Side-Chain Structure of Cell Surface Polysaccharide, Mannan, Affects Hypocholesterolemic Activity of Yeast

2009 ◽  
Vol 57 (17) ◽  
pp. 8003-8009 ◽  
Author(s):  
Yasuto Yoshida ◽  
Eiichiro Naito ◽  
Harumi Mizukoshi ◽  
Yoko Watanabe ◽  
Kazumasa Kimura ◽  
...  
Keyword(s):  
Cell Surface ◽  
Chain Structure ◽  
Side Chain ◽  
Surface Polysaccharide

scholarly journals Relationship of 25-hydroxyvitamin D3 side chain structure to biological activity.

1975 ◽  
Vol 250 (1) ◽  
pp. 226-230
Author(s):  
M F Holick ◽  
M Garabedian ◽  
H K Schnoes ◽  
H F DeLuca
Keyword(s):  
Biological Activity ◽  
Chain Structure ◽  
Side Chain ◽  
Relationship Of

Programming cell communications with pH-responsive DNA nanodevices

2021 ◽  
Author(s):  
Junjun Hou ◽  
Shitai Zhu ◽  
Ziwei Zhao ◽  
Jianlei Shen ◽  
Jie Chao ◽  
...  
Keyword(s):  
Cell Surface ◽  
Chain Structure ◽  
Ph Responsive ◽  
Double Chain ◽  
Physiological Conditions

The DNA nanoswitchs on cell surface could respond to the changes of pH under physiological conditions by switching from a three-chain structure to a double-chain structure, thus connecting another set...

scholarly journals Entropy driven chain effects on ligation chemistry

2015 ◽  
Vol 6 (2) ◽  
pp. 1061-1074 ◽  
Author(s):  
Kai Pahnke ◽  
Josef Brandt ◽  
Ganna Gryn'ova ◽  
Peter Lindner ◽  
Ralf Schweins ◽  
...  
Keyword(s):  
Building Block ◽  
Chain Structure ◽  
Step Change ◽  
Side Chain ◽  
On Demand ◽  
Bonding Systems ◽  
Intrinsic Stiffness

Entropic chain effects on dynamic bonding reactions are shown to enable the tuning of reaction equilibria not only by changing the mass of the reactants, but also by merely altering the building block side chain structure and thus the intrinsic stiffness. The findings enable a step change for the design of on-demand bonding systems and reversible ligation chemistry in general.

scholarly journals Altered Gingipain Maturation in vimA- and vimE-Defective Isogenic Mutants of Porphyromonas gingivalis

2005 ◽  
Vol 73 (3) ◽  
pp. 1357-1366 ◽  
Author(s):  
Elaine Vanterpool ◽  
Francis Roy ◽  
Lawrence Sandberg ◽  
Hansel M. Fletcher
Keyword(s):  
Cell Surface ◽  
Porphyromonas Gingivalis ◽  
Culture Supernatant ◽  
Specific Activity ◽  
Phenotypic Effect ◽  
Western Blots ◽  
Defective Mutant ◽  
Surface Polysaccharide ◽  
Isogenic Mutants ◽  
Specific Sugar

ABSTRACT We have previously shown that gingipain activity in Porphyromonas gingivalis is modulated by the unique vimA and vimE genes. To determine if these genes had a similar phenotypic effect on protease maturation and activation, isogenic mutants defective in those genes were further characterized. Western blot analyses with antigingipain antibodies showed RgpA-, RgpB-, and Kgp-immunoreactive bands in membrane fractions as well as the culture supernatant of both P. gingivalis W83 and FLL93, the vimE-defective mutant. In contrast, the membrane of P. gingivalis FLL92, the vimA-defective mutant, demonstrated immunoreactivity only with RgpB antibodies. With mass spectrometry or Western blots, full-length RgpA and RgpB were identified from extracellular fractions. In similar extracellular fractions from P. gingivalis FLL92 and FLL93, purified RgpB activated only arginine-specific activity. In addition, the lipopolysaccharide profiles of the vimA and vimE mutants were truncated in comparison to that of W83. While glycosylated proteins were detected in the membrane and extracellular fractions from the vimA- and vimE-defective mutants, a monoclonal antibody (1B5) that reacts with specific sugar moieties of the P. gingivalis cell surface polysaccharide and membrane-associated Rgp gingipain showed no immunoreactivity with these fractions. Taken together, these results indicate a possible defect in sugar biogenesis in both the vimA- and vimE-defective mutants. These modulating genes play a role in the secretion, processing, and/or anchorage of gingipains on the cell surface.

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