N-acetyl-2,3-didehydro-2-deoxyneuraminic acid
N-acetyl-2,3-didehydro-2-deoxyneuraminic acid structure
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Common Name | N-acetyl-2,3-didehydro-2-deoxyneuraminic acid | ||
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| CAS Number | 24967-27-9 | Molecular Weight | 291.25500 | |
| Density | 1.58g/cm3 | Boiling Point | 773.4ºC at 760 mmHg | |
| Molecular Formula | C11H17NO8 | Melting Point | 227-228ºC | |
| MSDS | Chinese USA | Flash Point | 421.6ºC | |
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Chemistry, metabolism, and biological functions of sialic acids.
Adv. Carbohydr. Chem. Biochem. 40 , 131, (1982)
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Identification of selective inhibitors for human neuraminidase isoenzymes using C4,C7-modified 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (DANA) analogues.
J. Med. Chem. 56(7) , 2948-58, (2013) In the past two decades, human neuraminidases (human sialidases, hNEUs) have been found to be involved in numerous pathways in biology. The development of selective and potent inhibitors of these enzymes will provide critical tools for glycobiology, help to a... |
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Elastin-derived peptides are new regulators of insulin resistance development in mice.
Diabetes 62(11) , 3807-16, (2013) Although it has long been established that the extracellular matrix acts as a mechanical support, its degradation products, which mainly accumulate during aging, have also been demonstrated to play an important role in cell physiology and the development of c... |
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Structural and biochemical characterization of the broad substrate specificity of Bacteroides thetaiotaomicron commensal sialidase.
Biochim. Biophys. Acta 1834(8) , 1510-9, (2013) Sialidases release the terminal sialic acid residue from a wide range of sialic acid-containing polysaccharides. Bacteroides thetaiotaomicron, a symbiotic commensal microbe, resides in and dominates the human intestinal tract. We characterized the recombinant... |
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Contributions of NanI sialidase to Caco-2 cell adherence by Clostridium perfringens type A and C strains causing human intestinal disease.
Infect. Immun. 82(11) , 4620-30, (2014) Previous studies showed that Clostridium perfringens type D animal disease strain CN3718 uses NanI sialidase for adhering to enterocyte-like Caco-2 cells. The current study analyzed whether NanI is similarly important when type A and C human intestinal diseas... |
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Sialyl residues modulate LPS-mediated signaling through the Toll-like receptor 4 complex.
PLoS ONE 7 , e32359, (2012) We previously reported that neuraminidase (NA) pretreatment of human PBMCs markedly increased their cytokine response to lipopolysaccharide (LPS). To study the mechanisms by which this occurs, we transfected HEK293T cells with plasmids encoding TLR4, CD14, an... |
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Uncoupling of Elastin Complex Receptor during In Vitro Aging Is Related to Modifications in Its Intrinsic Sialidase Activity and the Subsequent Lactosylceramide Production.
PLoS ONE 10 , e0129994, (2015) Degradation of elastin leads to the production of elastin-derived peptides (EDP), which exhibit several biological effects, such as cell proliferation or protease secretion. Binding of EDP on the elastin receptor complex (ERC) triggers lactosylceramide (LacCe... |
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Aurintricarboxylic acid is a potent inhibitor of influenza A and B virus neuraminidases.
PLoS ONE 4(12) , e8350, (2009) Influenza viruses cause serious infections that can be prevented or treated using vaccines or antiviral agents, respectively. While vaccines are effective, they have a number of limitations, and influenza strains resistant to currently available anti-influenz... |
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Exacerbation of influenza virus infections in mice by intranasal treatments and implications for evaluation of antiviral drugs.
Antimicrob. Agents Chemother. 56(12) , 6328-33, (2012) Compounds lacking oral activity may be delivered intranasally to treat influenza virus infections in mice. However, intranasal treatments greatly enhance the virulence of such virus infections. This can be partially compensated for by giving reduced virus cha... |
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Bacterial neuraminidase rescues influenza virus replication from inhibition by a neuraminidase inhibitor.
PLoS ONE 7(9) , e45371, (2012) Influenza virus neuraminidase (NA) cleaves terminal sialic acid residues on oligosaccharide chains that are receptors for virus binding, thus playing an important role in the release of virions from infected cells to promote the spread of cell-to-cell infecti... |