Literature DB >> 35657577

Disease Mechanisms of Multiple System Atrophy: What a Parallel Between the Form of Pasta and the Alpha-Synuclein Assemblies Involved in MSA and PD Tells Us.

Ronald Melki1.   

Abstract

Intracellular deposits rich in aggregated alpha-synuclein that appear within the central nervous system are intimately associated to Parkinson's disease and multiple system atrophy. While it is understandable that the aggregation of proteins, which share no primary structure identity, such as alpha-synuclein and tau protein, leads to different diseases, that of a given protein yielding distinct pathologies is counterintuitive. This short review relates molecular and mechanistic processes to the observed pathological diversity associated to alpha-synuclein aggregation.
© 2022. The Author(s).

Entities:  

Keywords:  Alpha-synuclein aggregation; Fibrillar polymorphism; Multiple system atrophy; Parkinson’s disease; Protein folding

Year:  2022        PMID: 35657577     DOI: 10.1007/s12311-022-01417-0

Source DB:  PubMed          Journal:  Cerebellum        ISSN: 1473-4222            Impact factor:   3.847


  73 in total

1.  Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein.

Authors:  Agya K Frimpong; Rinat R Abzalimov; Vladimir N Uversky; Igor A Kaltashov
Journal:  Proteins       Date:  2010-02-15

2.  Interplay between desolvation and secondary structure in mediating cosolvent and temperature induced alpha-synuclein aggregation.

Authors:  V L Anderson; W W Webb; D Eliezer
Journal:  Phys Biol       Date:  2012-08-29       Impact factor: 2.583

3.  Conformational properties of alpha-synuclein in its free and lipid-associated states.

Authors:  D Eliezer; E Kutluay; R Bussell; G Browne
Journal:  J Mol Biol       Date:  2001-04-06       Impact factor: 5.469

Review 4.  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

5.  Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence.

Authors:  Allan Chris M Ferreon; Yann Gambin; Edward A Lemke; Ashok A Deniz
Journal:  Proc Natl Acad Sci U S A       Date:  2009-03-17       Impact factor: 11.205

6.  Structural disorder of monomeric α-synuclein persists in mammalian cells.

Authors:  Francois-Xavier Theillet; Andres Binolfi; Beata Bekei; Andrea Martorana; Honor May Rose; Marchel Stuiver; Silvia Verzini; Dorothea Lorenz; Marleen van Rossum; Daniella Goldfarb; Philipp Selenko
Journal:  Nature       Date:  2016-01-25       Impact factor: 49.962

7.  Raman spectroscopic characterization of secondary structure in natively unfolded proteins: alpha-synuclein.

Authors:  Nakul C Maiti; Mihaela M Apetri; Michael G Zagorski; Paul R Carey; Vernon E Anderson
Journal:  J Am Chem Soc       Date:  2004-03-03       Impact factor: 15.419

Review 8.  The proteostasis network and its decline in ageing.

Authors:  Mark S Hipp; Prasad Kasturi; F Ulrich Hartl
Journal:  Nat Rev Mol Cell Biol       Date:  2019-07       Impact factor: 94.444

9.  Conformational equilibria in monomeric alpha-synuclein at the single-molecule level.

Authors:  Massimo Sandal; Francesco Valle; Isabella Tessari; Stefano Mammi; Elisabetta Bergantino; Francesco Musiani; Marco Brucale; Luigi Bubacco; Bruno Samorì
Journal:  PLoS Biol       Date:  2008-01       Impact factor: 8.029

10.  Properties of native brain α-synuclein.

Authors:  Jacqueline Burré; Sandro Vivona; Jiajie Diao; Manu Sharma; Axel T Brunger; Thomas C Südhof
Journal:  Nature       Date:  2013-06-13       Impact factor: 49.962

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.