Search Results - "Kuchtova, Andrea"

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  1. 1

    Domain evolution in enzymes of the neopullulanase subfamily by Kuchtová, Andrea, Janeček, Štefan

    “…Among the glycoside hydrolases (GHs) classified within the Carbohydrate-Active enZyme (CAZy) database, the α-amylase family GH13 containing ~30 different…”
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    Journal Article
  2. 2

    In silico analysis of family GH77 with focus on amylomaltases from borreliae and disproportionating enzymes DPE2 from plants and bacteria by Kuchtová, Andrea, Janeček, Štefan

    Published in Biochimica et biophysica acta (01-10-2015)
    “…The CAZy glycoside hydrolase (GH) family GH77 is a monospecific family containing 4-α-glucanotransferases that if from prokaryotes are known as amylomaltases…”
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    Journal Article
  3. 3

    In silico identification of catalytic residues and domain fold of the family GH119 sharing the catalytic machinery with the α-amylase family GH57 by Janeček, Štefan, Kuchtová, Andrea

    Published in FEBS letters (21-09-2012)
    “…► The GH119 family is predicted to adopt a (β/α)7-barrel fold. ► Conserved sequence regions of the family GH57 are recognised in GH119. ► The GH119 family…”
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  4. 4

    A novel GH13 subfamily of α-amylases with a pair of tryptophans in the helix α3 of the catalytic TIM-barrel, the LPDlx signature in the conserved sequence region V and a conserved aromatic motif at the C-terminus by Janeček, Štefan, Kuchtová, Andrea, Petrovičová, Soňa

    Published in Biológia (01-10-2015)
    “…The α-amylase enzyme specificity has been classified in the Carbohydrate-Active enZyme (CAZy) database into the families GH13, GH57, GH119 and eventually also…”
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    Journal Article
  5. 5

    The unique evolution of the carbohydrate‐binding module CBM20 in laforin by Kuchtová, Andrea, Gentry, Matthew S., Janeček, Štefan

    Published in FEBS letters (01-02-2018)
    “…Laforin catalyses glycogen dephosphorylation. Mutations in its gene result in Lafora disease, a fatal progressive myoclonus epilepsy, the hallmark being…”
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    Journal Article
  6. 6

    An empirical pipeline for personalized diagnosis of Lafora disease mutations by Brewer, M. Kathryn, Machio-Castello, Maria, Viana, Rosa, Wayne, Jeremiah L., Kuchtová, Andrea, Simmons, Zoe R., Sternbach, Sarah, Li, Sheng, García-Gimeno, Maria Adelaida, Serratosa, Jose M., Sanz, Pascual, Vander Kooi, Craig W., Gentry, Matthew S.

    Published in iScience (19-11-2021)
    “…Lafora disease (LD) is a fatal childhood dementia characterized by progressive myoclonic epilepsy manifesting in the teenage years, rapid neurological decline,…”
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    Journal Article
  7. 7

    Cooperative Kinetics of the Glucan Phosphatase Starch Excess4 by Mak, Claudia A., Weis, Kenyon, Henao, Tiffany, Kuchtova, Andrea, Chen, Tiantian, Sharma, Savita, Meekins, David A., Thalmann, Matthias, Vander Kooi, Craig W., Raththagala, Madushi

    Published in Biochemistry (Easton) (10-08-2021)
    “…Glucan phosphatases are members of a functionally diverse family of dual-specificity phosphatase (DSP) enzymes. The plant glucan phosphatase Starch Excess4…”
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    Journal Article
  8. 8

    The unique evolution of the carbohydrate‐binding module CBM 20 in laforin by Kuchtová, Andrea, Gentry, Matthew S., Janeček, Štefan

    Published in FEBS letters (01-02-2018)
    “…Laforin catalyses glycogen dephosphorylation. Mutations in its gene result in Lafora disease, a fatal progressive myoclonus epilepsy, the hallmark being…”
    Get full text
    Journal Article
  9. 9

    A novel GH13 subfamily of [alpha]-amylases with a pair of tryptophans in the helix [alpha]3 of the catalytic TIM-barrel, the LPDlx signature in the conserved sequence region V and a conserved aromatic motif at the C-terminus by Janecek, Stefan, Kuchtová, Andrea, Petrovicová, Sona

    Published in Biológia (01-10-2015)
    “…The α-amylase enzyme specificity has been classified in the Carbohydrate-Active enZyme (CAZy) database into the families GH13, GH57, GH119 and eventually also…”
    Get full text
    Journal Article
  10. 10

    novel GH13 subfamily of α-amylases with a pair of tryptophans in the helix α3 of the catalytic TIM-barrel, the LPDlx signature in the conserved sequence region V and a conserved aromatic motif at the C-terminus by Janeček, Å tefan, Andrea KuchtovÃ, Soňa PetrovičovÃ

    Published in Biológia (2016)
    “…The α-amylase enzyme specificity has been classified in the Carbohydrate-Active enZyme (CAZy) database into the families GH13, GH57, GH119 and eventually also…”
    Get full text
    Journal Article