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At least 1,063 records · Page 59Linked to original sources
PubMed1979

[Present-day serological diagnosis of syphilis: comparison of TPHA and FTA-ABS tests with classical flocculation and complement-fixation reaction (author's transl)].

Twelve laboratories in the north Rhine-Westphalia participated in comparing TPHA and FTA-ABS tests with the so-called classical syphilis reactions (VDRL test, cardiolipin and pallida complement-fixation reaction, as well as Meinicke clearing reaction II). TPHA and FTA-ABS tests proved to be superior to the conventional methods both as regards specificity and sensitivity. Present-day serological tests of syphilis can thus be limited to the TPHA test to exclude syphilis, the FTA-ABS test as a confirmatory reaction and the VDRL test to judge the need or effectiveness of antisyphilitic treatment. These reactions which supersede the conventional syphilis tests serve for rational, reliable and cheap serological diagnosis of syphilis.

Cardiolipins↗
PubMed2005

Biophysical characterization of longer forms of amyloid beta peptides: possible contribution to flocculent plaque formation.

Alzheimer's disease is characterized by amyloid deposits in the parenchyma and vasculature of the brain. The plaques are mainly composed of amyloid beta (Abeta) peptides ending in residues 40 and 42. Novel longer Abeta peptides were found in brain homogenates of mouse models of Alzheimer's disease and human brain tissue of patients carrying the familial amyloid precursor protein V717F mutation. The biophysical characteristics of these longer Abeta peptides and their role in plaque formation are not understood. We chose to focus our studies on Abeta peptides ending in residues Ile45, Val46 and Ile47 as these peptides were identified in human brain tissue. A combination of circular dichroism and electron microscopy was used to characterize the secondary and tertiary structures of these peptides. All three longer Abeta peptides consisted mainly of a beta-sheet secondary structure. Electron microscopy demonstrated that these beta-structured peptides formed predominantly amorphous aggregates, which convert to amyloid fibres over extended time periods. As these longer peptides may act as seeds for the nucleation of fibrils composed predominantly of shorter amyloid peptides, these interactions were studied. All peptides accelerated the random to beta-structural transitions and fibril formation of Abeta40 and 42.

Amyloid beta-Peptides↗