Literature DB >> 27830791

The activities of amyloids from a structural perspective.

Roland Riek1, David S Eisenberg2,3.   

Abstract

The aggregation of proteins into structures known as amyloids is observed in many neurodegenerative diseases, including Alzheimer's disease. Amyloids are composed of pairs of tightly interacting, many stranded and repetitive intermolecular β-sheets, which form the cross-β-sheet structure. This structure enables amyloids to grow by recruitment of the same protein and its repetition can transform a weak biological activity into a potent one through cooperativity and avidity. Amyloids therefore have the potential to self-replicate and can adapt to the environment, yielding cell-to-cell transmissibility, prion infectivity and toxicity.

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Year:  2016        PMID: 27830791     DOI: 10.1038/nature20416

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  135 in total

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2.  Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils.

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Journal:  Nature       Date:  1997-02-27       Impact factor: 49.962

4.  Correlation of structural elements and infectivity of the HET-s prion.

Authors:  Christiane Ritter; Marie-Lise Maddelein; Ansgar B Siemer; Thorsten Lührs; Matthias Ernst; Beat H Meier; Sven J Saupe; Roland Riek
Journal:  Nature       Date:  2005-06-09       Impact factor: 49.962

5.  Multidimensional structure-activity relationship of a protein in its aggregated states.

Authors:  Lei Wang; David Schubert; Michael R Sawaya; David Eisenberg; Roland Riek
Journal:  Angew Chem Int Ed Engl       Date:  2010-05-25       Impact factor: 15.336

6.  Protein-only transmission of three yeast prion strains.

Authors:  Chih-Yen King; Ruben Diaz-Avalos
Journal:  Nature       Date:  2004-03-18       Impact factor: 49.962

7.  Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease.

Authors:  Marcin I Apostol; Michael R Sawaya; Duilio Cascio; David Eisenberg
Journal:  J Biol Chem       Date:  2010-08-04       Impact factor: 5.157

8.  Molecular mechanisms for protein-encoded inheritance.

Authors:  Jed J W Wiltzius; Meytal Landau; Rebecca Nelson; Michael R Sawaya; Marcin I Apostol; Lukasz Goldschmidt; Angela B Soriaga; Duilio Cascio; Kanagalaghatta Rajashankar; David Eisenberg
Journal:  Nat Struct Mol Biol       Date:  2009-08-16       Impact factor: 15.369

9.  Acquisition of drug resistance and dependence by prions.

Authors:  Anja M Oelschlegel; Charles Weissmann
Journal:  PLoS Pathog       Date:  2013-02-07       Impact factor: 6.823

10.  The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy.

Authors:  Ester Vázquez-Fernández; Matthijn R Vos; Pavel Afanasyev; Lino Cebey; Alejandro M Sevillano; Enric Vidal; Isaac Rosa; Ludovic Renault; Adriana Ramos; Peter J Peters; José Jesús Fernández; Marin van Heel; Howard S Young; Jesús R Requena; Holger Wille
Journal:  PLoS Pathog       Date:  2016-09-08       Impact factor: 6.823

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  122 in total

Review 1.  Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.

Authors:  Durga Dharmadana; Nicholas P Reynolds; Charlotte E Conn; Céline Valéry
Journal:  Interface Focus       Date:  2017-06-16       Impact factor: 3.906

2.  A hydrophobic low-complexity region regulates aggregation of the yeast pyruvate kinase Cdc19 into amyloid-like aggregates in vitro.

Authors:  Erica Grignaschi; Gea Cereghetti; Fulvio Grigolato; Marie R G Kopp; Stefano Caimi; Lenka Faltova; Shady Saad; Matthias Peter; Paolo Arosio
Journal:  J Biol Chem       Date:  2018-05-31       Impact factor: 5.157

3.  VLITL is a major cross-β-sheet signal for fibrinogen Aα-chain frameshift variants.

Authors:  Cyrille Garnier; Fatma Briki; Brigitte Nedelec; Patrick Le Pogamp; Ahmet Dogan; Nathalie Rioux-Leclercq; Renan Goude; Caroline Beugnet; Laurent Martin; Marc Delpech; Frank Bridoux; Gilles Grateau; Jean Doucet; Philippe Derreumaux; Sophie Valleix
Journal:  Blood       Date:  2017-10-31       Impact factor: 22.113

4.  Conformational Ensembles of the Wild-Type and S8C Aβ1-42 Dimers.

Authors:  Viet Hoang Man; Phuong H Nguyen; Philippe Derreumaux
Journal:  J Phys Chem B       Date:  2017-03-10       Impact factor: 2.991

5.  Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy.

Authors:  Yaowang Li; Chunyu Zhao; Feng Luo; Zhenying Liu; Xinrui Gui; Zhipu Luo; Xiang Zhang; Dan Li; Cong Liu; Xueming Li
Journal:  Cell Res       Date:  2018-07-31       Impact factor: 25.617

6.  Amyloid: From Starch to Finish.

Authors:  Hannah L Krystal; David A Ross; Adam P Mecca
Journal:  Biol Psychiatry       Date:  2020-05-01       Impact factor: 13.382

7.  Organizing biochemistry in space and time using prion-like self-assembly.

Authors:  Christopher M Jakobson; Daniel F Jarosz
Journal:  Curr Opin Syst Biol       Date:  2017-12-06

8.  Zinc-binding structure of a catalytic amyloid from solid-state NMR.

Authors:  Myungwoon Lee; Tuo Wang; Olga V Makhlynets; Yibing Wu; Nicholas F Polizzi; Haifan Wu; Pallavi M Gosavi; Jan Stöhr; Ivan V Korendovych; William F DeGrado; Mei Hong
Journal:  Proc Natl Acad Sci U S A       Date:  2017-05-31       Impact factor: 11.205

9.  Aggregation-phase diagrams of β2-microglobulin reveal temperature and salt effects on competitive formation of amyloids versus amorphous aggregates.

Authors:  Masayuki Adachi; Masahiro Noji; Masatomo So; Kenji Sasahara; József Kardos; Hironobu Naiki; Yuji Goto
Journal:  J Biol Chem       Date:  2018-08-03       Impact factor: 5.157

10.  Transmembrane Proteins: Amyloids Hidden in Plain Sight?

Authors:  Nicholas L Truex; James S Nowick
Journal:  Biochemistry       Date:  2017-08-30       Impact factor: 3.162

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