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Pavla Bojarová

Researcher at Academy of Sciences of the Czech Republic

Publications -  83
Citations -  1924

Pavla Bojarová is an academic researcher from Academy of Sciences of the Czech Republic. The author has contributed to research in topics: Chemistry & Glycosylation. The author has an hindex of 23, co-authored 67 publications receiving 1529 citations. Previous affiliations of Pavla Bojarová include Schiller International University & University of Melbourne.

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Enzymatic Glycosylation of Small Molecules: Challenging Substrates Require Tailored Catalysts

TL;DR: In this review, biocatalytic alternatives are presented that offer both stricter specificities and higher yields of glycosylation reactions in various industrial sectors.
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Glycosidases: a key to tailored carbohydrates

TL;DR: This review presents recent developments in glycosidase-catalyzed synthesis via two complementary approaches: the use of wild-type enzymes with engineered substrates, and mutant Glycosidases.
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β-N-Acetylhexosaminidase: What's in a name…?

TL;DR: Extracellular β-N-acetylhexosaminidases from filamentous fungi are able to cleave and transfer substrates bearing various functionalities, ranging from carboxylates, sulfates, acylations to azides, and even 4-deoxy glycosides, which have proved to be versatile biosynthetic tools for the preparation of both natural and modified hexosaminides under mild conditions with good yields.
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Sulfotransferases, sulfatases and formylglycine-generating enzymes: a sulfation fascination

TL;DR: Mechanistic and structural details have recently been obtained for a group of cofactor-independent formylglycine-generating enzymes termed FGEs, and an increasing light has been cast upon the mechanism of sulfatase inactivation by agroup of clinically important agents, the aryl sulfamates.
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Purification and characterization of a nitrilase from Aspergillus niger K10

TL;DR: Aspergillus niger K10 cultivated on 2-cyanopyridine produced high levels of an intracellular nitrilase, which was partially purified (18.6-fold) with a 24% yield, and revealed high homology with those of hsp60 and an ubiquitin-conjugating enzyme.