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Zinc metalloproteinases and amyloid Beta-Peptide metabolism: the positive side of proteolysis in Alzheimer's disease

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Zinc metalloproteinases and amyloid Beta-Peptide metabolism: the positive side of proteolysis in Alzheimer's disease. / Gough, Mallory; Parr-Sturgess, Catherine; Parkin, Edward.
In: Biochemistry Research International, Vol. 2011, 721463, 2011.

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Gough M, Parr-Sturgess C, Parkin E. Zinc metalloproteinases and amyloid Beta-Peptide metabolism: the positive side of proteolysis in Alzheimer's disease. Biochemistry Research International. 2011;2011:721463. doi: 10.1155/2011/721463

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Gough, Mallory ; Parr-Sturgess, Catherine ; Parkin, Edward. / Zinc metalloproteinases and amyloid Beta-Peptide metabolism : the positive side of proteolysis in Alzheimer's disease. In: Biochemistry Research International. 2011 ; Vol. 2011.

Bibtex

@article{60392609b21e44cfbfcafbde1ccaeab7,
title = "Zinc metalloproteinases and amyloid Beta-Peptide metabolism: the positive side of proteolysis in Alzheimer's disease",
abstract = "Alzheimer's disease is a neurodegenerative condition characterized by an accumulation of toxic amyloid beta- (Aβ-)peptides in the brain causing progressive neuronal death. Aβ-peptides are produced by aspartyl proteinase-mediated cleavage of the larger amyloid precursor protein (APP). In contrast to this detrimental {"}amyloidogenic{"} form of proteolysis, a range of zinc metalloproteinases can process APP via an alternative {"}nonamyloidogenic{"} pathway in which the protein is cleaved within its Aβ region thereby precluding the formation of intact Aβ-peptides. In addition, other members of the zinc metalloproteinase family can degrade preformed Aβ-peptides. As such, the zinc metalloproteinases, collectively, are key to downregulating Aβ generation and enhancing its degradation. It is the role of zinc metalloproteinases in this {"}positive side of proteolysis in Alzheimer's disease{"} that is discussed in the current paper.",
author = "Mallory Gough and Catherine Parr-Sturgess and Edward Parkin",
note = "Copyright {\textcopyright} 2011 Mallory Gough et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.",
year = "2011",
doi = "10.1155/2011/721463",
language = "English",
volume = "2011",
journal = "Biochemistry Research International",
issn = "2090-2255",
publisher = "Hindawi Publishing Corporation",

}

RIS

TY - JOUR

T1 - Zinc metalloproteinases and amyloid Beta-Peptide metabolism

T2 - the positive side of proteolysis in Alzheimer's disease

AU - Gough, Mallory

AU - Parr-Sturgess, Catherine

AU - Parkin, Edward

N1 - Copyright © 2011 Mallory Gough et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

PY - 2011

Y1 - 2011

N2 - Alzheimer's disease is a neurodegenerative condition characterized by an accumulation of toxic amyloid beta- (Aβ-)peptides in the brain causing progressive neuronal death. Aβ-peptides are produced by aspartyl proteinase-mediated cleavage of the larger amyloid precursor protein (APP). In contrast to this detrimental "amyloidogenic" form of proteolysis, a range of zinc metalloproteinases can process APP via an alternative "nonamyloidogenic" pathway in which the protein is cleaved within its Aβ region thereby precluding the formation of intact Aβ-peptides. In addition, other members of the zinc metalloproteinase family can degrade preformed Aβ-peptides. As such, the zinc metalloproteinases, collectively, are key to downregulating Aβ generation and enhancing its degradation. It is the role of zinc metalloproteinases in this "positive side of proteolysis in Alzheimer's disease" that is discussed in the current paper.

AB - Alzheimer's disease is a neurodegenerative condition characterized by an accumulation of toxic amyloid beta- (Aβ-)peptides in the brain causing progressive neuronal death. Aβ-peptides are produced by aspartyl proteinase-mediated cleavage of the larger amyloid precursor protein (APP). In contrast to this detrimental "amyloidogenic" form of proteolysis, a range of zinc metalloproteinases can process APP via an alternative "nonamyloidogenic" pathway in which the protein is cleaved within its Aβ region thereby precluding the formation of intact Aβ-peptides. In addition, other members of the zinc metalloproteinase family can degrade preformed Aβ-peptides. As such, the zinc metalloproteinases, collectively, are key to downregulating Aβ generation and enhancing its degradation. It is the role of zinc metalloproteinases in this "positive side of proteolysis in Alzheimer's disease" that is discussed in the current paper.

U2 - 10.1155/2011/721463

DO - 10.1155/2011/721463

M3 - Journal article

C2 - 21152187

VL - 2011

JO - Biochemistry Research International

JF - Biochemistry Research International

SN - 2090-2255

M1 - 721463

ER -