Literature DB >> 9862427

Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease.

O M El-Agnaf1, R Jakes, M D Curran, A Wallace.   

Abstract

Alpha-synuclein (alpha-syn) protein has been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the alpha-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We report here that human wild-type alpha-syn, PD-linked mutant alpha-syn(Ala30Pro) and mutant alpha-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. The mutant alpha-syn forms more beta-sheet and mature filaments than the wild-type protein. These findings suggest that accumulation of alpha-syn as insoluble deposits of amyloid may play a major role in the pathogenesis of these neurodegenerative diseases.

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Year:  1998        PMID： 9862427     DOI： 10.1016/s0014-5793(98)01419-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  57 in total

1.  Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation.

Authors:  L C Serpell; J Berriman; R Jakes; M Goedert; R A Crowther
Journal:  Proc Natl Acad Sci U S A       Date:  2000-04-25       Impact factor: 11.205

Review 2.  Protein aggregates and dementia: is there a common toxicity?

Authors:  S Lovestone; D M McLoughlin
Journal:  J Neurol Neurosurg Psychiatry       Date:  2002-02       Impact factor: 10.154

3.  Selective insolubility of alpha-synuclein in human Lewy body diseases is recapitulated in a transgenic mouse model.

Authors:  P J Kahle; M Neumann; L Ozmen; V Müller; S Odoy; N Okamoto; H Jacobsen; T Iwatsubo; J Q Trojanowski; H Takahashi; K Wakabayashi; N Bogdanovic; P Riederer; H A Kretzschmar; C Haass
Journal:  Am J Pathol       Date:  2001-12       Impact factor: 4.307

4.  Neuropathology in mice expressing human alpha-synuclein.

Authors:  H van der Putten; K H Wiederhold; A Probst; S Barbieri; C Mistl; S Danner; S Kauffmann; K Hofele; W P Spooren; M A Ruegg; S Lin; P Caroni; B Sommer; M Tolnay; G Bilbe
Journal:  J Neurosci       Date:  2000-08-15       Impact factor: 6.167

5.  Distinct hydration properties of wild-type and familial point mutant A53T of α-synuclein associated with Parkinson's disease.

Authors:  E Hazy; M Bokor; L Kalmar; A Gelencser; P Kamasa; K-H Han; K Tompa; P Tompa
Journal:  Biophys J       Date:  2011-11-01       Impact factor: 4.033

6.  Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy.

Authors:  K A Conway; S J Lee; J C Rochet; T T Ding; R E Williamson; P T Lansbury
Journal:  Proc Natl Acad Sci U S A       Date:  2000-01-18       Impact factor: 11.205

7.  Definition of a molecular pathway mediating α-synuclein neurotoxicity.

Authors:  Jacqueline Burré; Manu Sharma; Thomas C Südhof
Journal:  J Neurosci       Date:  2015-04-01       Impact factor: 6.167

Review 8.  α-Synuclein nonhuman primate models of Parkinson's disease.

Authors:  David J Marmion; Jeffrey H Kordower
Journal:  J Neural Transm (Vienna)       Date:  2017-04-22       Impact factor: 3.575

Review 9.  The many faces of α-synuclein: from structure and toxicity to therapeutic target.

Authors:  Hilal A Lashuel; Cassia R Overk; Abid Oueslati; Eliezer Masliah
Journal:  Nat Rev Neurosci       Date:  2013-01       Impact factor: 34.870

Review 10.  Exploring the accessible conformations of N-terminal acetylated α-synuclein.

Authors:  Gina M Moriarty; Maria K Janowska; Lijuan Kang; Jean Baum
Journal:  FEBS Lett       Date:  2013-03-13       Impact factor: 4.124
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