scholarly journals Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines

Amyloid ◽  
2016 ◽  
Vol 23 (4) ◽  
pp. 209-213 ◽  
Author(s):  
Jean D. Sipe ◽  
Merrill D. Benson ◽  
Joel N. Buxbaum ◽  
Shu-ichi Ikeda ◽  
Giampaolo Merlini ◽  
...  
Keyword(s):  
International Society ◽  
Amyloid Fibril ◽  
Chemical Identification ◽  
Clinical Classification

Amyloid fibril protein nomenclature: 2012 recommendations from the Nomenclature Committee of the International Society of Amyloidosis

Amyloid ◽  
2012 ◽  
Vol 19 (4) ◽  
pp. 167-170 ◽  
Author(s):  
Jean D. Sipe ◽  
Merrill D. Benson ◽  
Joel N. Buxbaum ◽  
Shu-ichi Ikeda ◽  
Giampaolo Merlini ◽  
...  
Keyword(s):  
International Society ◽  
Amyloid Fibril ◽  
Nomenclature Committee ◽  
Amyloid Fibril Protein

Nomenclature 2014: Amyloid fibril proteins and clinical classification of the amyloidosis

Amyloid ◽  
2014 ◽  
Vol 21 (4) ◽  
pp. 221-224 ◽  
Author(s):  
Jean D. Sipe ◽  
Merrill D. Benson ◽  
Joel N. Buxbaum ◽  
Shu-ichi Ikeda ◽  
Giampaolo Merlini ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Clinical Classification

scholarly journals Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis

Amyloid ◽  
2010 ◽  
Vol 17 (3-4) ◽  
pp. 101-104 ◽  
Author(s):  
Jean D. Sipe ◽  
Merrill D. Benson ◽  
Joel N. Buxbaum ◽  
Shu-Ichi Ikeda ◽  
Giampaolo Merlini ◽  
...  
Keyword(s):  
International Society ◽  
Amyloid Fibril ◽  
Nomenclature Committee ◽  
Amyloid Fibril Protein

Immunocytochemical Localization of Amyloid Protein AA in the “Dense Fibrillar Inclusions” of the Reticuloendothelical Cells

1977 ◽  
Vol 35 ◽  
pp. 438-439
Author(s):  
T. Shirahama ◽  
M. Skinner ◽  
A.S. Cohen
Keyword(s):  
Amyloid Fibril ◽  
Close Association ◽  
Gel Filtration ◽  
Fibril Formation ◽  
Amyloid Protein ◽  
Electron Microscopic ◽  
Amyloid Deposits ◽  
Amyloid Fibril Formation ◽  
Electron Microscopic Technique ◽  
Lysosomal System

A1thought the mechanisms of amyloidogenesis have not been entirely clarified, proteolysis of the parent proteins may be one of the important steps in the amyloid fibril formation. Recently, we reported that "dense fibrillar inclusions" (DFI), which had the characteristics of lysosomes and contained organized fibrillar profiles as well, were observed in the reticuloendothelial cells in close association with the foci of new amyloid deposits. We considered the findings as evidence for the involvement of lysosomal system in amyloid fibril formation (l). In the present study, we attempted to determine the identity of the contents of the DFI by the use of antisera against the amyloid protein (AA) and an immuno-electron microscopic technique.Amyloidosis was induced in CBA/J mice by daily injections of casein (l). AA was isolated from amyloid-laden spleens by gel filtration and antibody to it was produced in rabbits (2). For immunocytochemistry, the unlabeled antibody enzyme method (3) was employed.

A General Method for Spectrometer Design in the Scoff Approximation

1976 ◽  
Vol 34 ◽  
pp. 538-539
Author(s):  
J. R. Fields
Keyword(s):  
Electron Microscope ◽  
Transmission Electron Microscope ◽  
Energy Analysis ◽  
Incident Beam ◽  
Scanning Transmission Electron Microscope ◽  
Chemical Identification ◽  
Scanning Transmission Electron ◽  
Transmission Electron ◽  
Scanning Transmission ◽  
General Method

The energy analysis of electrons scattered by a specimen in a scanning transmission electron microscope can improve contrast as well as aid in chemical identification. In so far as energy analysis is useful, one would like to be able to design a spectrometer which is tailored to his particular needs. In our own case, we require a spectrometer which will accept a parallel incident beam and which will focus the electrons in both the median and perpendicular planes. In addition, since we intend to follow the spectrometer by a detector array rather than a single energy selecting slit, we need as great a dispersion as possible. Therefore, we would like to follow our spectrometer by a magnifying lens. Consequently, the line along which electrons of varying energy are dispersed must be normal to the direction of the central ray at the spectrometer exit.

Effect of pH and inhibitors on beta-amyloid fibril assembly

1996 ◽  
Vol 54 ◽  
pp. 752-753
Author(s):  
Beverly E. Maleeff ◽  
Timothy K. Hart ◽  
Stephen J. Wood ◽  
Ronald Wetzel
Keyword(s):  
Amyloid Fibril ◽  
Peptide Fragment ◽  
Hydrophobic Peptides ◽  
Amyloid Fibril Formation ◽  
Effects Of Ph ◽  
Severity Of The Disease ◽  
Kinetics Of ◽  
The Brain

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.

THE IDEA OF TRUSTEESHIP IN INTERNATIONAL SOCIETY

2003 ◽  
Vol 368 ◽  
pp. 67-76 ◽  
Author(s):  
WILLIAM BAIN
Keyword(s):  
International Society
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