Potential involvement of copper and thiol-disulphide interchange in prion proteins' conformational conversion-Reference-Cited by-同舟云学术

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Potential involvement of copper and thiol-disulphide interchange in prion proteins' conformational conversion

Published:2002-09 Issue:3 Volume:59 Page:321-324
ISSN:0306-9877
Container-title:Medical Hypotheses
language:en
Short-container-title:Medical Hypotheses

Author:

Feughelman M,Willis B.K

Publisher

Elsevier BV

Subject

General Medicine

Reference22 articles.

1. The molecular basis of amyloidosis;Serpell;Cell. Mol. Life Sci.,1997

2. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform;James;Proc. Natl. Acad. Sci. USA,1997

3. Purification and properties of the cellular and scrapie hamster prion proteins;Turk;Eur. J. Biochem.,1988

4. Thiol-disulphide interchange a potential key to conformational change associated with amyloid fibril formation;Feughelman;J. Theor. Biol.,2000

5. Self-assembly of recombinant prion protein of 106 residues;Baskakov;Biochemistry,2000

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Structural Determinants in Prion Protein Folding and Stability;Journal of Molecular Biology;2014-11

2. Changing the solvent accessibility of the prion protein disulfide bond markedly influences its trafficking and effect on cell function;Biochemical Journal;2010-05-13

3. Copper-dependent degradation of recombinant ovine prion protein;FEBS Journal;2006-04-10

4. Selective prion protein binding to synaptic components is modulated by oxidative and nitrosative changes induced by copper(II) and peroxynitrite in cholinergic synaptosomes, unveiling a role for calcineurin B and thioredoxin;Journal of Neurochemistry;2003-11-21

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