Literature DB >> 25736087

Secondary nucleation wears the BRICHOS in this family.

Frank A Ferrone1.   

Abstract

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Year:  2015        PMID： 25736087     DOI： 10.1038/nsmb.2980

Source DB:  PubMed          Journal:  Nat Struct Mol Biol        ISSN： 1545-9985            Impact factor:   15.369


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  10 in total

1.  Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis.

Authors:  Rakez Kayed; Elizabeth Head; Jennifer L Thompson; Theresa M McIntire; Saskia C Milton; Carl W Cotman; Charles G Glabe
Journal:  Science       Date:  2003-04-18       Impact factor: 47.728

2.  High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C.

Authors:  Hanna Willander; Glareh Askarieh; Michael Landreh; Per Westermark; Kerstin Nordling; Henrik Keränen; Erik Hermansson; Aaron Hamvas; Lawrence M Nogee; Tomas Bergman; Alejandra Saenz; Cristina Casals; Johan Åqvistg; Hans Jörnvall; Helena Berglund; Jenny Presto; Stefan D Knight; Jan Johansson
Journal:  Proc Natl Acad Sci U S A       Date:  2012-02-02       Impact factor: 11.205

3.  BRICHOS domains efficiently delay fibrillation of amyloid β-peptide.

Authors:  Hanna Willander; Jenny Presto; Glareh Askarieh; Henrik Biverstål; Birgitta Frohm; Stefan D Knight; Jan Johansson; Sara Linse
Journal:  J Biol Chem       Date:  2012-07-16       Impact factor: 5.157

Review 4.  Physical and structural basis for polymorphism in amyloid fibrils.

Authors:  Robert Tycko
Journal:  Protein Sci       Date:  2014-09-13       Impact factor: 6.725

Review 5.  Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide.

Authors:  Christian Haass; Dennis J Selkoe
Journal:  Nat Rev Mol Cell Biol       Date:  2007-02       Impact factor: 94.444

6.  Kinetics of nucleation-controlled polymerization. A perturbation treatment for use with a secondary pathway.

Authors:  M F Bishop; F A Ferrone
Journal:  Biophys J       Date:  1984-11       Impact factor: 4.033

7.  Assembly of Aβ proceeds via monomeric nuclei.

Authors:  Frank A Ferrone
Journal:  J Mol Biol       Date:  2014-11-14       Impact factor: 5.469

8.  Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism.

Authors:  F A Ferrone; J Hofrichter; W A Eaton
Journal:  J Mol Biol       Date:  1985-06-25       Impact factor: 5.469

9.  A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.

Authors:  Samuel I A Cohen; Paolo Arosio; Jenny Presto; Firoz Roshan Kurudenkandy; Henrik Biverstal; Lisa Dolfe; Christopher Dunning; Xiaoting Yang; Birgitta Frohm; Michele Vendruscolo; Jan Johansson; Christopher M Dobson; André Fisahn; Tuomas P J Knowles; Sara Linse
Journal:  Nat Struct Mol Biol       Date:  2015-02-16       Impact factor: 15.369

10.  Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.

Authors:  Samuel I A Cohen; Sara Linse; Leila M Luheshi; Erik Hellstrand; Duncan A White; Luke Rajah; Daniel E Otzen; Michele Vendruscolo; Christopher M Dobson; Tuomas P J Knowles
Journal:  Proc Natl Acad Sci U S A       Date:  2013-05-23       Impact factor: 11.205
  10 in total
  1 in total

1.  In situ fibrillizing amyloid-beta 1-42 induces neurite degeneration and apoptosis of differentiated SH-SY5Y cells.

Authors:  Jekaterina Krishtal; Olga Bragina; Kristel Metsla; Peep Palumaa; Vello Tõugu
Journal:  PLoS One       Date:  2017-10-24       Impact factor: 3.240
  1 in total

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