Results 21 to 30 of about 20,212 (212)
Toxins, 2022 Clostridium perfringens type F food poisoning (FP) strains produce C. perfringens enterotoxin (CPE) to cause a common bacterial food-borne illness in the United States. During FP, CPE is synthesized in the intestines when C.
Jihong Li +3 more
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It All Starts with a Sandwich: Identification of Sialidases with Trans-Glycosylation Activity. [PDF]
PLoS ONE, 2016 Sialidases (3.2.1.18) may exhibit trans-sialidase activity to catalyze sialylation of lactose if the active site topology is congruent with that of the Trypanosoma cruzi trans-sialidase (EC 2.4.1.-). The present work was undertaken to test the hypothesis
Rune T Nordvang +7 more
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Two different sialidases, KDN-sialidase and regular sialidase in the starfish Asterina pectinifera [PDF]
Biochemical Journal, 1996 We have found the coexistence of two different sialidases in the entrails of the starfish Asterina pectinifera: a regular sialidase (RS), which cleaves sialic acid from sialoglycoconjugates, and a KDN-sialidase (KS) which releases the sialic acid analogue KDN (2-keto-3-deoxy-D-glycero-d-galacto-nononic acid) from KDN-containing glycoconjugates that are
J A, Yuziuk +5 more
openaire +2 more sources
Sialidase-(in)dependent NDV virion release.
, 2023 The streptavidin sensors were loaded to saturation with 3’S(LN)2-PAA. (A) NDV virions were associated with 3’S(LN)2-PAA in presence of BCX2798. (B and C) After association to 3’S(LN)2-PAA, sensors were dipped into PBS to allow NDV virions to dissociate ...
Frank J. M. van Kuppeveld (7252571) +6 more
core +1 more source
Structural studies on the sialidases from Streptococcus pneumoniae and Pseudomonas aeruginosa [PDF]
, 2009 The sialidases are a group of glycosyl hydrolases that specifically remove terminal sialic acid (Neu5Ac) residues from various glycans. In the two common human pathogenic bacteria Streptococcus pneumoniae and Pseudomonas aeruginosa, these enzymes have
Xu, Guogang
core +2 more sources
Journal of Investigative Dermatology, 1982 A fluorometric microassay is described for sialidase using the natural substrate sialyllactose. This technique has been used to characterize and quantify cutaneous sialidase. The enzyme was found exclusively in the particulate fraction of skin homogenates.
Mier, P.D. +3 more
openaire +2 more sources
Sialidase Activity in Human Blood Serum Has a Distinct Seasonal Pattern: A Pilot Study
Biology, 2020 Desialylation—loss of terminal sialic acid residues from glycoconjugates catalyzed by sialidases—is involved in many human diseases and is considered a key molecular event of atherosclerosis onset.
Victor Y. Glanz +5 more
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Frontiers in Cellular and Infection Microbiology, 2022 IntroductionSialidase activity in the cervicovaginal fluid (CVF) is associated with microscopic findings of bacterial vaginosis (BV). Sequencing of bacterial 16S rRNA gene in vaginal samples has revealed that the majority of microscopic BV cases fit into
Carolina Sanitá Tafner Ferreira +5 more
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Identification and characterization of a novel, versatile sialidase from a Sphingobacterium that can hydrolyze the glycosides of any sialic acid species at neutral pH [PDF]
, 2020 Bacterial sialidases are widely used to remove sialic acid (Sia) residues from glycans. Most of them cleave the glycosides of N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc) under acidic pHs; however, currently available bacterial
Takegawa, Kaoru +4 more
core +1 more source
Increase of intestinal bacterial sialidase activity exacerbates acute colitis in mice
Frontiers in Molecular Biosciences, 2022 The availability of endogenous and dietary carbohydrates in the gastrointestinal tract influences the composition of the gut microbiota. Carbohydrate foraging requires the action of bacterially-encoded glycoside hydrolases, which release mono- and ...
Tobias Hasler +7 more
doaj +1 more source