal Article
  4. 4

    Lipid modification gives rise to two distinct Haloferax volcanii S-layer glycoprotein populations by Kandiba, Lina, Guan, Ziqiang, Eichler, Jerry

    Published in Biochimica et biophysica acta (01-03-2013)
    “…The S-layer glycoprotein is the sole component of the protein shell surrounding Haloferax volcanii cells. The deduced amino acid sequence of the S-layer…”
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    Journal Article
  5. 5

    Deciphering a pathway of Halobacterium salinarum N‐glycosylation by Kandiba, Lina, Eichler, Jerry

    Published in MicrobiologyOpen (Weinheim) (01-02-2015)
    “…Genomic analysis points to N‐glycosylation as being a common posttranslational modification in Archaea. To date, however, pathways of archaeal N‐glycosylation…”
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    Journal Article
  6. 6

    Structural characterization of the N-linked pentasaccharide decorating glycoproteins of the halophilic archaeon Haloferax volcanii by Kandiba, Lina, Lin, Chia-Wei, Aebi, Markus, Eichler, Jerry, Guerardel, Yann

    Published in Glycobiology (Oxford) (01-07-2016)
    “…N-Glycosylation is a post-translational modification performed in all three domains of life. In the halophilic archaea Haloferax volcanii, glycoproteins such…”
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    Journal Article
  7. 7

    Archaeal S-layer glycoproteins: post-translational modification in the face of extremes by Kandiba, Lina, Eichler, Jerry

    Published in Frontiers in microbiology (26-11-2014)
    “…Corresponding to the sole or basic component of the surface (S)-layer surrounding the archaeal cell in most known cases, S-layer glycoproteins are in direct…”
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    Journal Article
  8. 8

    Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid by Kandiba, Lina, Aitio, Olli, Helin, Jari, Guan, Ziqiang, Permi, Perttu, Bamford, Dennis H., Eichler, Jerry, Roine, Elina

    Published in Molecular microbiology (01-05-2012)
    “…Summary VP4, the major structural protein of the haloarchaeal pleomorphic virus, HRPV‐1, is glycosylated. To define the glycan structure attached to this…”
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    Journal Article
  9. 9

    Add salt, add sugar: N-glycosylation in Haloferax volcanii by Kaminski, Lina, Naparstek, Shai, Kandiba, Lina, Cohen-Rosenzweig, Chen, Arbiv, Adi, Konrad, Zvia, Eichler, Jerry

    Published in Biochemical Society transactions (01-02-2013)
    “…Although performed by members of all three domains of life, the archaeal version of N-glycosylation remains the least understood. Studies on Haloferax volcanii…”
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    Journal Article
  10. 10

    N-glycosylation in Haloferax volcanii: adjusting the sweetness by Eichler, Jerry, Arbiv, Adi, Cohen-Rosenzweig, Chen, Kaminski, Lina, Kandiba, Lina, Konrad, Zvia

    Published in Frontiers in microbiology (24-12-2013)
    “…Long believed to be restricted to Eukarya, it is now known that cells of all three domains of life perform N-glycosylation, the covalent attachment of glycans…”
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    Journal Article