Faculty Opinions recommendation of Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1043127.493046 ◽

2006 ◽

Author(s):

Pascal Derkinderen

Keyword(s):

Histone Acetylation ◽

Alpha Synuclein

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Chaperone mediated degradation of aggregated alpha synuclein

Aktuelle Neurologie ◽

10.1055/s-2004-833268 ◽

2004 ◽

Vol 31 (S 1) ◽

Author(s):

J Klucken ◽

Y Shin ◽

PJ Mclean ◽

BT Hyman

Keyword(s):

Alpha Synuclein

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Conditional control of human wild-type and Parkinson's disease-associated mutant alpha-synuclein in transgenic mouse brain

Aktuelle Neurologie ◽

10.1055/s-2004-833272 ◽

2004 ◽

Vol 31 (S 1) ◽

Author(s):

S Nuber ◽

T Schmidt ◽

D Berg ◽

M Neumann ◽

C Holzmann ◽

...

Keyword(s):

Parkinson’S Disease ◽

Parkinson's Disease ◽

Transgenic Mouse ◽

Mouse Brain ◽

Alpha Synuclein ◽

Wild Type ◽

Conditional Control ◽

Human Wild Type

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Analysis of alpha-synuclein aggregation and associated pathologies in a cellular model of multiple system atrophy

Aktuelle Neurologie ◽

10.1055/s-2005-916295 ◽

2005 ◽

Vol 32 (06) ◽

Author(s):

G Fillon ◽

M Neumann ◽

R Zufferey ◽

P Aebischer ◽

HA Kretzschmar ◽

...

Keyword(s):

Multiple System Atrophy ◽

Alpha Synuclein ◽

Cellular Model ◽

Alpha Synuclein Aggregation

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Behavioral impairments after intranasal administration of alpha-synuclein oligomers in aged mice

10.26226/morressier.5971be86d462b80290b53191 ◽

2017 ◽

Author(s):

Ilya Kalinin

Keyword(s):

Intranasal Administration ◽

Alpha Synuclein ◽

Aged Mice ◽

Behavioral Impairments

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Alpha-synuclein effect on neuronal networks in cell culture

10.26226/morressier.5b31ec592afeeb001345aa94 ◽

2018 ◽

Author(s):

Kristian Leite

Keyword(s):

Cell Culture ◽

Neuronal Networks ◽

Alpha Synuclein

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ADAPTATION OF POLYMERASE CHAIN REACTION-RESTRICTION FRAGMENT LENGTH POLYMORPHISM METHOD FOR POLYMORPHISM (RS2583988) ANALYSIS IN ALPHA-SYNUCLEIN GENE

World of Medicine and Biology ◽

10.26724/2079-8334-2020-3-73-130-134 ◽

2020 ◽

Vol 16 (73) ◽

pp. 130

Author(s):

K.A. Tarianyk ◽

N.V. Lytvynenko ◽

V.K. Oliinychenko ◽

T.V. Byslik ◽

K.F. Pochernyaev

Keyword(s):

Polymerase Chain Reaction ◽

Restriction Fragment Length Polymorphism ◽

Restriction Fragment ◽

Length Polymorphism ◽

Fragment Length ◽

Fragment Length Polymorphism ◽

Alpha Synuclein ◽

Chain Reaction ◽

Polymerase Chain ◽

Restriction Fragment Length

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Faculty Opinions recommendation of Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1003340.30205 ◽

2001 ◽

Author(s):

Michael Meisterernst

Keyword(s):

Histone Acetylation ◽

Histone Acetyltransferase ◽

Gene Activation

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Faculty Opinions recommendation of Cutting edge: histone acetylation and recombination at the TCR gamma locus follows IL-7 induction.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1003486.35354 ◽

2002 ◽

Author(s):

Dinah Singer

Keyword(s):

Histone Acetylation ◽

Cutting Edge ◽

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

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1008343.104560 ◽

2002 ◽

Author(s):

John Hardy

Keyword(s):

Parkinson’S Disease ◽

Parkinson's Disease ◽

Transgenic Mice ◽

Neurodegenerative Disease ◽

Alpha Synuclein ◽

Alpha Synuclein Aggregation ◽

Familial Parkinson’S Disease

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Faculty Opinions recommendation of Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1010273.149808 ◽

2002 ◽

Author(s):

Harry Ischiropoulos

Keyword(s):

Parkinson’S Disease ◽

Parkinson's Disease ◽

Alpha Synuclein

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