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Sialidases

Current Protocols in Molecular Biology, 1994
AbstractSialic acids are a family of nine‐carbon acidic sugars found at the nonreducing terminus of many glycoconjugates. Sialidases can remove these sugar units selectively from cell surfaces, membranes, or purified glycoconjugates. In this unit, sialidase digestion of purified glycoproteins is described as is treatment of intact cells.
L D, Powell, A P, Varki
openaire   +2 more sources

Sialidases in biological systems.

Die Pharmazie, 2010
Sialidases are very common in biological systems. They are found particularly in diverse virus families and bacteria, but also in protozoa, some invertebrates and mammalian. The enzymes differ in their biochemical properties, e.g., kinetics, binding affinity or substrate preference. Nevertheless, they have conserved domains and structural similarities.
Melzig, M. F., Schwerdtfeger, S. M.
openaire   +2 more sources

Influenza Virus Sialidase

Nature, 1960
THE sialidase of influenza virus has been investigated quantitatively using the method recently described by Warren1 for determining free sialic acid in the presence of the compound bound to muco-protein substrates. For this work, the substrate used was a mucoid derived from the nest-cementing substance of the swiftlet (Collocalia sp.).
C, HOWE, L T, LEE, H M, ROSE
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Sialidases

2003
No Full ...
Dyason, Jeffrey   +2 more
openaire   +1 more source

Sialidase and malignancy: A minireview

Glycoconjugate Journal, 2003
Aberrant sialylation in cancer cells is thought to be a characteristic feature associated with malignant properties including invasiveness and metastatic potential. Sialidase which catalyzes the removal of sialic acid residues from glycoproteins and glycolipids, has been suggested to play important roles in many biological processes through regulation ...
Taeko, Miyagi   +3 more
openaire   +2 more sources

Characterization of myxovirus sialidase

Experientia, 1975
Die Sialidasen von Myxoviren zeigten eine ahnliche Substratspezifitat wie die Streptomyces-Sialidase. Siastatin A und B, Produkte von Streptomycesarten, wurden auf ihre hemmende Wirkung gegen Sialidasen verschiedenster Herkunft untersucht und als spezifische Hemmstoffe gegen bakterielle Sialidasen erkannt.
T, Aoyagi   +4 more
openaire   +2 more sources

Structure and Function of Mammalian Sialidases

2012
The removal of sialic acids, catalyzed by sialidase, is the initial step in degradation of oligosaccharides, glycoproteins, and glycolipids. The catalytic reaction may greatly influence biological processes through changing the conformation of glycoproteins and create or mask binding sites of functional molecules.
MONTI, Eugenio, Miyagi, Taeko
openaire   +3 more sources

Human sialidase as a cancer marker

PROTEOMICS, 2008
Abstract Altered sialylation of cell surface glycoproteins and glycolipids is closely related to the malignant phenotype of cancer cells, including the metastatic potential and invasiveness. Many cancer‐related antigens in clinical use contain sialic acids at the terminal position of sugar chains in the molecules.
Taeko, Miyagi   +7 more
openaire   +2 more sources

Sialidases: Therapeutic and Antiatherogenic Potential

Current Pharmaceutical Design, 2017
This review focuses on the biological role and clinical relevance of relatively poor studied enzymes known as sialidases. We describe structure and function of sialic acid, in particular as a component of gangliosides and plasma lipoproteins. Several types of sialidases are known in mammals, of which trans-sialidase is of special interest, since it is ...
Vasily Nikolaevich, Sukhorukov   +4 more
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Sialidases

1976
Abraham Rosenberg, Cara-Lynne Schengrund
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