In 1906, Alois Alzheimer reported first time the symptomatic changes in ageing brain of his dementia patient Auguste Deter. He reported the presence of senile plaques and neurofibrillary tangles in her autopsied brain tissues. Later, his senior Emil Kraepelin, in 1910, recognized the diseased condition as a new disease and gave it a name, Alzheimer's disease (AD) (Alzheimer, 1906; Kraepelin, 1910). Thereafter, a number of histochemical techniques have been brought with time to study amyloids. The advent of various staining methods formulated basic techniques, which have been used since then, to stain various kinds of biological and non-biological amyloids (Bennhold, 1922; Divry, 1927; Missmahl and Hartwig, 1953; Saeed and Fine, 1967; Wagner,
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Till now, a number of studies have been done, using EM (Goldsbury et al., 1997; Inoue et al., 1998; Kajava et al., 2004), X-ray (Fraser et al., 1992; Perutz et al., 2002), Nuclear magnetic resonance (NMR) (Antzutkin et al., 2002) and other staining techniques, to further identify and characterize various amyloid species throughout the living world (Makin and Serpell, 2005). A host of studies over amyloids, which are involved in various human diseases have made us more familiar with these species of proteins, causing an array of pathological conditions ranging from diabetes to neurodegeneration (Jimenez et al., 2002; Malinchik et al., 1998; Perutz et al., 2002). In Figure 1, we have tried to mark major achievements in the field of amyloids, over the time. Based on years of research, scientists are now able to deduce and define amyloids as structural entities with some hallmark characteristics. Next section elaborates very fine ultra-structural details of amyloid fibers based on knowledge accumulated over the timeline of research on amyloids.
2.2. Many Faces of Amyloid Structures: Strengths, Challenges, and
Till now, a number of studies have been done, using EM (Goldsbury et al., 1997; Inoue et al., 1998; Kajava et al., 2004), X-ray (Fraser et al., 1992; Perutz et al., 2002), Nuclear magnetic resonance (NMR) (Antzutkin et al., 2002) and other staining techniques, to further identify and characterize various amyloid species throughout the living world (Makin and Serpell, 2005). A host of studies over amyloids, which are involved in various human diseases have made us more familiar with these species of proteins, causing an array of pathological conditions ranging from diabetes to neurodegeneration (Jimenez et al., 2002; Malinchik et al., 1998; Perutz et al., 2002). In Figure 1, we have tried to mark major achievements in the field of amyloids, over the time. Based on years of research, scientists are now able to deduce and define amyloids as structural entities with some hallmark characteristics. Next section elaborates very fine ultra-structural details of amyloid fibers based on knowledge accumulated over the timeline of research on amyloids.
2.2. Many Faces of Amyloid Structures: Strengths, Challenges, and