Results 1 to 10 of about 18,596 (141)

Characterization of a novel N-acetylneuraminic acid lyase favoring industrial N-acetylneuraminic acid synthesis process [PDF]

open access: yesScientific Reports, 2015
AbstractN-Acetylneuraminic acid lyase (NAL, E.C. number 4.1.3.3) is a Class I aldolase that catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) from pyruvate and N-acetyl-D-mannosamine (ManNAc). Due to the high Neu5Ac cleavage activity in most isozyme forms, the enzyme catalyzes the rate-limiting step of two biocatalytic ...
Wenyan Ji   +7 more
openaire   +4 more sources

Correction: Corrigendum: Characterization of a novel N-acetylneuraminic acid lyase favoring industrial N-acetylneuraminic acid synthesis process [PDF]

open access: yesScientific Reports, 2017
Scientific Reports 5: Article number: 09341; published online: 23 March 2015; updated: 28 April 2017 The original version of this article contained an error in testing the kinetic parameters of CgNal towards pyruvate, in which the concentration of ManNAc (50 mM) was not in excess.
Wujin Sun   +7 more
openaire   +4 more sources

Synthesis of partially O-acetylated N-acetylneuraminic acid using regioselective silyl exchange technology. [PDF]

open access: yesOrg Lett, 2014
Postglycosylation acetylation of sialic acid imparts unique roles to sialoglycoconjugates in mammalian immune response making structural and functional understanding of these analogues important.
Gervay-Hague, Jacquelyn, Park, Simon S
core   +3 more sources

A novel variant in CMAH is associated with blood type AB in Ragdoll cats [PDF]

open access: yes, 2016
Citation: Gandolfi, B., Grahn, R. A., Gustafson, N. A., Proverbio, D., Spada, E., Adhikari, B., . . . Helps, C. R. (2016). A novel variant in CMAH is associated with blood type AB in Ragdoll cats. Plos One, 11(5).
Adhikari, B.   +9 more
core   +7 more sources

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

Neuraminidase Activity in \u3cem\u3eDiplococcus pneumoniae\u3c/em\u3e [PDF]

open access: yes, 1966
Kelly, R. T. (Marquette University School of Medicine, Milwaukee, Wis.), D. Greiff, and S. Farmer. Neuraminidase activity in Diplococcus pneumoniae. J. Bacteriol. 91:601–603.
ADA G. L.   +9 more
core   +2 more sources

An orthologue of bacteroides fragilis NanH is the principal sialidase in tannerella forsythia [PDF]

open access: yes, 2009
Sialidase activity is a putative virulence factor of the anaerobic periodontal pathogen Tannerella forsythia, but it is uncertain which genes encode this activity.
Booth, V.   +4 more
core   +3 more sources

Molecular imprinting and grafting of n-acetylneuraminic acid in synthetic polymers for virus targeting [PDF]

open access: yes, 2021
In this work, the synthesis of Molecularly Imprinted Polymers (MIPs) was executed using different solvents, N,N-dimethylformamide (DMF), Acetonitrile (ACN), and a mixture of both reagents, two different monomers, 4-vinylpiridine (4VP) and 4 ...
Noronha, Verônica Teixeira
core  

Occurrence of a new hematoside in the kidney of guinea pig [PDF]

open access: yes, 1983
We have isolated a new hematoside from guinea pig kidney. Like the usual hematoside (II3NeuAc-LacCer), isolated from human erythrocytes, this new hematoside contained glucose, galactose, and N-acetylneuraminic acid in an equimolar proportion.
Hirabayashi, Yoshia   +2 more
core   +1 more source

Streptococcus pneumoniae NanC. Structural insights into the specificity and mechanism of a sialidase that produces a sialidase inhibitor [PDF]

open access: yes, 2015
This work was supported by the Biotechnology and Biological Sciences Research Council (UK) and the Medical Research Council (UK).Streptococcus pneumoniae is an important human pathogen that causes a range of disease states.
Lukacik, Petra   +5 more
core   +1 more source

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