Literature DB >> 33326534

Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-β aggregation.

Joana S Cristóvão1, Guilherme G Moreira, Filipe E P Rodrigues, Ana P Carapeto, Mário S Rodrigues, Isabel Cardoso, António E N Ferreira, Miguel Machuqueiro, Guenter Fritz, Cláudio M Gomes.   

Abstract

S100B is an extracellular protein implicated in Alzheimer's Disease and a suppressor of amyloid-β aggregation. Herein we report a mechanism tying Cu2+ binding to a change in assembly state yielding disulfide cross-linked oligomers with higher anti-aggregation activity. This chemical control of chaperone function illustrates a regulatory process relevant under metal and proteostasis dysfunction as in neurodegeneration.

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Year:  2021        PMID： 33326534     DOI： 10.1039/d0cc06842j

Source DB:  PubMed          Journal:  Chem Commun (Camb)        ISSN： 1359-7345            Impact factor:   6.222


  2 in total

1.  Computational Analysis of the Interactions between the S100B Extracellular Chaperone and Its Amyloid β Peptide Client.

Authors:  Filipe E P Rodrigues; António J Figueira; Cláudio M Gomes; Miguel Machuqueiro
Journal:  Int J Mol Sci       Date:  2021-03-31       Impact factor: 5.923

2.  Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding.

Authors:  Guilherme G Moreira; François-Xavier Cantrelle; Andrea Quezada; Filipa S Carvalho; Joana S Cristóvão; Urmi Sengupta; Nicha Puangmalai; Ana P Carapeto; Mário S Rodrigues; Isabel Cardoso; Güenter Fritz; Federico Herrera; Rakez Kayed; Isabelle Landrieu; Cláudio M Gomes
Journal:  Nat Commun       Date:  2021-11-01       Impact factor: 14.919
  2 in total

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