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Protein aggregation, metals and oxidative stress in neurodegenerative diseases.

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Protein aggregation, metals and oxidative stress in neurodegenerative diseases. / Tabner, Brian J.; El-Agnaf, Omar M. A.; German, M. J. et al.
In: Biochemical Society Transactions, Vol. 33, No. 5, 11.2005, p. 1082-1086.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Tabner, BJ, El-Agnaf, OMA, German, MJ, Fullwood, NJ & Allsop, D 2005, 'Protein aggregation, metals and oxidative stress in neurodegenerative diseases.', Biochemical Society Transactions, vol. 33, no. 5, pp. 1082-1086. https://doi.org/10.1042/BST20051082

APA

Vancouver

Tabner BJ, El-Agnaf OMA, German MJ, Fullwood NJ, Allsop D. Protein aggregation, metals and oxidative stress in neurodegenerative diseases. Biochemical Society Transactions. 2005 Nov;33(5):1082-1086. doi: 10.1042/BST20051082

Author

Tabner, Brian J. ; El-Agnaf, Omar M. A. ; German, M. J. et al. / Protein aggregation, metals and oxidative stress in neurodegenerative diseases. In: Biochemical Society Transactions. 2005 ; Vol. 33, No. 5. pp. 1082-1086.

Bibtex

@article{96ecfba3342d408e8445cde134046df7,
title = "Protein aggregation, metals and oxidative stress in neurodegenerative diseases.",
abstract = "There is clear evidence implicating oxidative stress in the pathology of many different neurodegenerative diseases. ROS (reactive oxygen species) are the primary mediators of oxidative stress and many of the aggregating proteins and peptides associated with neurodegenerative disease can generate hydrogen peroxide, a key ROS, apparently through interactions with redox-active metal ions. Our recent results suggest that ROS are generated during the very early stages of protein aggregation, when protofibrils or soluble oligomers are present, but in the absence of mature amyloid fibrils. The generation of ROS during early-stage protein aggregation may be a common, fundamental molecular mechanism underlying the pathogenesis of oxidative damage, neurodegeneration and cell death in several different neurodegenerative diseases. Drugs that specifically target this process could be useful in the future therapy of these diseases.",
keywords = "amyloid, hydrogen peroxide, metal, neurodegeneration, oligomer, oxidative stress., humans, neurotoxins, proteins",
author = "Tabner, {Brian J.} and El-Agnaf, {Omar M. A.} and German, {M. J.} and Fullwood, {Nigel J.} and David Allsop",
year = "2005",
month = nov,
doi = "10.1042/BST20051082",
language = "English",
volume = "33",
pages = "1082--1086",
journal = "Biochemical Society Transactions",
issn = "0300-5127",
publisher = "Portland Press Ltd.",
number = "5",

}

RIS

TY - JOUR

T1 - Protein aggregation, metals and oxidative stress in neurodegenerative diseases.

AU - Tabner, Brian J.

AU - El-Agnaf, Omar M. A.

AU - German, M. J.

AU - Fullwood, Nigel J.

AU - Allsop, David

PY - 2005/11

Y1 - 2005/11

N2 - There is clear evidence implicating oxidative stress in the pathology of many different neurodegenerative diseases. ROS (reactive oxygen species) are the primary mediators of oxidative stress and many of the aggregating proteins and peptides associated with neurodegenerative disease can generate hydrogen peroxide, a key ROS, apparently through interactions with redox-active metal ions. Our recent results suggest that ROS are generated during the very early stages of protein aggregation, when protofibrils or soluble oligomers are present, but in the absence of mature amyloid fibrils. The generation of ROS during early-stage protein aggregation may be a common, fundamental molecular mechanism underlying the pathogenesis of oxidative damage, neurodegeneration and cell death in several different neurodegenerative diseases. Drugs that specifically target this process could be useful in the future therapy of these diseases.

AB - There is clear evidence implicating oxidative stress in the pathology of many different neurodegenerative diseases. ROS (reactive oxygen species) are the primary mediators of oxidative stress and many of the aggregating proteins and peptides associated with neurodegenerative disease can generate hydrogen peroxide, a key ROS, apparently through interactions with redox-active metal ions. Our recent results suggest that ROS are generated during the very early stages of protein aggregation, when protofibrils or soluble oligomers are present, but in the absence of mature amyloid fibrils. The generation of ROS during early-stage protein aggregation may be a common, fundamental molecular mechanism underlying the pathogenesis of oxidative damage, neurodegeneration and cell death in several different neurodegenerative diseases. Drugs that specifically target this process could be useful in the future therapy of these diseases.

KW - amyloid

KW - hydrogen peroxide

KW - metal

KW - neurodegeneration

KW - oligomer

KW - oxidative stress.

KW - humans

KW - neurotoxins

KW - proteins

U2 - 10.1042/BST20051082

DO - 10.1042/BST20051082

M3 - Journal article

VL - 33

SP - 1082

EP - 1086

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 5

ER -