Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing α-synuclein oligomeric species toxicity (Q33619357)

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English	Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing α-synuclein oligomeric species toxicity	scientific article

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12 March 2020

Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing α-synuclein oligomeric species toxicity (English)

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12 March 2020

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César L. Avila

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12 March 2020

Leandro Barbosa

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12 March 2020

María Soledad Celej

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Sergio B Socías

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Sergio B Socías

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Clarisa M Torres-Bugeau

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Clarisa M Torres-Bugeau

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Dulce Papy-Garcia

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Rita Raisman-Vozari

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Elisa Morandé Sales

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12 March 2020

Mohand O Ouidja

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26 March 2014

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12 March 2020

Journal of Biological Chemistry

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12 March 2020

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12 March 2020

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12 March 2020

13838-13850

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12 March 2020

Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds

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The secreted oligomeric form of α-synuclein affects multiple steps of membrane trafficking.

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Does a prion-like mechanism play a major role in the apparent spread of α-synuclein pathology?

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Direct observation of the interconversion of normal and toxic forms of α-synuclein

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Age-related changes in rat myocardium involve altered capacities of glycosaminoglycans to potentiate growth factor functions and heparan sulfate-altered sulfation

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21 June 2018

Characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase early amyloid-like oligomers and their implication in α-synuclein aggregation.

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On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control

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21 June 2018

A deadly spread: cellular mechanisms of α-synuclein transfer

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21 June 2018

Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation

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21 June 2018

Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism

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Association and heterogeneity at the GAPDH locus in Alzheimer's disease

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Amyloidogenic protein-membrane interactions: mechanistic insight from model systems

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Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration

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Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells

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21 June 2018

Structural classification of toxic amyloid oligomers

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21 June 2018

Clearance and deposition of extracellular alpha-synuclein aggregates in microglia.

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21 June 2018

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

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21 June 2018

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21 June 2018

Polymorphism in the intermediates and products of amyloid assembly

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21 June 2018

Protein misfolding, functional amyloid, and human disease

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21 June 2018

Intravesicular localization and exocytosis of alpha-synuclein and its aggregates.

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21 June 2018

S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding

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21 June 2018

Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase

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21 June 2018

A simple method for the isolation and purification of total lipides from animal tissues

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21 June 2018

S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component

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21 June 2018

Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders

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Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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10.1074/JBC.M113.544288

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12 March 2020

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12 March 2020

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12 March 2020

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