In vivo fluorescence kinetics of mono-l-aspartyl chlorin e6 (NPe6) and influence of angiogenesis in fibrosarcoma-bearing mice

1998 ◽  
Vol 3 (4) ◽  
pp. 209-215 ◽  
Author(s):  
Masahiko Harada ◽  
Katsuo Aizawa ◽  
Tetsuya Okunaka ◽  
Harubumi Kato
1996 ◽  
Vol 73 (5) ◽  
pp. 573-580 ◽  
Author(s):  
MJH Witjes ◽  
OC Speelman ◽  
PGJ Nikkels ◽  
CAAM Nooren ◽  
JM Nauta ◽  
...  

2016 ◽  
Vol 57 (2) ◽  
pp. 647 ◽  
Author(s):  
Robin Sharma ◽  
Christina Schwarz ◽  
David R. Williams ◽  
Grazyna Palczewska ◽  
Krzysztof Palczewski ◽  
...  

2003 ◽  
Vol 149 (5) ◽  
pp. 972-976 ◽  
Author(s):  
I.M. Stefanaki ◽  
S. Georgiou ◽  
G.C. Themelis ◽  
E.M. Vazgiouraki ◽  
A.D. Tosca

Author(s):  
Beverly E. Maleeff ◽  
Timothy K. Hart ◽  
Stephen J. Wood ◽  
Ronald Wetzel

Alzheimer's disease is characterized post-mortem in part by abnormal extracellular neuritic plaques found in brain tissue. There appears to be a correlation between the severity of Alzheimer's dementia in vivo and the number of plaques found in particular areas of the brain. These plaques are known to be the deposition sites of fibrils of the protein β-amyloid. It is thought that if the assembly of these plaques could be inhibited, the severity of the disease would be decreased. The peptide fragment Aβ, a precursor of the p-amyloid protein, has a 40 amino acid sequence, and has been shown to be toxic to neuronal cells in culture after an aging process of several days. This toxicity corresponds to the kinetics of in vitro amyloid fibril formation. In this study, we report the biochemical and ultrastructural effects of pH and the inhibitory agent hexadecyl-N-methylpiperidinium (HMP) bromide, one of a class of ionic micellar detergents known to be capable of solubilizing hydrophobic peptides, on the in vitro assembly of the peptide fragment Aβ.


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