Flexible Synthesis and Biological Activity of Uronic Acid-Typegem-Diamine 1-N-Iminosugars:  A New Family of Glycosidase Inhibitors

2000 ◽  
Vol 65 (1) ◽  
pp. 2-11 ◽  
Author(s):  
Yoshio Nishimura ◽  
Eiki Shitara ◽  
Hayamitsu Adachi ◽  
Minako Toyoshima ◽  
Motowo Nakajima ◽  
...  
2008 ◽  
Vol 3 (10) ◽  
pp. 1934578X0800301 ◽  
Author(s):  
Maria I. Bilan ◽  
Anatolii I. Usov

Sulfated polysaccharides of brown algae (“fucoidans”) constitute a wide variety of biopolymers from simple sulfated fucans up to complex heteropolysaccharides composed of several neutral monosaccharides, uronic acid and sulfate. The increased interest in this class of polysaccharides is explained by their high and versatile biological activities, and hence, by their possible use in new drug design. Structural analysis of several fucoidans demonstrates that their biological properties are determined not only by charge density, but also by fine chemical structure, although distinct correlations between structure and biological activity cannot be formulated at present. The aim of this review is to describe the methods of structural analysis currently used in fucoidan chemistry, and to discuss some new information on the structures of fucoidans presented in recent publications.


Author(s):  
Yong Shen

Alzheimer’s disease (AD) is a constantly progressive and highly complex neurodegenerative disease, and there are many ways to molecularly characterize the various stages. Morphologically, AD patients are characterized by neurofibrillar abnormalities associated with pathological hyperphosphorylation of tau protein, and deposits of ß– amyloid peptides (Aß). There is an overwhelming amount of information to support the hypothesis that generation, formation, and ß-amyloid deposits play key mechanistic roles in the early development of AD. It is known that the cause of early-onset familial AD (FAD) is due to mutations in three genes which cause an increase in the production of the toxic peptide, Aß42. The molecules that cause the proteolytic activities of beta and gamma secretase, two proteases that free the Aß-peptide by endoproteolyzing APP, have recently been discovered. Homologous to BACE1, BACE2 was also a recent discovery (Lin et al, 2000; Vassar et al, 1999; Yan et al, 1999), and together these two enzymes make up a new family of transmembrane aspartic proteases. The key enzyme, BACE1, initiates the formation of Aß, represents a candidate biomarker, as well as a drug target for AD, exhibit all the functional properties of ß–secretase. This chapter will review the biology of BACE1 and focus attention to BACE1 as a candidate biomarker for the early detection, prediction, and biological activity in AD.


1992 ◽  
Vol 45 (6) ◽  
pp. 861-867 ◽  
Author(s):  
FRANK VANMIDDLESWORTH ◽  
ROBERT A. GIACOBBE ◽  
MARIA LOPEZ ◽  
GEORGE GARRITY ◽  
JUDITH A. BLAND ◽  
...  

ChemInform ◽  
2010 ◽  
Vol 28 (39) ◽  
pp. no-no
Author(s):  
Y. KAMEDA ◽  
K. KAWASHIMA ◽  
M. TAKEUCHI ◽  
K. IKEDA ◽  
N. ASANO ◽  
...  

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