Results 21 to 30 of about 7,591 (197)

Post-Glycosylation Modification of Sialic Acid and Its Role in Virus Pathogenesis

open access: yesVaccines, 2019
Sialic acids are a family of nine carbon keto-aldononulosonic acids presented at the terminal ends of glycans on cellular membranes. α-Linked sialoglycoconjugates often undergo post-glycosylation modifications, among which O-acetylation of N-acetyl ...
Simon S. Park
doaj   +1 more source

Ferrets exclusively synthesize Neu5Ac and express naturally humanized influenza A virus receptors [PDF]

open access: yes, 2014
Mammals express the sialic acids ​N-acetylneuraminic acid (​Neu5Ac) and ​N-glycolylneuraminic acid (​Neu5Gc) on cell surfaces, where they act as receptors for pathogens, including influenza A virus (IAV). ​Neu5Gc is synthesized from ​Neu5Ac by the enzyme
Böhm, Raphael   +14 more
core   +1 more source

Bioorthogonal metabolic glycoengineering of human larynx carcinoma (HEp-2) cells targeting sialic acid

open access: yesBeilstein Journal of Organic Chemistry, 2010
Sialic acids are located at the termini of mammalian cell-surface glycostructures, which participate in essential interaction processes including adhesion of pathogens prior to infection and immunogenicity. Here we present the synthesis and bioorthogonal
Arne Homann   +4 more
doaj   +1 more source

In vitro increased respiratory activity of selected oral bacteria may explain competitive and collaborative interactions in the oral microbiome [PDF]

open access: yes, 2017
Understanding the driving forces behind the shifts in the ecological balance of the oral microbiota will become essential for the future management and treatment of periodontitis. As the use of competitive approaches for modulating bacterial outgrowth is
Boon, Nico   +6 more
core   +3 more sources

Expression of sialic acids and other nonulosonic acids in Leptospira [PDF]

open access: yes, 2012
BackgroundSialic acids are negatively charged nine carbon backbone sugars expressed on mammalian cell surfaces. Sialic acids are part of a larger family of nonulosonic acid (NulO) molecules that includes pseudaminic and legionaminic acids.
Lewis, Amanda L   +3 more
core   +3 more sources

Mass Spectrometry in the Elucidation of the Glycoproteome of Bacterial Pathogens [PDF]

open access: yes, 2010
Presently some three hundred post-translational modifications are known to occur in bacteria in vivo. Many of these modifications play critical roles in the regulation of proteins and control key biological processes.
Graham, Robert L. J., Hess, Sonja
core   +1 more source

Insights into the evolution of sialic acid catabolism among bacteria [PDF]

open access: yes, 2009
Background Sialic acids comprise a family of nine-carbon amino sugars that are prevalent in mucus rich environments. Sialic acids from the human host are used by a number of pathogens as an energy source.
Salvador Almagro-Moreno, E Fidelma Boyd
core   +2 more sources

Recognition of specific sialoglycan structures by oral streptococci impacts the severity of endocardial infection. [PDF]

open access: yes, 2019
Streptococcus gordonii and Streptococcus sanguinis are primary colonizers of the tooth surface. Although generally non-pathogenic in the oral environment, they are a frequent cause of infective endocarditis.
Barnard, Karen N   +10 more
core   +3 more sources

Glycomic analysis of high density lipoprotein shows a highly sialylated particle. [PDF]

open access: yes, 2014
Many of the functional proteins and lipids in high density lipoprotein (HDL) particles are potentially glycosylated, yet very little is known about the glycoconjugates of HDL.
German, J Bruce   +6 more
core   +1 more source

The Lp_3561 and Lp_3562 enzymes support a functional divergence process in the lipase/esterase toolkit from Lactobacillus plantarum [PDF]

open access: yes, 2016
Lactobacillus plantarum species is a good source of esterases since both lipolytic and esterase activities have been described for strains of this species. No fundamental biochemical difference exists among esterases and lipases since both share a common
de las Rivas, Blanca   +5 more
core   +4 more sources

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