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Titlebook: Alterations in the Neuronal Cytoskeleton in Alzheimer Disease; George Perry Book 1987 Plenum Press, New York 1987 Alzheimer.Parkinson.bioc

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期刊全称Alterations in the Neuronal Cytoskeleton in Alzheimer Disease
影响因子2023George Perry
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学科分类Advances in Behavioral Biology
图书封面Titlebook: Alterations in the Neuronal Cytoskeleton in Alzheimer Disease;  George Perry Book 1987 Plenum Press, New York 1987 Alzheimer.Parkinson.bioc
影响因子The neuronal cytoskeleton is a complex structure responsive to both intrinsic and extrinsic factors. Defined populations of neurons in the brains of patients with Alzheimer and several other neurodegenerative diseases contain abnormal filamentous accumulations which share elements with the cytoskeleton. Although there is a general consensus that these abnormal filaments do contain cytoskeletal elements, much debate remains regarding which cytoskeletal elements are incorporated and whether the cytoskeletal rearrangement is primary or secondary to other cellular changes. In this book these questions are addressed in a historical perspect­ ive in light of new data that allows the reinterpretation of previously reported results. Contributions are based on many of the major tech­ niques of modern biology including biochemistry, molecular biology, electron microscopy and immunocytochemistry. In the view of the editor, this volume is being written at a time when our understanding of the cytopathology of Alzheimer disease is moving from predominantly descriptive to both analytical and mechanistic. I hope that this contribution will provide impetus to speed this transi­ tion. George Perry C
Pindex Book 1987
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发表于 2025-3-21 22:20:49 | 显示全部楼层
Alterations in the Neuronal Cytoskeleton in Alzheimer Disease
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https://doi.org/10.1007/978-3-662-62692-4re one of the major constituents of neuronal cytoskeletons and play important roles in regulating cell morphology, intracellular transport processes and secretions. The microtubules are polymers of tubulin and they also contain accessory proteins, notably MAP1, MAP2, and the tau proteins..
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https://doi.org/10.1007/978-3-642-59907-1in in primary amyloidosis has been shown to be the amino terminal fragment of immunoglobulin light chains with a variable molecular weight, ranging from 5–23 kDa.. Some subgroups of light chains appear to have a highly amyloidogenic primary structure, as shown by preferential association of λVI with
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Diagnosekodierung in der Praxisapplication of electron microscopy using shadowing and negative staining techniques has revealed the PHF as a left-handed double helix . with a relatively short axial length; this makes the structure different from the fibrous sub-structure of neurofilaments .. Negative staining of isolated PHF, bov
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