Results 1 to 10 of about 7,156 (161)

β-Hexosaminidases Along the Secretory Pathway of Nicotiana benthamiana Have Distinct Specificities Toward Engineered Helminth N-Glycans on Recombinant Glycoproteins

open access: yesFrontiers in Plant Science, 2021
Secretions of parasitic worms (helminths) contain a wide collection of immunomodulatory glycoproteins with the potential to treat inflammatory disorders, like autoimmune diseases.
Nicolò Alvisi   +10 more
doaj   +2 more sources

Structural-Functional Analysis Reveals a Specific Domain Organization in Family GH20 Hexosaminidases. [PDF]

open access: yesPLoS ONE, 2015
Hexosaminidases are involved in important biological processes catalyzing the hydrolysis of N-acetyl-hexosaminyl residues in glycosaminoglycans and glycoconjugates.
Cristina Val-Cid   +3 more
doaj   +2 more sources

Computational Studies on the Potency and Selectivity of PUGNAc Derivatives Against GH3, GH20, and GH84 β-N-acetyl-D-hexosaminidases

open access: yesFrontiers in Chemistry, 2019
β-N-acetyl-D-hexosaminidases have attracted significant attention due to their crucial role in diverse physiological functions including antibacterial synergists, pathogen defense, virus infection, lysosomal storage, and protein glycosylation.
Lili Dong   +6 more
doaj   +2 more sources

Human recombinant lysosomal β-Hexosaminidases produced in Pichia pastoris efficiently reduced lipid accumulation in Tay-Sachs fibroblasts. [PDF]

open access: yesAm J Med Genet C Semin Med Genet, 2020
GM2 gangliosidosis, Tay‐Sachs and Sandhoff diseases, are lysosomal storage disorders characterized by the lysosomal accumulation of GM2 gangliosides. This accumulation is due to deficiency in the activity of the β‐hexosaminidases Hex‐A or Hex‐B, which ...
Espejo-Mojica AJ   +7 more
europepmc   +2 more sources

Characterization of recombinant human lysosomal beta-hexosaminidases produced in the methylotrophic yeast Pichia pastoris

open access: yesUniversitas Scientiarum, 2016
β-hexosaminidases (Hex) are dimeric enzymes involved in the lysosomal degradation of glycolipids and glycans. They are formed by α- and/or β-subunits encoded byHEXA and HEXB genes, respectively.
Angela Johana Espejo Mojica   +7 more
doaj   +2 more sources

Follow-up of pre-motor symptoms of Parkinson’s disease in adult patients with Gaucher disease type 1 and analysis of their lysosomal enzyme profiles in the CSF [PDF]

open access: yesOrphanet Journal of Rare Diseases, 2023
Background Parkinson’s disease (PD) is the second most common neurodegenerative disease worldwide. Its classic motor symptoms may be preceded by non-motor symptoms (NMS).
Matheus Vernet Machado Bressan Wilke   +14 more
doaj   +2 more sources

Iminosugars of the Invasive Arboreal Amorpha fruticosa and Glycosidase Inhibition Potential [PDF]

open access: yesPlants
Amorpha fruticosa L. (Fabaceae) originates from North America and has become an aggressive invasive plant in many parts of the world. It affects the local biodiversity in many negative ways. Our previous in vivo tests of purified extract of A.
Robert J. Nash   +3 more
doaj   +2 more sources

Molecular Phylogeny and Predicted 3D Structure of Plant beta-D-N-Acetylhexosaminidase [PDF]

open access: yesThe Scientific World Journal, 2014
beta-D-N-Acetylhexosaminidase, a family 20 glycosyl hydrolase, catalyzes the removal of β-1,4-linked N-acetylhexosamine residues from oligosaccharides and their conjugates. We constructed phylogenetic tree of β-hexosaminidases to analyze the evolutionary
Md. Anowar Hossain, Hairul Azman Roslan
doaj   +3 more sources

Combining functional metagenomics and glycoanalytics to identify enzymes that facilitate structural characterization of sulfated N-glycans. [PDF]

open access: yesMicrob Cell Fact, 2021
Background Sulfate modification of N-glycans is important for several biological functions such as clearance of pituitary hormones or immunoregulation.
Chuzel L   +8 more
europepmc   +3 more sources

Multivalency To Inhibit and Discriminate Hexosaminidases [PDF]

open access: yesChemistry, 2017
Adachi, Isao   +21 more
core   +2 more sources

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