Immunohistochemical study of advanced glycation end products in aging and Alzheimer's disease brain (Q48826779)

15 February 2018

title

Immunohistochemical study of advanced glycation end products in aging and Alzheimer's disease brain (English)

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15 February 2018

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Takedo A

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Yasuda T

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Miyata T

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Mizuno K

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Li M

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Yoneyama S

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Horie K

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Maeda K

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Sobue G

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language of work or name

English

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publication date

1 December 1996

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15 February 2018

published in

Neuroscience Letters

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volume

221

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issue

1

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15 February 2018

page(s)

17-20

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15 February 2018

Role of oxidative stress in development of complications in diabetes

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Accumulation of Maillard reaction products in skin collagen in diabetes and aging

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Hydrogen peroxide production during experimental protein glycation

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Are advanced glycation end-products associated with amyloidosis in Alzheimer's disease?

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Accumulation of advanced glycation end products of the Maillard reaction with age in human hippocampal neurons.

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Tau protein from Alzheimer's disease patients is glycated at its tubulin-binding domain.

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Differential expression of advanced glycosylation end-products in neurons of different species

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Age-dependent accumulation of advanced glycosylation end products in human neurons.

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beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis

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Identification of pentosidine as a native structure for advanced glycation end products in beta-2-microglobulin-containing amyloid fibrils in patients with dialysis-related amyloidosis

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Monocyte/macrophage response to beta 2-microglobulin modified with advanced glycation end products

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Nonenzymatic glycosylation, the Maillard reaction and the aging process

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N epsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins

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Superoxide production from nonenzymatically glycated protein

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Glycation of lens proteins by the oxidation products of ascorbic acid

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Advanced Maillard reaction end products are associated with Alzheimer disease pathology

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Advanced glycation end products contribute to amyloidosis in Alzheimer disease

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Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress

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10.1016/S0304-3940(96)13275-4

Identifiers

DOI

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15 February 2018

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15 February 2018