Increased alpha-synuclein aggregation following limited cleavage by certain matrix metalloproteinases (Q24316244)

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17 January 2020

title

Increased alpha-synuclein aggregation following limited cleavage by certain matrix metalloproteinases (English)

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Matrix metallopeptidase 9

17 January 2020

main subject

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Matrix metallopeptidase 3

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Matrix metallopeptidase 1

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proteolysis

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1

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17 January 2020

Armin Giese

2

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author name string

Kai Boetzel

3

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17 January 2020

Lars Israel

4

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17 January 2020

Tobias Högen

5

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17 January 2020

Georg Nübling

6

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17 January 2020

Hans Kretzschmar

7

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17 January 2020

Stefan Lorenzl

8

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17 January 2020

language of work or name

English

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publication date

31 October 2008

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17 January 2020

published in

Experimental Neurology

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17 January 2020

volume

215

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issue

1

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page(s)

201-208

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The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia

17 January 2020

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Characterization of plasma gelsolin as a substrate for matrix metalloproteinases

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Cytotoxicity by matrix metalloprotease-1 in organotypic spinal cord and dissociated neuronal cultures

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Mechanistic aspects of Parkinson's disease: alpha-synuclein and the biomembrane

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Origins and effects of extracellular alpha-synuclein: implications in Parkinson's disease

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The matrix metalloproteinases inhibitor Ro 28-2653 [correction of Ro 26-2853] extends survival in transgenic ALS mice

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Matrix metalloproteinase-9 regulates TNF-alpha and FasL expression in neuronal, glial cells and its absence extends life in a transgenic mouse model of amyotrophic lateral sclerosis

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Secondary structure of alpha-synuclein oligomers: characterization by raman and atomic force microscopy

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Elevated levels of matrix metalloproteinases-9 and -1 and of tissue inhibitors of MMPs, TIMP-1 and TIMP-2 in postmortem brain tissue of progressive supranuclear palsy

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Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers

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Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution

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Synthetic filaments assembled from C-terminally truncated alpha-synuclein

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Alpha-synuclein locus duplication as a cause of familial Parkinson's disease

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Causal relation between alpha-synuclein gene duplication and familial Parkinson's disease

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Increased plasma levels of matrix metalloproteinase-9 in patients with Alzheimer's disease

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Non-A.beta. Component of Alzheimer's Disease Amyloid (NAC) is Amyloidogenic

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Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes

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7 January 2021

Role of alpha-synuclein carboxy-terminus on fibril formation in vitro

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7 January 2021

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone

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7 January 2021

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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Alpha-synuclein in Lewy bodies

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Determination of protease cleavage site motifs using mixture-based oriented peptide libraries

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A century-old debate on protein aggregation and neurodegeneration enters the clinic

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Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease

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Metalloendoprotease cleavage triggers gelsolin amyloidogenesis

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The solubility of alpha-synuclein in multiple system atrophy differs from that of dementia with Lewy bodies and Parkinson's disease

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Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations

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Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53 --> Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease

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Matrix metalloproteinase-9 is elevated in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced parkinsonism in mice

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7 January 2021

Aggregated alpha-synuclein mediates dopaminergic neurotoxicity in vivo.

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Ataxin-3 represses transcription via chromatin binding, interaction with histone deacetylase 3, and histone deacetylation

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7 January 2021

Different species of alpha-synuclein oligomers induce calcium influx and seeding.

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7 January 2021

10.1016/J.EXPNEUROL.2008.10.010

Identifiers

DOI

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release_y42be6p5n5e3fpi3o6ywdyvuhi

17 January 2020

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/y42be6p5n5e3fpi3o6ywdyvuhi

24 November 2022

mapped directly with Wikidata item

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